Document Detail


Three members of the Arabidopsis glycosyltransferase family 8 are xylan glucuronosyltransferases.
MedLine Citation:
PMID:  22706449     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Xylan is a major component of the plant cell wall and the most abundant noncellulosic component in the secondary cell walls that constitute the largest part of plant biomass. Dicot glucuronoxylan consists of a linear backbone of β(1,4)-linked xylose residues substituted with α(1,2)-linked glucuronic acid (GlcA). Although several genes have been implicated in xylan synthesis through mutant analyses, the biochemical mechanisms responsible for synthesizing xylan are largely unknown. Here, we show evidence for biochemical activity of GUX1 (for GlcA substitution of xylan 1), a member of Glycosyltransferase Family 8 in Arabidopsis (Arabidopsis thaliana) that is responsible for adding the glucuronosyl substitutions onto the xylan backbone. GUX1 has characteristics typical of Golgi-localized glycosyltransferases and a K(m) for UDP-GlcA of 165 μm. GUX1 strongly favors xylohexaose as an acceptor over shorter xylooligosaccharides, and with xylohexaose as an acceptor, GlcA is almost exclusively added to the fifth xylose residue from the nonreducing end. We also show that several related proteins, GUX2 to GUX5 and Plant Glycogenin-like Starch Initiation Protein6, are Golgi localized and that only two of these proteins, GUX2 and GUX4, have activity as xylan α-glucuronosyltransferases.
Authors:
Emilie A Rennie; Sara Fasmer Hansen; Edward E K Baidoo; Masood Z Hadi; Jay D Keasling; Henrik Vibe Scheller
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-06-15
Journal Detail:
Title:  Plant physiology     Volume:  159     ISSN:  1532-2548     ISO Abbreviation:  Plant Physiol.     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-08-03     Completed Date:  2012-12-10     Revised Date:  2013-04-01    
Medline Journal Info:
Nlm Unique ID:  0401224     Medline TA:  Plant Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1408-17     Citation Subset:  IM    
Affiliation:
Feedstocks Division, Joint BioEnergy Institute, Emeryville, California 94608, USA.
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MeSH Terms
Descriptor/Qualifier:
Arabidopsis / enzymology*
Arabidopsis Proteins / genetics,  isolation & purification,  metabolism*
Glucuronosyltransferase / metabolism*
Glycosyltransferases / metabolism*
Microsomes / enzymology
Models, Molecular
Phylogeny
Protein Transport
Recombinant Proteins / isolation & purification,  metabolism
Subcellular Fractions / enzymology
Tobacco / metabolism
Xylans / metabolism*
Chemical
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Recombinant Proteins; 0/Xylans; EC 2.4.-/GUX1 protein, Arabidopsis; EC 2.4.-/GUX2 protein, Arabidopsis; EC 2.4.-/Glycosyltransferases; EC 2.4.1.17/Glucuronosyltransferase
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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