Evidence map›Paper›PMID 22966747›Full record

ArticleThe Plant journal : for cell and molecular biology2013

Identification of an additional protein involved in mannan biosynthesis.

Yan Wang, Jennifer C Mortimer, Jonathan Davis, Paul Dupree, Kenneth Keegstra

Open access · bronzeAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  6. Review
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  10. ACS omega · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Glucomannan inGenes · 2022
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Mechanistic insights from plant heteromannan synthesis in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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

5 authors at 3 institutions in 2 countries.

Yan WangGreat Lakes Bioenergy Research Center, Michigan State University, East Lansing, MI, 48824, USA.
Jennifer C MortimerDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK.
Jonathan DavisDepartment of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI, 48824, USA.
Paul DupreeDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, UK.
Kenneth KeegstraGreat Lakes Bioenergy Research Center, Michigan State University, East Lansing, MI, 48824, USA.
Great Lakes Bioenergy Research Center · USUniversity of Cambridge · GBMichigan State University · US

Funding

Biotechnology and Biological Sciences Research Council BB/G016240/1
6 · The paper itself

Abstract

Galactomannans comprise a β-1,4-mannan backbone substituted with α-1,6-galactosyl residues. Genes encoding the enzymes that are primarily responsible for backbone synthesis and side-chain addition of galactomannans were previously identified and characterized. To identify additional genes involved in galactomannan biosynthesis, we previously performed deep EST profiling of fenugreek (Trigonella foenum-graecum L.) seed endosperm, which accumulates large quantities of galactomannans as a reserve carbohydrate during seed development. One of the candidate genes encodes a protein that is likely to be a glycosyltransferase. Because this protein is involved in mannan biosynthesis, we named it 'mannan synthesis-related' (MSR). Here, we report the characterization of a fenugreek MSR gene (TfMSR) and its two Arabidopsis homologs, AtMSR1 and AtMSR2. TfMSR was highly and specifically expressed in the endosperm. TfMSR, AtMSR1 and AtMSR2 proteins were all determined to be localized to the Golgi by fluorescence confocal microscopy. The level of mannosyl residues in stem glucomannans decreased by approximately 40% for Arabidopsis msr1 single T-DNA insertion mutants and by more than 50% for msr1 msr2 double mutants, but remained unchanged for msr2 single mutants. In addition, in vitro mannan synthase activity from the stems of msr1 single and msr1 msr2 double mutants also decreased. Expression of AtMSR1 or AtMSR2 in the msr1 msr2 double mutant completely or partially restored mannosyl levels. From these results, we conclude that the MSR protein is important for mannan biosynthesis, and offer some ideas about its role.

Indexed as

EndospermGenes, PlantGolgi ApparatusMannansMannosyltransferasesMicrosomesPlant ProteinsTrigonellaMannansmannan synthetaseMannosyltransferasesPlant ProteinsArabidopsisfenugreekglycosyltransferaseGolgi proteinGT65mannan biosynthesis

Identifiers

PMID22966747
PMCPMC3558879
OpenAlexW2045246140

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.