NDLI: Prediction of the structures of the plant-specific regions of vascular plant cellulose synthases and correlated functional analysis

Content Provider	Springer Nature Link
Author	Sethaphong, Latsavongsakda Davis, Jonathan K. Slabaugh, Erin Singh, Abhishek Haigler, Candace H. Yingling, Yaroslava G.
Copyright Year	2015
Abstract	Seed plants express cellulose synthase (CESA) protein isoforms with non-redundant functions, but how the isoforms function differently is unknown. Compared to bacterial cellulose synthases, CESAs have two insertions in the large cytosolic loop: the relatively well-conserved Plant Conserved Region (P-CR) and a Class Specific Region (CSR) that varies between CESAs. Absent any atomic structure of a plant CESA, we used ab initio protein structure prediction and molecular modeling to explore how these plant-specific regions may modulate CESA function. We modeled P-CR and CSR peptides from Arabidopsis thaliana CESAs representing the six clades of seed plant CESAs. As expected, the predicted wild type P-CR structures were similar. Modeling of the mutant P-CR of Atcesa8 R362K (fra6) suggested that changes in local structural stability and surface electrostatics may cause the mutant phenotype. Among CSRs within CESAs required for primary wall cellulose synthesis, the amino sequence and the modeled arrangement of helices was most similar in AtCESA1 and AtCESA3. Genetic complementation of known Arabidopsis mutants showed that the CSRs of AtCESA1 and AtCESA3 can function interchangeably in vivo. Analysis of protein surface electrostatics led to ideas about how the surface charges on CSRs may mediate protein–protein interactions. Refined modeling of the P-CR and CSR regions of GhCESA1 from cotton modified their tertiary structures, spatial relationships to the catalytic domain, and preliminary predictions about CESA oligomer formation. Cumulatively, the results provide structural clues about the function of plant-specific regions of CESA.
Starting Page	145
Ending Page	161
Page Count	17
File Format	PDF
ISSN	09690239
Journal	Cellulose
Volume Number	23
Issue Number	1
e-ISSN	1572882X
Language	English
Publisher	Springer Netherlands
Publisher Date	2015-10-24
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Arabidopsis thaliana Cellulose synthesis Computational protein structure prediction Isoform specificity Mutant complementation Bioorganic Chemistry Physical Chemistry Organic Chemistry Polymer Sciences
Content Type	Text
Resource Type	Article
Subject	Polymers and Plastics

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