Linked Life Data

12576669

Source:http://linkedlifedata.com/resource/pubmed/id/12576669

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-2-10
pubmed:abstractText
In plants gibberellins (GAs) are responsible for triggering stem or internodal elongation. To comprehend the molecular basis of internodal elongation in rice, a proteomics approach using differentially displayed proteins on two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) was carried out to identify the proteins expressed during the GA controlled leaf-sheath elongation response. Out of 352 protein spots detected on 2-D PAGE, 32 proteins showed modulation in the expression levels in GA3-treated leaf-sheath for 48 h as compared to control. These proteins were analyzed using protein sequencer and/or mass spectrometry in conjunction with the protein database to assign putative identities. The twin protein spots (LS079 and LS083), identified as calreticulin, showed different isoelectric points and expression level in GA3-treated leaf-sheath. The expression level of LS083 (pI 4.0) was down-regulated as compared to the up-regulation of LS079 (pI 4.3). In the presence of GA3 and growth inhibitor, uniconazole and abscisic acid, respectively, no elongation in leaf-sheath occurred and calreticulin did not shift from LS083 to LS079. Over-expression of calreticulin in rice inhibited the callus regeneration and seedling growth. These results suggest that calreticulin is an important component in the GA signaling pathway that regulates rice seedling leaf-sheath elongation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
129-36
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Characterization of proteins responsive to gibberellin in the leaf-sheath of rice (Oryza sativa L.) seedling using proteome analysis.
pubmed:affiliation
Department of Molecular Biology, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't