Evidence map›Paper›PMID 25262226›Full record

ArticleJournal of experimental botany2014

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

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 18 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Erin SlabaughDepartment of Crop Science and Department of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695, USA.
Latsavongsakda SethaphongDepartment of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Chaowen XiaoDepartment of Biology, the Pennsylvania State University, University Park, PA 16802, USA.
Joshua AmickDepartment of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Charles T AndersonDepartment of Biology, the Pennsylvania State University, University Park, PA 16802, USA.
Candace H HaiglerDepartment of Crop Science and Department of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695, USA yara_yingling@ncsu.edu candace_haigler@ncsu.edu.
Yaroslava G YinglingDepartment of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA yara_yingling@ncsu.edu candace_haigler@ncsu.edu.
North Carolina State University · USPennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

BiocatalysisComputational BiologyAmino Acid SequenceArabidopsisArabidopsis ProteinsGlucosyltransferasesMolecular Sequence DataMutant ProteinsMutationPhenotypeProtein Structure, SecondaryRecombinant Fusion ProteinsSequence AlignmentStructure-Activity RelationshipArabidopsis Proteinscellulose synthaseGlucosyltransferasesMutant ProteinsRecombinant Fusion ProteinsCellulose biosynthesisCESAgenetic complementationprotein structural modellingrsw1 mutanttransmembrane helix.

Identifiers

PMID25262226
PMCPMC4246192
OpenAlexW2109335397

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.