Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression
Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidenc...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Kim, Ju Hee [verfasserIn] Lim, Sung Don [verfasserIn] Jang, Cheol Seong [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2020 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Plant molecular biology - Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981, 103(2020), 3 vom: 21. März, Seite 235-252 |
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| Übergeordnetes Werk: |
volume:103 ; year:2020 ; number:3 ; day:21 ; month:03 ; pages:235-252 |
| Links: |
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| DOI / URN: |
10.1007/s11103-020-00989-x |
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| Katalog-ID: |
SPR039706001 |
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| 245 | 1 | 0 | |a Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression |
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| 520 | |a Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. | ||
| 520 | |a Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. | ||
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| 700 | 1 | |a Lim, Sung Don |e verfasserin |4 aut | |
| 700 | 1 | |a Jang, Cheol Seong |e verfasserin |4 aut | |
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10.1007/s11103-020-00989-x doi (DE-627)SPR039706001 (SPR)s11103-020-00989-x-e DE-627 ger DE-627 rakwb eng 580 ASE 42.43 bkl 48.58 bkl Kim, Ju Hee verfasserin aut Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. 26S proteasome (dpeaa)DE-He213 Environmental stress (dpeaa)DE-He213 RING E3 ligase (dpeaa)DE-He213 Protein degradation (dpeaa)DE-He213 Rice (dpeaa)DE-He213 Ubiquitination (dpeaa)DE-He213 Lim, Sung Don verfasserin aut Jang, Cheol Seong verfasserin aut Enthalten in Plant molecular biology Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981 103(2020), 3 vom: 21. März, Seite 235-252 (DE-627)269758658 (DE-600)1475712-6 1573-5028 nnns volume:103 year:2020 number:3 day:21 month:03 pages:235-252 https://dx.doi.org/10.1007/s11103-020-00989-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.43 ASE 48.58 ASE AR 103 2020 3 21 03 235-252 |
| spelling |
10.1007/s11103-020-00989-x doi (DE-627)SPR039706001 (SPR)s11103-020-00989-x-e DE-627 ger DE-627 rakwb eng 580 ASE 42.43 bkl 48.58 bkl Kim, Ju Hee verfasserin aut Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. 26S proteasome (dpeaa)DE-He213 Environmental stress (dpeaa)DE-He213 RING E3 ligase (dpeaa)DE-He213 Protein degradation (dpeaa)DE-He213 Rice (dpeaa)DE-He213 Ubiquitination (dpeaa)DE-He213 Lim, Sung Don verfasserin aut Jang, Cheol Seong verfasserin aut Enthalten in Plant molecular biology Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981 103(2020), 3 vom: 21. März, Seite 235-252 (DE-627)269758658 (DE-600)1475712-6 1573-5028 nnns volume:103 year:2020 number:3 day:21 month:03 pages:235-252 https://dx.doi.org/10.1007/s11103-020-00989-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.43 ASE 48.58 ASE AR 103 2020 3 21 03 235-252 |
| allfields_unstemmed |
10.1007/s11103-020-00989-x doi (DE-627)SPR039706001 (SPR)s11103-020-00989-x-e DE-627 ger DE-627 rakwb eng 580 ASE 42.43 bkl 48.58 bkl Kim, Ju Hee verfasserin aut Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. 26S proteasome (dpeaa)DE-He213 Environmental stress (dpeaa)DE-He213 RING E3 ligase (dpeaa)DE-He213 Protein degradation (dpeaa)DE-He213 Rice (dpeaa)DE-He213 Ubiquitination (dpeaa)DE-He213 Lim, Sung Don verfasserin aut Jang, Cheol Seong verfasserin aut Enthalten in Plant molecular biology Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981 103(2020), 3 vom: 21. März, Seite 235-252 (DE-627)269758658 (DE-600)1475712-6 1573-5028 nnns volume:103 year:2020 number:3 day:21 month:03 pages:235-252 https://dx.doi.org/10.1007/s11103-020-00989-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.43 ASE 48.58 ASE AR 103 2020 3 21 03 235-252 |
| allfieldsGer |
10.1007/s11103-020-00989-x doi (DE-627)SPR039706001 (SPR)s11103-020-00989-x-e DE-627 ger DE-627 rakwb eng 580 ASE 42.43 bkl 48.58 bkl Kim, Ju Hee verfasserin aut Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. 26S proteasome (dpeaa)DE-He213 Environmental stress (dpeaa)DE-He213 RING E3 ligase (dpeaa)DE-He213 Protein degradation (dpeaa)DE-He213 Rice (dpeaa)DE-He213 Ubiquitination (dpeaa)DE-He213 Lim, Sung Don verfasserin aut Jang, Cheol Seong verfasserin aut Enthalten in Plant molecular biology Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981 103(2020), 3 vom: 21. März, Seite 235-252 (DE-627)269758658 (DE-600)1475712-6 1573-5028 nnns volume:103 year:2020 number:3 day:21 month:03 pages:235-252 https://dx.doi.org/10.1007/s11103-020-00989-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.43 ASE 48.58 ASE AR 103 2020 3 21 03 235-252 |
| allfieldsSound |
10.1007/s11103-020-00989-x doi (DE-627)SPR039706001 (SPR)s11103-020-00989-x-e DE-627 ger DE-627 rakwb eng 580 ASE 42.43 bkl 48.58 bkl Kim, Ju Hee verfasserin aut Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. 26S proteasome (dpeaa)DE-He213 Environmental stress (dpeaa)DE-He213 RING E3 ligase (dpeaa)DE-He213 Protein degradation (dpeaa)DE-He213 Rice (dpeaa)DE-He213 Ubiquitination (dpeaa)DE-He213 Lim, Sung Don verfasserin aut Jang, Cheol Seong verfasserin aut Enthalten in Plant molecular biology Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981 103(2020), 3 vom: 21. März, Seite 235-252 (DE-627)269758658 (DE-600)1475712-6 1573-5028 nnns volume:103 year:2020 number:3 day:21 month:03 pages:235-252 https://dx.doi.org/10.1007/s11103-020-00989-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 42.43 ASE 48.58 ASE AR 103 2020 3 21 03 235-252 |
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English |
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Enthalten in Plant molecular biology 103(2020), 3 vom: 21. März, Seite 235-252 volume:103 year:2020 number:3 day:21 month:03 pages:235-252 |
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Enthalten in Plant molecular biology 103(2020), 3 vom: 21. März, Seite 235-252 volume:103 year:2020 number:3 day:21 month:03 pages:235-252 |
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26S proteasome Environmental stress RING E3 ligase Protein degradation Rice Ubiquitination |
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Plant molecular biology |
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Kim, Ju Hee @@aut@@ Lim, Sung Don @@aut@@ Jang, Cheol Seong @@aut@@ |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR039706001</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519082145.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s11103-020-00989-x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR039706001</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s11103-020-00989-x-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">580</subfield><subfield code="q">ASE</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">42.43</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">48.58</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Kim, Ju Hee</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">26S proteasome</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Environmental stress</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">RING E3 ligase</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein degradation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Rice</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Ubiquitination</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Lim, Sung Don</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Jang, Cheol Seong</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Plant molecular biology</subfield><subfield code="d">Dordrecht [u.a.] : Springer Science + Business Media B.V, 1981</subfield><subfield code="g">103(2020), 3 vom: 21. 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|
| author |
Kim, Ju Hee |
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Kim, Ju Hee ddc 580 bkl 42.43 bkl 48.58 misc 26S proteasome misc Environmental stress misc RING E3 ligase misc Protein degradation misc Rice misc Ubiquitination Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression |
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580 ASE 42.43 bkl 48.58 bkl Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression 26S proteasome (dpeaa)DE-He213 Environmental stress (dpeaa)DE-He213 RING E3 ligase (dpeaa)DE-He213 Protein degradation (dpeaa)DE-He213 Rice (dpeaa)DE-He213 Ubiquitination (dpeaa)DE-He213 |
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ddc 580 bkl 42.43 bkl 48.58 misc 26S proteasome misc Environmental stress misc RING E3 ligase misc Protein degradation misc Rice misc Ubiquitination |
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ddc 580 bkl 42.43 bkl 48.58 misc 26S proteasome misc Environmental stress misc RING E3 ligase misc Protein degradation misc Rice misc Ubiquitination |
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ddc 580 bkl 42.43 bkl 48.58 misc 26S proteasome misc Environmental stress misc RING E3 ligase misc Protein degradation misc Rice misc Ubiquitination |
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Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression |
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| title_full |
Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression |
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Kim, Ju Hee |
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Plant molecular biology |
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Kim, Ju Hee Lim, Sung Don Jang, Cheol Seong |
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oryza sativa drought-, heat-, and salt-induced ring finger protein 1 (osdhsrp1) negatively regulates abiotic stress-responsive gene expression |
| title_auth |
Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression |
| abstract |
Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. |
| abstractGer |
Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. |
| abstract_unstemmed |
Abstract Plants are sessile and unable to avoid environmental stresses, such as drought, high temperature, and high salinity, which often limit the overall plant growth. Plants have evolved many complex mechanisms to survive these abiotic stresses via post-translational modifications. Recent evidence suggests that ubiquitination plays a crucial role in regulating abiotic stress responses in plants by regulating their substrate proteins. Here, we reported the molecular function of a RING finger E3 ligase, Oryza sativa Drought, Heat and Salt-induced RING finger protein 1 (OsDHSRP1), involved in regulating plant abiotic stress tolerance via the Ub/26S proteasome system. The OsDHSRP1 gene transcripts were highly expressed under various abiotic stresses such as NaCl, drought, and heat and the phytohormone abscisic acid (ABA). In addition, in vitro ubiquitination assays demonstrated that the OsDHSRP1 protein possesses a RING-H2 type domain that confers ligase functionality. The results of yeast two-hybrid (Y2H), in vitro pull-down, and bimolecular fluorescence complementation assays support that OsDHSRP1 is able to regulate two substrates, O. sativa glyoxalase (OsGLYI-11.2) and O. sativa abiotic stress-induced cysteine proteinase 1 (OsACP1). We further confirmed that these two substrate proteins were ubiquitinated by OsDHSRP1 E3 ligase and caused protein degradation via the Ub/26S proteasome system. The Arabidopsis plants overexpressing OsDHSRP1 exhibited hypersensitivity to drought, heat, and NaCl stress and a decrease in their germination rates and root lengths compared to the control plants because the degradation of the OsGLYI-11.2 protein maintained lower glyoxalase levels, which increased the methylglyoxal amount in transgenic Arabidopsis plants. However, the OsDHSRP1-overexpressing plants showed no significant difference when treated with ABA. Our finding supports the hypothesis that the OsDHSRP1 E3 ligase acts as a negative regulator, and the degradation of its substrate proteins via ubiquitination plays important roles in regulating various abiotic stress responses via an ABA-independent pathway. Key message OsDHSRP1 is an E3 ligase that acts as a negative regulator in the plant response to various abiotic stresses via the 26S proteasomal system regulation of substrate proteins, which it provides important information for adaptation and regulation under abiotic stress in plant cells. |
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Oryza sativa drought-, heat-, and salt-induced RING finger protein 1 (OsDHSRP1) negatively regulates abiotic stress-responsive gene expression |
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| score |
7.4006968 |