Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system
Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorl...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Mokry, David Z. [verfasserIn] da Silva, Viviane C. H. [verfasserIn] Abrahão, Josielle [verfasserIn] Ramos, Carlos H. I. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Journal of plant biochemistry and biotechnology - Berlin : Springer, 1992, 26(2017), 4 vom: 05. Juni, Seite 478-487 |
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| Übergeordnetes Werk: |
volume:26 ; year:2017 ; number:4 ; day:05 ; month:06 ; pages:478-487 |
| Links: |
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| DOI / URN: |
10.1007/s13562-017-0409-7 |
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| Katalog-ID: |
SPR031804667 |
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| 100 | 1 | |a Mokry, David Z. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system |
| 264 | 1 | |c 2017 | |
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| 520 | |a Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. | ||
| 650 | 4 | |a Heat shock protein (HSP) |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Hsp101 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Molecular chaperone |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Protein folding |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Abiotic stress |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a da Silva, Viviane C. H. |e verfasserin |4 aut | |
| 700 | 1 | |a Abrahão, Josielle |e verfasserin |4 aut | |
| 700 | 1 | |a Ramos, Carlos H. I. |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Journal of plant biochemistry and biotechnology |d Berlin : Springer, 1992 |g 26(2017), 4 vom: 05. Juni, Seite 478-487 |w (DE-627)501417192 |w (DE-600)2206337-7 |x 0974-1275 |7 nnns |
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| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s13562-017-0409-7 |z lizenzpflichtig |3 Volltext |
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| 912 | |a GBV_ILN_2021 | ||
| 912 | |a GBV_ILN_2025 | ||
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| 912 | |a GBV_ILN_2031 | ||
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| 912 | |a GBV_ILN_2037 | ||
| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2039 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
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| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2065 | ||
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| 912 | |a GBV_ILN_2070 | ||
| 912 | |a GBV_ILN_2086 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2107 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
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| 912 | |a GBV_ILN_2118 | ||
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| 912 | |a GBV_ILN_4323 | ||
| 912 | |a GBV_ILN_4324 | ||
| 912 | |a GBV_ILN_4325 | ||
| 912 | |a GBV_ILN_4326 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
| 912 | |a GBV_ILN_4336 | ||
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10.1007/s13562-017-0409-7 doi (DE-627)SPR031804667 (SPR)s13562-017-0409-7-e DE-627 ger DE-627 rakwb eng 540 570 ASE Mokry, David Z. verfasserin aut Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. Heat shock protein (HSP) (dpeaa)DE-He213 Hsp101 (dpeaa)DE-He213 Molecular chaperone (dpeaa)DE-He213 Protein folding (dpeaa)DE-He213 Abiotic stress (dpeaa)DE-He213 da Silva, Viviane C. H. verfasserin aut Abrahão, Josielle verfasserin aut Ramos, Carlos H. I. verfasserin aut Enthalten in Journal of plant biochemistry and biotechnology Berlin : Springer, 1992 26(2017), 4 vom: 05. Juni, Seite 478-487 (DE-627)501417192 (DE-600)2206337-7 0974-1275 nnns volume:26 year:2017 number:4 day:05 month:06 pages:478-487 https://dx.doi.org/10.1007/s13562-017-0409-7 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_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 26 2017 4 05 06 478-487 |
| spelling |
10.1007/s13562-017-0409-7 doi (DE-627)SPR031804667 (SPR)s13562-017-0409-7-e DE-627 ger DE-627 rakwb eng 540 570 ASE Mokry, David Z. verfasserin aut Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. Heat shock protein (HSP) (dpeaa)DE-He213 Hsp101 (dpeaa)DE-He213 Molecular chaperone (dpeaa)DE-He213 Protein folding (dpeaa)DE-He213 Abiotic stress (dpeaa)DE-He213 da Silva, Viviane C. H. verfasserin aut Abrahão, Josielle verfasserin aut Ramos, Carlos H. I. verfasserin aut Enthalten in Journal of plant biochemistry and biotechnology Berlin : Springer, 1992 26(2017), 4 vom: 05. Juni, Seite 478-487 (DE-627)501417192 (DE-600)2206337-7 0974-1275 nnns volume:26 year:2017 number:4 day:05 month:06 pages:478-487 https://dx.doi.org/10.1007/s13562-017-0409-7 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_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 26 2017 4 05 06 478-487 |
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10.1007/s13562-017-0409-7 doi (DE-627)SPR031804667 (SPR)s13562-017-0409-7-e DE-627 ger DE-627 rakwb eng 540 570 ASE Mokry, David Z. verfasserin aut Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. Heat shock protein (HSP) (dpeaa)DE-He213 Hsp101 (dpeaa)DE-He213 Molecular chaperone (dpeaa)DE-He213 Protein folding (dpeaa)DE-He213 Abiotic stress (dpeaa)DE-He213 da Silva, Viviane C. H. verfasserin aut Abrahão, Josielle verfasserin aut Ramos, Carlos H. I. verfasserin aut Enthalten in Journal of plant biochemistry and biotechnology Berlin : Springer, 1992 26(2017), 4 vom: 05. Juni, Seite 478-487 (DE-627)501417192 (DE-600)2206337-7 0974-1275 nnns volume:26 year:2017 number:4 day:05 month:06 pages:478-487 https://dx.doi.org/10.1007/s13562-017-0409-7 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_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 26 2017 4 05 06 478-487 |
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10.1007/s13562-017-0409-7 doi (DE-627)SPR031804667 (SPR)s13562-017-0409-7-e DE-627 ger DE-627 rakwb eng 540 570 ASE Mokry, David Z. verfasserin aut Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. Heat shock protein (HSP) (dpeaa)DE-He213 Hsp101 (dpeaa)DE-He213 Molecular chaperone (dpeaa)DE-He213 Protein folding (dpeaa)DE-He213 Abiotic stress (dpeaa)DE-He213 da Silva, Viviane C. H. verfasserin aut Abrahão, Josielle verfasserin aut Ramos, Carlos H. I. verfasserin aut Enthalten in Journal of plant biochemistry and biotechnology Berlin : Springer, 1992 26(2017), 4 vom: 05. Juni, Seite 478-487 (DE-627)501417192 (DE-600)2206337-7 0974-1275 nnns volume:26 year:2017 number:4 day:05 month:06 pages:478-487 https://dx.doi.org/10.1007/s13562-017-0409-7 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_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 26 2017 4 05 06 478-487 |
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10.1007/s13562-017-0409-7 doi (DE-627)SPR031804667 (SPR)s13562-017-0409-7-e DE-627 ger DE-627 rakwb eng 540 570 ASE Mokry, David Z. verfasserin aut Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. Heat shock protein (HSP) (dpeaa)DE-He213 Hsp101 (dpeaa)DE-He213 Molecular chaperone (dpeaa)DE-He213 Protein folding (dpeaa)DE-He213 Abiotic stress (dpeaa)DE-He213 da Silva, Viviane C. H. verfasserin aut Abrahão, Josielle verfasserin aut Ramos, Carlos H. I. verfasserin aut Enthalten in Journal of plant biochemistry and biotechnology Berlin : Springer, 1992 26(2017), 4 vom: 05. Juni, Seite 478-487 (DE-627)501417192 (DE-600)2206337-7 0974-1275 nnns volume:26 year:2017 number:4 day:05 month:06 pages:478-487 https://dx.doi.org/10.1007/s13562-017-0409-7 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_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 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_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_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 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_2116 GBV_ILN_2118 GBV_ILN_2119 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_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_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 26 2017 4 05 06 478-487 |
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Enthalten in Journal of plant biochemistry and biotechnology 26(2017), 4 vom: 05. Juni, Seite 478-487 volume:26 year:2017 number:4 day:05 month:06 pages:478-487 |
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Heat shock protein (HSP) Hsp101 Molecular chaperone Protein folding Abiotic stress |
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Journal of plant biochemistry and biotechnology |
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Mokry, David Z. @@aut@@ da Silva, Viviane C. H. @@aut@@ Abrahão, Josielle @@aut@@ Ramos, Carlos H. I. @@aut@@ |
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Mokry, David Z. |
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Mokry, David Z. ddc 540 misc Heat shock protein (HSP) misc Hsp101 misc Molecular chaperone misc Protein folding misc Abiotic stress Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system |
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540 570 ASE Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system Heat shock protein (HSP) (dpeaa)DE-He213 Hsp101 (dpeaa)DE-He213 Molecular chaperone (dpeaa)DE-He213 Protein folding (dpeaa)DE-He213 Abiotic stress (dpeaa)DE-He213 |
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ddc 540 misc Heat shock protein (HSP) misc Hsp101 misc Molecular chaperone misc Protein folding misc Abiotic stress |
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ddc 540 misc Heat shock protein (HSP) misc Hsp101 misc Molecular chaperone misc Protein folding misc Abiotic stress |
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Journal of plant biochemistry and biotechnology |
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Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system |
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Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system |
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Mokry, David Z. |
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Journal of plant biochemistry and biotechnology |
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Mokry, David Z. da Silva, Viviane C. H. Abrahão, Josielle Ramos, Carlos H. I. |
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characterization of the hsp100 disaggregase from sugarcane (shsp101) for chaperone like activity in a yeast system |
| title_auth |
Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system |
| abstract |
Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. |
| abstractGer |
Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. |
| abstract_unstemmed |
Abstract The Hsp104/ClpB protein subfamily is unique in its ability to reactivate protein aggregates, which are implicated in several human and animal diseases. However, when compared to the unicellular yeast Hsp104 and bacterial ClpB disaggregases, the multicellular plant ortholog (Hsp101) is poorly studied. Here, we present a functional characterization of the Hsp101 (SHsp101) from the economically and agriculturally important sugarcane cultivar. Like Hsp104, SHsp101 has in vitro ATP/ATPγS dependent aggregate reactivation activity, confers induced thermotolerance in yeast and its ATPase activity is sensitive to guanidinium chloride. However, SHsp101 has distinct properties not previously reported for Hsp104, including higher ATPase activity at elevated temperatures and ATP independent intrinsic chaperone activity. Hence, SHsp101 has overlapping and distinct features from Hsp104. |
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4 |
| title_short |
Characterization of the Hsp100 disaggregase from sugarcane (SHsp101) for chaperone like activity in a yeast system |
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https://dx.doi.org/10.1007/s13562-017-0409-7 |
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| author2 |
da Silva, Viviane C. H. Abrahão, Josielle Ramos, Carlos H. I. |
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da Silva, Viviane C. H. Abrahão, Josielle Ramos, Carlos H. I. |
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| doi_str |
10.1007/s13562-017-0409-7 |
| up_date |
2024-07-04T01:18:55.580Z |
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| score |
7.4005327 |