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

8 Citations (Scopus)

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

Fingerprint

cellulose synthase
Cellulose
cellulose
mutants
missense mutation
biocompatible materials
Temperature
Plant Cells
Biocompatible Materials
Missense Mutation
glucans
structure-activity relationships
point mutation
Point Mutation
Arabidopsis
Computer Simulation
Cell Wall
temperature
plasma membrane
Arabidopsis thaliana

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science

Cite this

Slabaugh, Erin ; Sethaphong, Latsavongsakda ; Xiao, Chaowen ; Amick, Joshua ; Anderson, Charles T. ; Haigler, Candace H. ; Yingling, Yaroslava G. / Computational and genetic evidence that different structural conformations of a non-catalytic region affect the function of plant cellulose synthase. In: Journal of experimental botany. 2014 ; Vol. 65, No. 22. pp. 6645-6653.
@article{e3d068e7e09c491c85f41a3b0d1b5584,
title = "Computational and genetic evidence that different structural conformations of a non-catalytic region affect the function of plant cellulose synthase",
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.",
author = "Erin Slabaugh and Latsavongsakda Sethaphong and Chaowen Xiao and Joshua Amick and Anderson, {Charles T.} and Haigler, {Candace H.} and Yingling, {Yaroslava G.}",
year = "2014",
month = "12",
day = "1",
doi = "10.1093/jxb/eru383",
language = "English (US)",
volume = "65",
pages = "6645--6653",
journal = "Journal of Experimental Botany",
issn = "0022-0957",
publisher = "Oxford University Press",
number = "22",

}

Computational and genetic evidence that different structural conformations of a non-catalytic region affect the function of plant cellulose synthase. / Slabaugh, Erin; Sethaphong, Latsavongsakda; Xiao, Chaowen; Amick, Joshua; Anderson, Charles T.; Haigler, Candace H.; Yingling, Yaroslava G.

In: Journal of experimental botany, Vol. 65, No. 22, 01.12.2014, p. 6645-6653.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Computational and genetic evidence that different structural conformations of a non-catalytic region affect the function of plant cellulose synthase

AU - Slabaugh, Erin

AU - Sethaphong, Latsavongsakda

AU - Xiao, Chaowen

AU - Amick, Joshua

AU - Anderson, Charles T.

AU - Haigler, Candace H.

AU - Yingling, Yaroslava G.

PY - 2014/12/1

Y1 - 2014/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84922471264&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84922471264&partnerID=8YFLogxK

U2 - 10.1093/jxb/eru383

DO - 10.1093/jxb/eru383

M3 - Article

C2 - 25262226

AN - SCOPUS:84922471264

VL - 65

SP - 6645

EP - 6653

JO - Journal of Experimental Botany

JF - Journal of Experimental Botany

SN - 0022-0957

IS - 22

ER -