Computational and genetic evidence that different structural conformations of a non-catalytic region affect the function of plant cellulose synthase

Erin Slabaugh, Latsavongsakda Sethaphong, Chaowen Xiao, Joshua Amick, Charles T. Anderson, Candace H. Haigler, Yaroslava G. Yingling

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

The β-1,4-glucan chains comprising cellulose are synthesized by cellulose synthases in the plasma membranes of diverse organisms including bacteria and plants. Understanding structure-function relationships in the plant enzymes involved in cellulose synthesis (CESAs) is important because cellulose is the most abundant component in the plant cell wall, a key renewable biomaterial. Here, we explored the structure and function of the region encompassing transmembrane helices (TMHs) 5 and 6 in CESA using computational and genetic tools. Ab initio computational structure prediction revealed novel bi-modal structural conformations of the region between TMH5 and 6 that may affect CESA function. Here we present our computational findings on this region in three CESAs of Arabidopsis thaliana (AtCESA1, 3, and 6), the Atcesa3 ixr1-2 mutant, and a novel missense mutation in AtCESA1. A newly engineered point mutation in AtCESA1 (Atcesa1 F954L) that altered the structural conformation in silico resulted in a protein that was not fully functional in the temperature-sensitive Atcesa1 rsw1-1 mutant at the restrictive temperature. The combination of computational and genetic results provides evidence that the ability of the TMH5-6 region to adopt specific structural conformations is important for CESA function.

Original languageEnglish (US)
Pages (from-to)6645-6653
Number of pages9
JournalJournal of experimental botany
Volume65
Issue number22
DOIs
StatePublished - Dec 1 2014

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All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science

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