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Title: Evidence for Plant-Conserved Region Mediated Trimeric CESAs in Plant Cellulose Synthase Complexes

Abstract

Higher plants synthesize cellulose using membrane-bound, six-lobed cellulose synthase complexes, each lobe containing trimeric cellulose synthases (CESAs). Although molecular biology reports support heteromeric trimers composed of different isoforms, a homomeric trimer was reported for in vitro studies of the catalytic domain of CESA1 of Arabidopsis (AtCESA1CatD) and confirmed in cryoEM structures of full-length CESA8 and CESA7 of poplar and cotton, respectively. In both structures, a small portion of the plant-conserved region (P-CR) forms the only contacts between catalytic domains of the monomers. Here, we report inter-subunit lysine-crosslinks that localize to the small P-CR, negative-stain EM structure, and modeling data for homotrimers of AtCESA1CatD. Molecular dynamics simulations for AtCESA1CatD trimers based on the CESA8 cryoEM structure were stable and dependent upon a small set of residue contacts. The results suggest that homomeric CESA trimers may be important for the synthesis of primary and secondary cell walls and identify key residues for future mutagenic studies.

Authors:
 [1];  [2];  [3]; ORCiD logo [4];  [4];  [5];  [5]; ORCiD logo [5]; ORCiD logo [2];  [3]; ORCiD logo [4]; ORCiD logo [4]
  1. Sichuan Univ., Chengdu (China); Pennsylvania State Univ., University Park, PA (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  3. Rockefeller Univ., New York, NY (United States)
  4. Pennsylvania State Univ., University Park, PA (United States)
  5. North Carolina State Univ., Raleigh, NC (United States)
Publication Date:
Research Org.:
Pennsylvania State Univ., University Park, PA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH)
OSTI Identifier:
1922484
Grant/Contract Number:  
SC0001090; P41 GM109824; P41 GM103314
Resource Type:
Accepted Manuscript
Journal Name:
Biomacromolecules
Additional Journal Information:
Journal Volume: 23; Journal Issue: 9; Journal ID: ISSN 1525-7797
Publisher:
American Chemical Society
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; cellulose synthase; cell walls; cryoEM; cellulose synthase complex; structure; plant cell wall; Arabidopsis

Citation Formats

Du, Juan, Vandavasi, Venu Gopal, Molloy, Kelly R., Yang, Hui, Massenburg, Lynnicia N., Singh, Abhishek, Kwansa, Albert L., Yingling, Yaroslava G., O’Neill, Hugh, Chait, Brian T., Kumar, Manish, and Nixon, B. Tracy. Evidence for Plant-Conserved Region Mediated Trimeric CESAs in Plant Cellulose Synthase Complexes. United States: N. p., 2022. Web. doi:10.1021/acs.biomac.2c00550.
Du, Juan, Vandavasi, Venu Gopal, Molloy, Kelly R., Yang, Hui, Massenburg, Lynnicia N., Singh, Abhishek, Kwansa, Albert L., Yingling, Yaroslava G., O’Neill, Hugh, Chait, Brian T., Kumar, Manish, & Nixon, B. Tracy. Evidence for Plant-Conserved Region Mediated Trimeric CESAs in Plant Cellulose Synthase Complexes. United States. https://doi.org/10.1021/acs.biomac.2c00550
Du, Juan, Vandavasi, Venu Gopal, Molloy, Kelly R., Yang, Hui, Massenburg, Lynnicia N., Singh, Abhishek, Kwansa, Albert L., Yingling, Yaroslava G., O’Neill, Hugh, Chait, Brian T., Kumar, Manish, and Nixon, B. Tracy. Wed . "Evidence for Plant-Conserved Region Mediated Trimeric CESAs in Plant Cellulose Synthase Complexes". United States. https://doi.org/10.1021/acs.biomac.2c00550. https://www.osti.gov/servlets/purl/1922484.
@article{osti_1922484,
title = {Evidence for Plant-Conserved Region Mediated Trimeric CESAs in Plant Cellulose Synthase Complexes},
author = {Du, Juan and Vandavasi, Venu Gopal and Molloy, Kelly R. and Yang, Hui and Massenburg, Lynnicia N. and Singh, Abhishek and Kwansa, Albert L. and Yingling, Yaroslava G. and O’Neill, Hugh and Chait, Brian T. and Kumar, Manish and Nixon, B. Tracy},
abstractNote = {Higher plants synthesize cellulose using membrane-bound, six-lobed cellulose synthase complexes, each lobe containing trimeric cellulose synthases (CESAs). Although molecular biology reports support heteromeric trimers composed of different isoforms, a homomeric trimer was reported for in vitro studies of the catalytic domain of CESA1 of Arabidopsis (AtCESA1CatD) and confirmed in cryoEM structures of full-length CESA8 and CESA7 of poplar and cotton, respectively. In both structures, a small portion of the plant-conserved region (P-CR) forms the only contacts between catalytic domains of the monomers. Here, we report inter-subunit lysine-crosslinks that localize to the small P-CR, negative-stain EM structure, and modeling data for homotrimers of AtCESA1CatD. Molecular dynamics simulations for AtCESA1CatD trimers based on the CESA8 cryoEM structure were stable and dependent upon a small set of residue contacts. The results suggest that homomeric CESA trimers may be important for the synthesis of primary and secondary cell walls and identify key residues for future mutagenic studies.},
doi = {10.1021/acs.biomac.2c00550},
journal = {Biomacromolecules},
number = 9,
volume = 23,
place = {United States},
year = {Wed Aug 10 00:00:00 EDT 2022},
month = {Wed Aug 10 00:00:00 EDT 2022}
}

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