Linked Life Data

15655675

Source:http://linkedlifedata.com/resource/pubmed/id/15655675

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-6-14
pubmed:abstractText
UDP-xylose (UDP-Xyl) is a sugar donor for the synthesis of glycoproteins, polysaccharides, various metabolites, and oligosaccharides in plants, vertebrates, and fungi. In plants, the biosynthesis of UDP-Xyl from UDP-glucuronic acid (UDP-GlcA) appears to be catalyzed by numerous UDP-glucuronic acid decarboxylase (Uxs) isoforms. For example, six Uxs isoforms in Arabidopsis thaliana (L.) and four in rice have been identified. However, the reason/s for the existence of several isoforms that are necessary for the synthesis of UDP-Xyl remains unknown. Here, we describe a Uxs isoform in Arabidopsis, AtUXS2, encoding an integral membrane protein that appears to be localized to the Golgi apparatus. The enzyme is a dimer and has distinct properties. Unlike the UXS3 isoform, which is shown here to be a soluble protein, the UXS2 isoform is membrane bound. The characteristics of the membrane-bound AtUxs2 and cytosolic AtUxs3 support the hypothesis that unique UDP-GlcA-DCs possessing distinct sub-cellular localizations can spatially regulate specific xylosylation events in plant cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0032-0935
pubmed:author
pubmed:issnType
Print
pubmed:volume
221
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
538-48
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Biosynthesis of UDP-xylose: characterization of membrane-bound AtUxs2.
pubmed:affiliation
Complex Carbohydrate Research Center and Department of Plant Biology, University of Georgia, 315 Riverbend Road, Athens, GA 30602-4712, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.