Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2000-4-24
pubmed:databankReference
pubmed:abstractText
Adhesion of pollen grains to the stigmatic surface is a critical step during sexual reproduction in plants. In Brassica, S locus-related glycoprotein 1 (SLR1), a stigma-specific protein belonging to the S gene family of proteins, has been shown to be involved in this step. However, the identity of the interacting counterpart in pollen and the molecular mechanism of this interaction have not been determined. Using an optical biosensor immobilized with S gene family proteins, we detected strong SLR1-binding activity in pollen coat extracts of Brassica campestris. Two SLR1-binding proteins, named SLR1-BP1 and SLR1-BP2, were identified and purified by the combination of SLR1 affinity column chromatography and reverse-phase HPLC. Sequence analyses revealed that these two proteins (i) differ only in that a proline residue near the N terminus is hydroxylated in SLR1-BP1 but not in SLR1-BP2, and (ii) are members of the class A pollen coat protein (PCP) family, which includes PCP-A1, an SLG (S locus glycoprotein)-binding protein isolated from Brassica oleracea. Kinetic analysis showed that SLR1-BP1 and SLR1-BP2 specifically bound SLR1 with high affinity (K(d) = 5.6 and 4.4 nM, respectively). The SLR1-BP gene was specifically expressed in pollen at late stages of development, and its sequence is highly conserved in Brassica species with the A genome.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-10471721, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-10576728, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-10677556, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-11607350, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-1681543, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-1707843, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-1863779, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-2535545, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-3808952, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-7672580, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-8564299, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-8771786, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-9539157, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-9707533, http://linkedlifedata.com/resource/pubmed/commentcorrection/10716697-9927642
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
97
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3765-70
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Isolation and characterization of pollen coat proteins of Brassica campestris that interact with S locus-related glycoprotein 1 involved in pollen-stigma adhesion.
pubmed:affiliation
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0101, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't