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

Journal Article · · New Phytologist
DOI:https://doi.org/10.1111/nph.15505· OSTI ID:1506674
 [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)

Summary 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. Here, we studied 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 RNA i suppression of Ptr CAD 1 in P. trichocarpa transgenics caused a reduction in SDX CCR activity. RNA i suppression of Ptr CCR 2 , 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 Ptr CAD 1 and Ptr CCR 2. Biomolecular fluorescence complementation and pull‐down/co‐immunoprecipitation experiments supported a hypothesis of Ptr CAD 1/Ptr CCR 2 heterodimer formation. These results provide evidence for the formation of Ptr CAD 1/Ptr CCR 2 protein complexes in monolignol biosynthesis in planta .

Research Organization:
Univ. of Wisconsin, Madison, WI (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
SC0018409; BER DE‐FC02‐07ER64494; DE‐SC0018409
OSTI ID:
1506674
Alternate ID(s):
OSTI ID: 1479510
Journal Information:
New Phytologist, Vol. 222, Issue 1; ISSN 0028-646X
Publisher:
WileyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 29 works
Citation information provided by
Web of Science

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Enzyme-Enzyme Interactions in Monolignol Biosynthesis journal January 2019
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An introduction to a Virtual Issue on Wood Biology journal January 2020
Functional Characteristics of Caffeoyl Shikimate Esterase in Larix Kaempferi and Monolignol Biosynthesis in Gymnosperms journal December 2019