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rdf:type |
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lifeskim:mentions |
umls-concept:C0003062,
umls-concept:C0016964,
umls-concept:C0017337,
umls-concept:C0078641,
umls-concept:C0162741,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0702242,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C2700640
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pubmed:issue |
7
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pubmed:dateCreated |
2003-7-2
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pubmed:abstractText |
Xyloglucans are the principal glycans that interlace cellulose microfibrils in most flowering plants. The mur3 mutant of Arabidopsis contains a severely altered structure of this polysaccharide because of the absence of a conserved alpha-L-fucosyl-(1-->2)-beta-D-galactosyl side chain and excessive galactosylation at an alternative xylose residue. Despite this severe structural alteration, mur3 plants were phenotypically normal and exhibited tensile strength in their inflorescence stems comparable to that of wild-type plants. The MUR3 gene was cloned positionally and shown to encode a xyloglucan galactosyltransferase that acts specifically on the third xylose residue within the XXXG core structure of xyloglucan. MUR3 belongs to a large family of type-II membrane proteins that is evolutionarily conserved among higher plants. The enzyme shows sequence similarities to the glucuronosyltransferase domain of exostosins, a class of animal glycosyltransferases that catalyze the synthesis of heparan sulfate, a glycosaminoglycan with numerous roles in cell differentiation and development. This finding suggests that components of the plant cell wall and of the animal extracellular matrix are synthesized by evolutionarily related enzymes even though the structures of the corresponding polysaccharides are entirely different from each other.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-10373113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-10747946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-10864928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11014181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11042448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11152613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11554468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11554480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11743104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11752315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-11854459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-12032363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-12045103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-12451175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-12566589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-14207550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-16663614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-1844884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-3107426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-7639791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-8106085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-8188214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-8401598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-8650583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-8938374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-9011379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-9107029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-9127953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-9301086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12837954-9306698
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1040-4651
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1662-70
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pubmed:dateRevised |
2010-9-14
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pubmed:meshHeading |
pubmed-meshheading:12837954-Amino Acid Sequence,
pubmed-meshheading:12837954-Animals,
pubmed-meshheading:12837954-Arabidopsis,
pubmed-meshheading:12837954-Arabidopsis Proteins,
pubmed-meshheading:12837954-Cell Surface Extensions,
pubmed-meshheading:12837954-Cell Wall,
pubmed-meshheading:12837954-Cloning, Molecular,
pubmed-meshheading:12837954-Evolution, Molecular,
pubmed-meshheading:12837954-Galactosyltransferases,
pubmed-meshheading:12837954-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:12837954-Gene Expression Regulation, Plant,
pubmed-meshheading:12837954-Glucans,
pubmed-meshheading:12837954-Microscopy, Electron, Scanning,
pubmed-meshheading:12837954-Molecular Sequence Data,
pubmed-meshheading:12837954-Mutation,
pubmed-meshheading:12837954-Phenotype,
pubmed-meshheading:12837954-Sequence Homology, Amino Acid,
pubmed-meshheading:12837954-Transcription Factors,
pubmed-meshheading:12837954-Xylans
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pubmed:year |
2003
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pubmed:articleTitle |
The MUR3 gene of Arabidopsis encodes a xyloglucan galactosyltransferase that is evolutionarily related to animal exostosins.
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pubmed:affiliation |
Department of Botany and Plant Pathology, Purdue University, West Lafayette, Indiana 47907-1155, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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