Evidence map›Paper›PMID 26850276›Full record

ArticlePlant physiology2016

A Glycosyltransferase from Nicotiana alata Pollen Mediates Synthesis of a Linear (1,5)-α-L-Arabinan When Expressed in Arabidopsis.

Edwin R Lampugnani, Yin Ying Ho, Isabel E Moller, Poh-Ling Koh, John F Golz, Antony Bacic, Ed Newbigin

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  4. NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion inProceedings of the National Academy of Sciences of the United States of America · 2024
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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.

Edwin R LampugnaniPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.).ORCID 0000-0002-3666-7240
Yin Ying HoPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.).
Isabel E MollerPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.).
Poh-Ling KohPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.).
John F GolzPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.).ORCID 0000-0001-9478-5459
Antony BacicPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.).
Ed NewbiginPlant Cell Biology Research Centre, School of BioSciences (E.R.L., Y.Y.H., I.E.M., P.-L.K., A.B., E.N.), and School of BioSciences (J.F.G.), University of Melbourne, Melbourne, Victoria, 3010 Australia; andAustralian Research Council Centre of Excellence in Plant Cell Walls, School of BioSciences, University of Melbourne, Parkville, Victoria 3010, Australia (E.R.L., Y.Y.H., I.E.M., A.B.) edwardjn@unimelb.edu.au.ORCID 0000-0002-9644-302X
Australian Research Council · AUThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The walls of Nicotiana alata pollen tubes contain a linear arabinan composed of (1,5)-α-linked arabinofuranose residues. Although generally found as a side chain on the backbone of the pectic polysaccharide rhamnogalacturonan I, the arabinan in N. alata pollen tubes is considered free, as there is no detectable rhamnogalacturonan I in these walls. Carbohydrate-specific antibodies detected arabinan epitopes at the tip and along the shank of N. alata pollen tubes that are predominantly part of the primary layer of the bilayered wall. A sequence related to ARABINAN DEFICIENT1 (AtARAD1), a presumed arabinan arabinosyltransferase from Arabidopsis (Arabidopsis thaliana), was identified by searching an N alata pollen transcriptome. Transcripts for this ARAD1-like sequence, which we have named N. alata ARABINAN DEFICIENT-LIKE1 (NaARADL1), accumulate in various tissues, most abundantly in the pollen grain and tube, and encode a protein that is a type II membrane protein with its catalytic carboxyl terminus located in the Golgi lumen. The NaARADL1 protein can form homodimers when transiently expressed in Nicotiana benthamiana leaves and heterodimers when coexpressed with AtARAD1 The expression of NaARADL1 in Arabidopsis led to plants with more arabinan in their walls and that also exuded a guttation fluid rich in arabinan. Chemical and enzymatic characterization of the guttation fluid showed that a soluble, linear α-(1,5)-arabinan was the most abundant polymer present. These results are consistent with NaARADL1 having an arabinan (1,5)-α-arabinosyltransferase activity.

Indexed as

ArabidopsisFluorescenceGlycosyltransferasesGolgi ApparatusNicotianaPentosyltransferasesPhylogenyPlant ProteinsPlants, Genetically ModifiedPollenPollen TubePolysaccharidesProtein MultimerizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSubcellular FractionsarabanarabinosyltransferaseGlycosyltransferasesPentosyltransferasesPlant ProteinsPolysaccharides

Identifiers

PMID26850276
PMCPMC4825119
OpenAlexW2271329302

What OpenQuestion holds

Textmetadata
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.