Linked Life Data

12930826

Source:http://linkedlifedata.com/resource/pubmed/id/12930826

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2003-10-27
pubmed:abstractText
The surface of a pollen grain consists of an outermost coat and an underlying wall. In maize (Zea mays L.), the pollen coat contains two major proteins derived from the adjacent tapetum cells in the anthers. One of the proteins is a 35-kDa endoxylanase (Wu, S. S. H., Suen, D. F., Chang, H. C., and Huang, A. H. C. (2002) J. Biol. Chem. 277, 49055-49064). The other protein of 70 kDa was purified to homogeneity and shown to be a beta-glucanase. Its gene sequence and the developmental pattern of its mRNA differ from those of the known beta-glucanases that hydrolyze the callose wall of the microspore tetrad. Mature pollen placed in a liquid medium released about nine major proteins. These proteins were partially sequenced and identified via GenBank trade mark data bases, and some had not been previously reported to be in pollen. They appear to have wall-loosening, structural, and enzymatic functions. A novel pollen wall-bound protein of 17 kDa has a unique pattern of cysteine distribution in its sequence (six tandem repeats of CX3CX10-15) that could chelate cations and form signal-receiving finger motifs. These pollen-released proteins were synthesized in the pollen interior, and their mRNA increased during pollen maturation and germination. They were localized mainly in the pollen tube wall. The pollen shell was isolated and found to contain no detectable proteins. We suggest that the pollen-coat beta-glucanase and xylanase hydrolyze the stigma wall for pollen tube entry and that the pollen secrete proteins to loosen or become new wall constituents of the tube and to break the wall of the transmitting track for tube advance.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43672-81
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:12930826-Allergens, pubmed-meshheading:12930826-Amino Acid Motifs, pubmed-meshheading:12930826-Amino Acid Sequence, pubmed-meshheading:12930826-Cations, pubmed-meshheading:12930826-Cell Wall, pubmed-meshheading:12930826-DNA, Complementary, pubmed-meshheading:12930826-Databases as Topic, pubmed-meshheading:12930826-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12930826-Ether, Ethyl, pubmed-meshheading:12930826-Flowers, pubmed-meshheading:12930826-Glycoside Hydrolases, pubmed-meshheading:12930826-Microscopy, Fluorescence, pubmed-meshheading:12930826-Molecular Sequence Data, pubmed-meshheading:12930826-Phylogeny, pubmed-meshheading:12930826-Plant Proteins, pubmed-meshheading:12930826-Pollen, pubmed-meshheading:12930826-Protein Structure, Tertiary, pubmed-meshheading:12930826-RNA, pubmed-meshheading:12930826-RNA, Messenger, pubmed-meshheading:12930826-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:12930826-Sequence Homology, Amino Acid, pubmed-meshheading:12930826-Zea mays
pubmed:year
2003
pubmed:articleTitle
Cell wall reactive proteins in the coat and wall of maize pollen: potential role in pollen tube growth on the stigma and through the style.
pubmed:affiliation
Center for Plant Cell Biology, Department of Botany and Plant Sciences, University of California, Riverside, California 92521, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't