Cytochrome b 5 Is an Obligate Electron Shuttle Protein for Syringyl Lignin Biosynthesis in Arabidopsis
Abstract
In monolignol biosynthetic pathway, three cytochrome P450-catalzyed reactions essentially determine the structural characteristics of lignin precursors. Among them, ferulate 5-hydroxylase (F5H) is specifically responsible for syringyl (S) lignin subunit formation. NADPH Cytochrome P450 oxidoreductase (CPR) is commonly regarded as the electron carrier for the P450-catalyzed reactions in monolignol biosynthesis. Here we show that cytochrome b5 isoform D (CB5D) is an indispensable electron shuttle intermediate specific for S-lignin biosynthesis. Arabidopsis CB5D localizes on endoplasmic reticulum membrane and physically associates with monolignol P450 enzymes. Disrupting CB5D in Arabidopsis results in >60% reduction of S-lignin subunits but no impairment on G-lignin formation compared to the wild type, which sharply contrasts to the impairment of both G- and S-lignin synthesis after disruption of ATR2, the Arabidopsis CPR. The defect of S-lignin synthesis in cb5d mutants is rescued with expression of the gene encoding CB5D but not with the CB5D mutant variants devoid of its electron shuttle property. While disruption of ATR2 suppresses both C4H and F5H catalytic activities, elimination of CB5D specifically depletes the latter's activity. Our study demonstrates that CB5D functions as an obligate electron shuttle intermediate specifically augmenting F5H-catalyzed reaction thus controlling S-lignin biosynthesis.
- Authors:
-
[1];
[2];
[1];
[3];
[1];
[1]
- Biology Department, Brookhaven National Laboratory, Upton, New York 11973
- Biology Department, Brookhaven National Laboratory, Upton, New York 11973, Guangdong Provincial Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou 510650, China
- Biology Department, Brookhaven National Laboratory, Upton, New York 11973, College of Chemistry and Chemical Engineering, Chongqing University of Technology, Chongqing 400054, People’s Republic of China
- Publication Date:
- Research Org.:
- Brookhaven National Laboratory (BNL), Upton, NY (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); China Scholarship Council (CSC)
- OSTI Identifier:
- 1573095
- Alternate Identifier(s):
- OSTI ID: 1515153
- Report Number(s):
- BNL-211687-2019-JAAM
Journal ID: ISSN 1040-4651; /plantcell/31/6/1344.atom
- Grant/Contract Number:
- SC0012704
- Resource Type:
- Published Article
- Journal Name:
- The Plant Cell
- Additional Journal Information:
- Journal Name: The Plant Cell Journal Volume: 31 Journal Issue: 6; Journal ID: ISSN 1040-4651
- Publisher:
- Oxford University Press
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Gou, Mingyue, Yang, Xiaoman, Zhao, Yunjun, Ran, Xiuzhi, Song, Yanzhai, and Liu, Chang-Jun. Cytochrome b 5 Is an Obligate Electron Shuttle Protein for Syringyl Lignin Biosynthesis in Arabidopsis. United States: N. p., 2019.
Web. doi:10.1105/tpc.18.00778.
Gou, Mingyue, Yang, Xiaoman, Zhao, Yunjun, Ran, Xiuzhi, Song, Yanzhai, & Liu, Chang-Jun. Cytochrome b 5 Is an Obligate Electron Shuttle Protein for Syringyl Lignin Biosynthesis in Arabidopsis. United States. https://doi.org/10.1105/tpc.18.00778
Gou, Mingyue, Yang, Xiaoman, Zhao, Yunjun, Ran, Xiuzhi, Song, Yanzhai, and Liu, Chang-Jun. Mon .
"Cytochrome b 5 Is an Obligate Electron Shuttle Protein for Syringyl Lignin Biosynthesis in Arabidopsis". United States. https://doi.org/10.1105/tpc.18.00778.
@article{osti_1573095,
title = {Cytochrome b 5 Is an Obligate Electron Shuttle Protein for Syringyl Lignin Biosynthesis in Arabidopsis},
author = {Gou, Mingyue and Yang, Xiaoman and Zhao, Yunjun and Ran, Xiuzhi and Song, Yanzhai and Liu, Chang-Jun},
abstractNote = {In monolignol biosynthetic pathway, three cytochrome P450-catalzyed reactions essentially determine the structural characteristics of lignin precursors. Among them, ferulate 5-hydroxylase (F5H) is specifically responsible for syringyl (S) lignin subunit formation. NADPH Cytochrome P450 oxidoreductase (CPR) is commonly regarded as the electron carrier for the P450-catalyzed reactions in monolignol biosynthesis. Here we show that cytochrome b5 isoform D (CB5D) is an indispensable electron shuttle intermediate specific for S-lignin biosynthesis. Arabidopsis CB5D localizes on endoplasmic reticulum membrane and physically associates with monolignol P450 enzymes. Disrupting CB5D in Arabidopsis results in >60% reduction of S-lignin subunits but no impairment on G-lignin formation compared to the wild type, which sharply contrasts to the impairment of both G- and S-lignin synthesis after disruption of ATR2, the Arabidopsis CPR. The defect of S-lignin synthesis in cb5d mutants is rescued with expression of the gene encoding CB5D but not with the CB5D mutant variants devoid of its electron shuttle property. While disruption of ATR2 suppresses both C4H and F5H catalytic activities, elimination of CB5D specifically depletes the latter's activity. Our study demonstrates that CB5D functions as an obligate electron shuttle intermediate specifically augmenting F5H-catalyzed reaction thus controlling S-lignin biosynthesis.},
doi = {10.1105/tpc.18.00778},
journal = {The Plant Cell},
number = 6,
volume = 31,
place = {United States},
year = {Mon Apr 08 00:00:00 EDT 2019},
month = {Mon Apr 08 00:00:00 EDT 2019}
}
https://doi.org/10.1105/tpc.18.00778
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