Evidence map›Paper›PMID 17056709›Full record

ArticleThe Plant cell2006

Arabidopsis thaliana RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-D-xylosyltransferases involved in the synthesis of pectic rhamnogalacturonan-II.

Jack Egelund, Bent Larsen Petersen, Mohammed Saddik Motawia, Iben Damager, Ahmed Faik, Carl Erik Olsen, Tadashi Ishii, Henrik Clausen, Peter Ulvskov, Naomi Geshi

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
9.5field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 138 citations in OpenAlex.

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  11. A Pipeline towards the Biochemical Characterization of theInternational journal of molecular sciences · 2021
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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

10 authors at 3 institutions in 3 countries.

Jack EgelundBiotechnology Group, Danish Institute of Agricultural Sciences and Center for Molecular Plant Physiology, DK-1871 Frederiksberg C, Denmark.
Bent Larsen Petersen
Mohammed Saddik Motawia
Iben Damager
Ahmed Faik
Carl Erik Olsen
Tadashi Ishii
Henrik Clausen
Peter Ulvskov
Naomi Geshi
Forestry and Forest Products Research Institute · JPMichigan State University · USUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two homologous plant-specific Arabidopsis thaliana genes, RGXT1 and RGXT2, belong to a new family of glycosyltransferases (CAZy GT-family-77) and encode cell wall (1,3)-alpha-d-xylosyltransferases. The deduced amino acid sequences contain single transmembrane domains near the N terminus, indicative of a type II membrane protein structure. Soluble secreted forms of the corresponding proteins expressed in insect cells showed xylosyltransferase activity, transferring d-xylose from UDP-alpha-d-xylose to l-fucose. The disaccharide product was hydrolyzed by alpha-xylosidase, whereas no reaction was catalyzed by beta-xylosidase. Furthermore, the regio- and stereochemistry of the methyl xylosyl-fucoside was determined by nuclear magnetic resonance to be an alpha-(1,3) linkage, demonstrating the isolated glycosyltransferases to be (1,3)-alpha-d-xylosyltransferases. This particular linkage is only known in rhamnogalacturonan-II, a complex polysaccharide essential to vascular plants, and is conserved across higher plant families. Rhamnogalacturonan-II isolated from both RGXT1 and RGXT2 T-DNA insertional mutants functioned as specific acceptor molecules in the xylosyltransferase assay. Expression of RGXT1- and RGXT2-enhanced green fluorescent protein constructs in Arabidopsis revealed that both fusion proteins were targeted to a Brefeldin A-sensitive compartment and also colocalized with the Golgi marker dye BODIPY TR ceramide, consistent with targeting to the Golgi apparatus. Taken together, these results suggest that RGXT1 and RGXT2 encode Golgi-localized (1,3)-alpha-d-xylosyltransferases involved in the biosynthesis of pectic rhamnogalacturonan-II.

Indexed as

Amino Acid SequenceAnimalsArabidopsis ProteinsBaculoviridaeBase SequenceDNA PrimersGolgi ApparatusInsectaIsoenzymesMolecular Sequence DataPectinsPentosyltransferasesReverse Transcriptase Polymerase Chain ReactionSequence Homology, Amino AcidSubstrate SpecificityUDP Xylose-Protein XylosyltransferaseArabidopsis ProteinsDNA PrimersIsoenzymesPectinsPentosyltransferasesrhamnogalacturonan IIUDP Xylose-Protein Xylosyltransferase

Identifiers

PMID17056709
PMCPMC1626629
OpenAlexW2096455668

What OpenQuestion holds

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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.