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Title: CAD 1 and CCR 2 protein complex formation in monolignol biosynthesis in Populus trichocarpa

Abstract

Lignin is the major phenolic polymer in plant secondary cell walls and is polymerized from monomeric subunits, the monolignols. Eleven enzyme families are implicated in monolignol biosynthesis. In this report, we examined the functions of members of the cinnamyl alcohol dehydrogenase (CAD) and cinnamoyl-CoA reductase (CCR) families in wood formation in Populus trichocarpa, including the regulatory effects of their transcripts and protein activities on monolignol biosynthesis. Enzyme activity assays from stem-differentiating xylem (SDX) proteins showed that RNAi suppression of PtrCAD1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNAi suppression of PtrCCR2, the only CCR member highly expressed in SDX, caused a reciprocal reduction in SDX protein CAD activities. The enzyme assays of mixed and coexpressed recombinant proteins supported physical interactions between PtrCAD1 and PtrCCR2. Biomolecular fluorescence complementation and pull-down/co-immunoprecipitation experiments supported a hypothesis of PtrCAD1/PtrCCR2 heterodimer formation. These results imply evidence for the formation of PtrCAD1/PtrCCR2 protein complexes in monolignol biosynthesis in planta.

Authors:
 [1];  [2];  [3];  [4];  [1];  [2];  [5];  [2];  [2];  [6];  [2];  [3];  [2];  [1];  [6]
  1. Chinese Academy of Forestry, Beijing (China)
  2. North Carolina State Univ., Raleigh, NC (United States)
  3. Univ. of Wisconsin, Madison, WI (United States)
  4. Northeast Forestry Univ., Harbin (China); Beihua Univ., Jilin (China)
  5. Northeast Forestry Univ., Harbin (China); National Taiwan Univ., Taipei (Taiwan)
  6. North Carolina State Univ., Raleigh, NC (United States); Northeast Forestry Univ., Harbin (China)
Publication Date:
Research Org.:
Univ. of Wisconsin, Madison, WI (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1506674
Alternate Identifier(s):
OSTI ID: 1479510
Grant/Contract Number:  
SC0018409; BER DE‐FC02‐07ER64494; DE‐SC0018409
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
New Phytologist
Additional Journal Information:
Journal Volume: 222; Journal Issue: 1; Journal ID: ISSN 0028-646X
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; co‐immunoprecipitation; enzyme activity; monolignol biosynthetic pathway; nuclear magnetic resonance (NMR); Populus trichocarpa; stem‐differentiating xylem protein

Citation Formats

Yan, Xiaojing, Liu, Jie, Kim, Hoon, Liu, Baoguang, Huang, Xiong, Yang, Zhichang, Lin, Ying‐Chung Jimmy, Chen, Hao, Yang, Chenmin, Wang, Jack P., Muddiman, David C., Ralph, John, Sederoff, Ronald R., Li, Quanzi, and Chiang, Vincent L.. CAD 1 and CCR 2 protein complex formation in monolignol biosynthesis in Populus trichocarpa. United States: N. p., 2018. Web. doi:10.1111/nph.15505.
Yan, Xiaojing, Liu, Jie, Kim, Hoon, Liu, Baoguang, Huang, Xiong, Yang, Zhichang, Lin, Ying‐Chung Jimmy, Chen, Hao, Yang, Chenmin, Wang, Jack P., Muddiman, David C., Ralph, John, Sederoff, Ronald R., Li, Quanzi, & Chiang, Vincent L.. CAD 1 and CCR 2 protein complex formation in monolignol biosynthesis in Populus trichocarpa. United States. doi:10.1111/nph.15505.
Yan, Xiaojing, Liu, Jie, Kim, Hoon, Liu, Baoguang, Huang, Xiong, Yang, Zhichang, Lin, Ying‐Chung Jimmy, Chen, Hao, Yang, Chenmin, Wang, Jack P., Muddiman, David C., Ralph, John, Sederoff, Ronald R., Li, Quanzi, and Chiang, Vincent L.. Mon . "CAD 1 and CCR 2 protein complex formation in monolignol biosynthesis in Populus trichocarpa". United States. doi:10.1111/nph.15505.
@article{osti_1506674,
title = {CAD 1 and CCR 2 protein complex formation in monolignol biosynthesis in Populus trichocarpa},
author = {Yan, Xiaojing and Liu, Jie and Kim, Hoon and Liu, Baoguang and Huang, Xiong and Yang, Zhichang and Lin, Ying‐Chung Jimmy and Chen, Hao and Yang, Chenmin and Wang, Jack P. and Muddiman, David C. and Ralph, John and Sederoff, Ronald R. and Li, Quanzi and Chiang, Vincent L.},
abstractNote = {Lignin is the major phenolic polymer in plant secondary cell walls and is polymerized from monomeric subunits, the monolignols. Eleven enzyme families are implicated in monolignol biosynthesis. In this report, we examined the functions of members of the cinnamyl alcohol dehydrogenase (CAD) and cinnamoyl-CoA reductase (CCR) families in wood formation in Populus trichocarpa, including the regulatory effects of their transcripts and protein activities on monolignol biosynthesis. Enzyme activity assays from stem-differentiating xylem (SDX) proteins showed that RNAi suppression of PtrCAD1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNAi suppression of PtrCCR2, the only CCR member highly expressed in SDX, caused a reciprocal reduction in SDX protein CAD activities. The enzyme assays of mixed and coexpressed recombinant proteins supported physical interactions between PtrCAD1 and PtrCCR2. Biomolecular fluorescence complementation and pull-down/co-immunoprecipitation experiments supported a hypothesis of PtrCAD1/PtrCCR2 heterodimer formation. These results imply evidence for the formation of PtrCAD1/PtrCCR2 protein complexes in monolignol biosynthesis in planta.},
doi = {10.1111/nph.15505},
journal = {New Phytologist},
issn = {0028-646X},
number = 1,
volume = 222,
place = {United States},
year = {2018},
month = {10}
}

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