Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-4-3
pubmed:abstractText
Using phragmoplastin as a bait, we isolated an Arabidopsis cDNA encoding a novel UDP-glucose transferase (UGT1). This interaction was confirmed by an in vitro protein--protein interaction assay using purified UGT1 and radiolabeled phragmoplastin. Protein gel blot results revealed that UGT1 is associated with the membrane fraction and copurified with the product-entrapped callose synthase complex. These data suggest that UGT1 may act as a subunit of callose synthase that uses UDP-glucose to synthesize callose, a 1,3-beta-glucan. UGT1 also interacted with Rop1, a Rho-like protein, and this interaction occurred only in its GTP-bound configuration, suggesting that the plant callose synthase may be regulated by Rop1 through the interaction with UGT1. The green fluorescent protein--UGT1 fusion protein was located on the forming cell plate during cytokinesis. We propose that UGT1 may transfer UDP-glucose from sucrose synthase to the callose synthase and thus help form a substrate channel for the synthesis of callose at the forming cell plate.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10066805, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10330464, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10488239, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10593966, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10594100, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10713266, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10722722, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10938350, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-10982429, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-11283334, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-1329666, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-16593478, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-7559757, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-7568131, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-7649185, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-7883697, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8085154, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8193299, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8257601, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8384581, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8489015, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8602515, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8631291, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-8938400, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9061948, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9076990, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9193713, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9295054, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9349281, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9445479, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9535914, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9640664, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9714825, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9765526, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9778851, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9874763, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9874810, http://linkedlifedata.com/resource/pubmed/commentcorrection/11283335-9884404
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1040-4651
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
769-79
pubmed:dateRevised
2010-9-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
A novel UDP-glucose transferase is part of the callose synthase complex and interacts with phragmoplastin at the forming cell plate.
pubmed:affiliation
Department of Molecular Genetics and Plant Biotechnology Center, Ohio State University, 1060 Carmack Road, Columbus, Ohio 43210-1002, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.