Linked Life Data

15937722

Source:http://linkedlifedata.com/resource/pubmed/id/15937722

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-7-19
pubmed:abstractText
Pathogenesis-related proteins (PR), including beta-1,3-glucanases may provide the first line of defense against fungal pathogens. Many PR proteins are activated by salicylic acid (SA), which acts as an endogenous signal. We have previously isolated seven members of the beta-1,3-glucanase gene family in barley (Hordeum vulgare). In this paper, we characterized the beta-1,3-glucanase isoenzyme GIII for SA-responsive elements in the GIII gene promoter. A series of deletion mutations of the promoter were fused to the reporter gene beta-glucuronidase (gus). The GUS activity was analyzed in rice calli (Oryza sativa L.) in response to SA. A deletion fragment between -362 and +106 bp showed the highest level of GUS activity in these assays. This promoter fused with gus was further introduced into rice plants for stable transformation. Histochemical staining and fluorometric quantitation of GUS activity in leaves of transgenic plants revealed prominent GUS expression after SA induction. RNA analysis by Northern blotting confirmed the importance of this region, indicating that cis-acting elements required for SA-inducible expression exist within 362 bp upstream from the transcriptional start site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0918-9440
pubmed:author
pubmed:issnType
Print
pubmed:volume
118
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-21
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Activation of the gene promoter of barley beta-1,3-glucanase isoenzyme GIII is salicylic acid (SA)-dependent in transgenic rice plants.
pubmed:affiliation
Biotechnology Research Center, The Key Laboratory of Gene Engineering of Education Ministry, Zhongshan University, Guangzhou, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't