Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis
Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the l...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Herrero, Joaquín [verfasserIn] Fernández-Pérez, Francisco [verfasserIn] Yebra, Tatiana [verfasserIn] Novo-Uzal, Esther [verfasserIn] Pomar, Federico [verfasserIn] Pedreño, Mª Ángeles [verfasserIn] Cuello, Juan [verfasserIn] Guéra, Alfredo [verfasserIn] Esteban-Carrasco, Alberto [verfasserIn] Zapata, José Miguel [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Planta - Berlin : Springer, 1925, 237(2013), 6 vom: 19. März, Seite 1599-1612 |
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| Übergeordnetes Werk: |
volume:237 ; year:2013 ; number:6 ; day:19 ; month:03 ; pages:1599-1612 |
| Links: |
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| DOI / URN: |
10.1007/s00425-013-1865-5 |
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| Katalog-ID: |
SPR005666848 |
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| 100 | 1 | |a Herrero, Joaquín |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis |
| 264 | 1 | |c 2013 | |
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| 337 | |a Computermedien |b c |2 rdamedia | ||
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| 520 | |a Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. | ||
| 650 | 4 | |a AtPrx72 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Bioinformatics |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Chlorophyll |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a fluorescence |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Histochemistry |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Lignification |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Peroxidase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Xylem vessels |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a ZePrx |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Fernández-Pérez, Francisco |e verfasserin |4 aut | |
| 700 | 1 | |a Yebra, Tatiana |e verfasserin |4 aut | |
| 700 | 1 | |a Novo-Uzal, Esther |e verfasserin |4 aut | |
| 700 | 1 | |a Pomar, Federico |e verfasserin |4 aut | |
| 700 | 1 | |a Pedreño, Mª Ángeles |e verfasserin |4 aut | |
| 700 | 1 | |a Cuello, Juan |e verfasserin |4 aut | |
| 700 | 1 | |a Guéra, Alfredo |e verfasserin |4 aut | |
| 700 | 1 | |a Esteban-Carrasco, Alberto |e verfasserin |4 aut | |
| 700 | 1 | |a Zapata, José Miguel |e verfasserin |4 aut | |
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| 773 | 1 | 8 | |g volume:237 |g year:2013 |g number:6 |g day:19 |g month:03 |g pages:1599-1612 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1007/s00425-013-1865-5 |z lizenzpflichtig |3 Volltext |
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| 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 | ||
| 912 | |a GBV_ILN_2111 | ||
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| 912 | |a GBV_ILN_2116 | ||
| 912 | |a GBV_ILN_2118 | ||
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10.1007/s00425-013-1865-5 doi (DE-627)SPR005666848 (SPR)s00425-013-1865-5-e DE-627 ger DE-627 rakwb eng 580 ASE 42.38 bkl Herrero, Joaquín verfasserin aut Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. AtPrx72 (dpeaa)DE-He213 Bioinformatics (dpeaa)DE-He213 Chlorophyll (dpeaa)DE-He213 fluorescence (dpeaa)DE-He213 Histochemistry (dpeaa)DE-He213 Lignification (dpeaa)DE-He213 Peroxidase (dpeaa)DE-He213 Xylem vessels (dpeaa)DE-He213 ZePrx (dpeaa)DE-He213 Fernández-Pérez, Francisco verfasserin aut Yebra, Tatiana verfasserin aut Novo-Uzal, Esther verfasserin aut Pomar, Federico verfasserin aut Pedreño, Mª Ángeles verfasserin aut Cuello, Juan verfasserin aut Guéra, Alfredo verfasserin aut Esteban-Carrasco, Alberto verfasserin aut Zapata, José Miguel verfasserin aut Enthalten in Planta Berlin : Springer, 1925 237(2013), 6 vom: 19. März, Seite 1599-1612 (DE-627)254639100 (DE-600)1463030-8 1432-2048 nnns volume:237 year:2013 number:6 day:19 month:03 pages:1599-1612 https://dx.doi.org/10.1007/s00425-013-1865-5 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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 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_2018 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_2946 GBV_ILN_2949 GBV_ILN_2951 GBV_ILN_4012 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_4346 GBV_ILN_4393 GBV_ILN_4700 42.38 ASE AR 237 2013 6 19 03 1599-1612 |
| spelling |
10.1007/s00425-013-1865-5 doi (DE-627)SPR005666848 (SPR)s00425-013-1865-5-e DE-627 ger DE-627 rakwb eng 580 ASE 42.38 bkl Herrero, Joaquín verfasserin aut Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. AtPrx72 (dpeaa)DE-He213 Bioinformatics (dpeaa)DE-He213 Chlorophyll (dpeaa)DE-He213 fluorescence (dpeaa)DE-He213 Histochemistry (dpeaa)DE-He213 Lignification (dpeaa)DE-He213 Peroxidase (dpeaa)DE-He213 Xylem vessels (dpeaa)DE-He213 ZePrx (dpeaa)DE-He213 Fernández-Pérez, Francisco verfasserin aut Yebra, Tatiana verfasserin aut Novo-Uzal, Esther verfasserin aut Pomar, Federico verfasserin aut Pedreño, Mª Ángeles verfasserin aut Cuello, Juan verfasserin aut Guéra, Alfredo verfasserin aut Esteban-Carrasco, Alberto verfasserin aut Zapata, José Miguel verfasserin aut Enthalten in Planta Berlin : Springer, 1925 237(2013), 6 vom: 19. März, Seite 1599-1612 (DE-627)254639100 (DE-600)1463030-8 1432-2048 nnns volume:237 year:2013 number:6 day:19 month:03 pages:1599-1612 https://dx.doi.org/10.1007/s00425-013-1865-5 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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 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_2018 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_2946 GBV_ILN_2949 GBV_ILN_2951 GBV_ILN_4012 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_4346 GBV_ILN_4393 GBV_ILN_4700 42.38 ASE AR 237 2013 6 19 03 1599-1612 |
| allfields_unstemmed |
10.1007/s00425-013-1865-5 doi (DE-627)SPR005666848 (SPR)s00425-013-1865-5-e DE-627 ger DE-627 rakwb eng 580 ASE 42.38 bkl Herrero, Joaquín verfasserin aut Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. AtPrx72 (dpeaa)DE-He213 Bioinformatics (dpeaa)DE-He213 Chlorophyll (dpeaa)DE-He213 fluorescence (dpeaa)DE-He213 Histochemistry (dpeaa)DE-He213 Lignification (dpeaa)DE-He213 Peroxidase (dpeaa)DE-He213 Xylem vessels (dpeaa)DE-He213 ZePrx (dpeaa)DE-He213 Fernández-Pérez, Francisco verfasserin aut Yebra, Tatiana verfasserin aut Novo-Uzal, Esther verfasserin aut Pomar, Federico verfasserin aut Pedreño, Mª Ángeles verfasserin aut Cuello, Juan verfasserin aut Guéra, Alfredo verfasserin aut Esteban-Carrasco, Alberto verfasserin aut Zapata, José Miguel verfasserin aut Enthalten in Planta Berlin : Springer, 1925 237(2013), 6 vom: 19. März, Seite 1599-1612 (DE-627)254639100 (DE-600)1463030-8 1432-2048 nnns volume:237 year:2013 number:6 day:19 month:03 pages:1599-1612 https://dx.doi.org/10.1007/s00425-013-1865-5 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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 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_2018 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_2946 GBV_ILN_2949 GBV_ILN_2951 GBV_ILN_4012 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_4346 GBV_ILN_4393 GBV_ILN_4700 42.38 ASE AR 237 2013 6 19 03 1599-1612 |
| allfieldsGer |
10.1007/s00425-013-1865-5 doi (DE-627)SPR005666848 (SPR)s00425-013-1865-5-e DE-627 ger DE-627 rakwb eng 580 ASE 42.38 bkl Herrero, Joaquín verfasserin aut Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. AtPrx72 (dpeaa)DE-He213 Bioinformatics (dpeaa)DE-He213 Chlorophyll (dpeaa)DE-He213 fluorescence (dpeaa)DE-He213 Histochemistry (dpeaa)DE-He213 Lignification (dpeaa)DE-He213 Peroxidase (dpeaa)DE-He213 Xylem vessels (dpeaa)DE-He213 ZePrx (dpeaa)DE-He213 Fernández-Pérez, Francisco verfasserin aut Yebra, Tatiana verfasserin aut Novo-Uzal, Esther verfasserin aut Pomar, Federico verfasserin aut Pedreño, Mª Ángeles verfasserin aut Cuello, Juan verfasserin aut Guéra, Alfredo verfasserin aut Esteban-Carrasco, Alberto verfasserin aut Zapata, José Miguel verfasserin aut Enthalten in Planta Berlin : Springer, 1925 237(2013), 6 vom: 19. März, Seite 1599-1612 (DE-627)254639100 (DE-600)1463030-8 1432-2048 nnns volume:237 year:2013 number:6 day:19 month:03 pages:1599-1612 https://dx.doi.org/10.1007/s00425-013-1865-5 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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 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_2018 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_2946 GBV_ILN_2949 GBV_ILN_2951 GBV_ILN_4012 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_4346 GBV_ILN_4393 GBV_ILN_4700 42.38 ASE AR 237 2013 6 19 03 1599-1612 |
| allfieldsSound |
10.1007/s00425-013-1865-5 doi (DE-627)SPR005666848 (SPR)s00425-013-1865-5-e DE-627 ger DE-627 rakwb eng 580 ASE 42.38 bkl Herrero, Joaquín verfasserin aut Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis 2013 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. AtPrx72 (dpeaa)DE-He213 Bioinformatics (dpeaa)DE-He213 Chlorophyll (dpeaa)DE-He213 fluorescence (dpeaa)DE-He213 Histochemistry (dpeaa)DE-He213 Lignification (dpeaa)DE-He213 Peroxidase (dpeaa)DE-He213 Xylem vessels (dpeaa)DE-He213 ZePrx (dpeaa)DE-He213 Fernández-Pérez, Francisco verfasserin aut Yebra, Tatiana verfasserin aut Novo-Uzal, Esther verfasserin aut Pomar, Federico verfasserin aut Pedreño, Mª Ángeles verfasserin aut Cuello, Juan verfasserin aut Guéra, Alfredo verfasserin aut Esteban-Carrasco, Alberto verfasserin aut Zapata, José Miguel verfasserin aut Enthalten in Planta Berlin : Springer, 1925 237(2013), 6 vom: 19. März, Seite 1599-1612 (DE-627)254639100 (DE-600)1463030-8 1432-2048 nnns volume:237 year:2013 number:6 day:19 month:03 pages:1599-1612 https://dx.doi.org/10.1007/s00425-013-1865-5 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_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 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_2018 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_2946 GBV_ILN_2949 GBV_ILN_2951 GBV_ILN_4012 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_4346 GBV_ILN_4393 GBV_ILN_4700 42.38 ASE AR 237 2013 6 19 03 1599-1612 |
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AtPrx72 Bioinformatics Chlorophyll fluorescence Histochemistry Lignification Peroxidase Xylem vessels ZePrx |
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Herrero, Joaquín @@aut@@ Fernández-Pérez, Francisco @@aut@@ Yebra, Tatiana @@aut@@ Novo-Uzal, Esther @@aut@@ Pomar, Federico @@aut@@ Pedreño, Mª Ángeles @@aut@@ Cuello, Juan @@aut@@ Guéra, Alfredo @@aut@@ Esteban-Carrasco, Alberto @@aut@@ Zapata, José Miguel @@aut@@ |
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| author |
Herrero, Joaquín |
| spellingShingle |
Herrero, Joaquín ddc 580 bkl 42.38 misc AtPrx72 misc Bioinformatics misc Chlorophyll misc fluorescence misc Histochemistry misc Lignification misc Peroxidase misc Xylem vessels misc ZePrx Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis |
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Herrero, Joaquín |
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1432-2048 |
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580 ASE 42.38 bkl Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis AtPrx72 (dpeaa)DE-He213 Bioinformatics (dpeaa)DE-He213 Chlorophyll (dpeaa)DE-He213 fluorescence (dpeaa)DE-He213 Histochemistry (dpeaa)DE-He213 Lignification (dpeaa)DE-He213 Peroxidase (dpeaa)DE-He213 Xylem vessels (dpeaa)DE-He213 ZePrx (dpeaa)DE-He213 |
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ddc 580 bkl 42.38 misc AtPrx72 misc Bioinformatics misc Chlorophyll misc fluorescence misc Histochemistry misc Lignification misc Peroxidase misc Xylem vessels misc ZePrx |
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ddc 580 bkl 42.38 misc AtPrx72 misc Bioinformatics misc Chlorophyll misc fluorescence misc Histochemistry misc Lignification misc Peroxidase misc Xylem vessels misc ZePrx |
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ddc 580 bkl 42.38 misc AtPrx72 misc Bioinformatics misc Chlorophyll misc fluorescence misc Histochemistry misc Lignification misc Peroxidase misc Xylem vessels misc ZePrx |
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Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis |
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(DE-627)SPR005666848 (SPR)s00425-013-1865-5-e |
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Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis |
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Herrero, Joaquín |
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Herrero, Joaquín Fernández-Pérez, Francisco Yebra, Tatiana Novo-Uzal, Esther Pomar, Federico Pedreño, Mª Ángeles Cuello, Juan Guéra, Alfredo Esteban-Carrasco, Alberto Zapata, José Miguel |
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Herrero, Joaquín |
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10.1007/s00425-013-1865-5 |
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verfasserin |
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bioinformatic and functional characterization of the basic peroxidase 72 from arabidopsis thaliana involved in lignin biosynthesis |
| title_auth |
Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis |
| abstract |
Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. |
| abstractGer |
Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. |
| abstract_unstemmed |
Abstract Lignins result from the oxidative polymerization of three hydroxycinnamyl (p-coumaryl, coniferyl, and sinapyl) alcohols in a reaction mediated by peroxidases. The most important of these is the cationic peroxidase from Zinnia elegans (ZePrx), an enzyme considered to be responsible for the last step of lignification in this plant. Bibliographical evidence indicates that the arabidopsis peroxidase 72 (AtPrx72), which is homolog to ZePrx, could have an important role in lignification. For this reason, we performed a bioinformatic, histochemical, photosynthetic, and phenotypical and lignin composition analysis of an arabidopsis knock-out mutant of AtPrx72 with the aim of characterizing the effects that occurred due to the absence of expression of this peroxidase from the aspects of plant physiology such as vascular development, lignification, and photosynthesis. In silico analyses indicated a high homology between AtPrx72 and ZePrx, cell wall localization and probably optimal levels of translation of AtPrx72. The histochemical study revealed a low content in syringyl units and a decrease in the amount of lignin in the atprx72 mutant plants compared to WT. The atprx72 mutant plants grew more slowly than WT plants, with both smaller rosette and principal stem, and with fewer branches and siliques than the WT plants. Lastly, chlorophyll a fluorescence revealed a significant decrease in $ Φ_{PSII} $ and qL in atprx72 mutant plants that could be related to changes in carbon partitioning and/or utilization of redox equivalents in arabidopsis metabolism. The results suggest an important role of AtPrx72 in lignin biosynthesis. In addition, knock-out plants were able to respond and adapt to an insufficiency of lignification. |
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6 |
| title_short |
Bioinformatic and functional characterization of the basic peroxidase 72 from Arabidopsis thaliana involved in lignin biosynthesis |
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https://dx.doi.org/10.1007/s00425-013-1865-5 |
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Fernández-Pérez, Francisco Yebra, Tatiana Novo-Uzal, Esther Pomar, Federico Pedreño, Mª Ángeles Cuello, Juan Guéra, Alfredo Esteban-Carrasco, Alberto Zapata, José Miguel |
| author2Str |
Fernández-Pérez, Francisco Yebra, Tatiana Novo-Uzal, Esther Pomar, Federico Pedreño, Mª Ángeles Cuello, Juan Guéra, Alfredo Esteban-Carrasco, Alberto Zapata, José Miguel |
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| doi_str |
10.1007/s00425-013-1865-5 |
| up_date |
2024-07-03T17:53:59.924Z |
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| score |
7.4018145 |