rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
40
|
pubmed:dateCreated |
2003-10-7
|
pubmed:databankReference |
|
pubmed:abstractText |
Hundreds of proteins involved in signaling pathways contain a Ca(2+)-dependent membrane-binding motif called the C2-domain. However, no small C2-domain proteins consisting of a single C2-domain have been reported in animal cells. We have isolated two cDNA clones, OsERG1a and OsERG1b, that encode two small C2-domain proteins of 156 and 159 amino acids, respectively, from a fungal elicitor-treated rice cDNA library. The clones are believed to have originated from a single gene by alternative splicing. Transcript levels of the OsERG1 gene are dramatically elevated by a fungal elicitor prepared from Magnaporthe grisea or by Ca(2+) ions. The OsERG1 protein produced in Escherichia coli binds to phospholipid vesicles in a Ca(2+)-dependent manner and is translocated to the plasma membrane of plant cells by treatment with either a fungal elicitor or a Ca(2+) ionophore. These results suggest that OsERG1 proteins containing a single C2-domain are involved in plant defense signaling systems.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0006-2960
|
pubmed:author |
pubmed-author:BahkJeong DongJD,
pubmed-author:ChoMoo JeMJ,
pubmed-author:HwangInhwanI,
pubmed-author:JinJing BoJB,
pubmed-author:KangChang HoCH,
pubmed-author:KangKyu YoungKY,
pubmed-author:KimCha YoungCY,
pubmed-author:KimMan LyangML,
pubmed-author:KimSun TaeST,
pubmed-author:KooYoon DuckYD,
pubmed-author:LeeSang YeolSY,
pubmed-author:LeeSo YoungSY,
pubmed-author:MoonByeong CheolBC,
pubmed-author:ParkByung OukBO
|
pubmed:issnType |
Print
|
pubmed:day |
14
|
pubmed:volume |
42
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
11625-33
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:14529272-Amino Acid Motifs,
pubmed-meshheading:14529272-Amino Acid Sequence,
pubmed-meshheading:14529272-Calcium Signaling,
pubmed-meshheading:14529272-Cell Membrane,
pubmed-meshheading:14529272-Cloning, Molecular,
pubmed-meshheading:14529272-Cytosol,
pubmed-meshheading:14529272-Gene Expression Regulation, Plant,
pubmed-meshheading:14529272-Genes, Plant,
pubmed-meshheading:14529272-Genome, Plant,
pubmed-meshheading:14529272-Magnaporthe,
pubmed-meshheading:14529272-Membrane Proteins,
pubmed-meshheading:14529272-Molecular Sequence Data,
pubmed-meshheading:14529272-Oryza sativa,
pubmed-meshheading:14529272-Phospholipids,
pubmed-meshheading:14529272-Plant Diseases,
pubmed-meshheading:14529272-Plant Proteins,
pubmed-meshheading:14529272-Protein Binding,
pubmed-meshheading:14529272-Protein Structure, Tertiary,
pubmed-meshheading:14529272-Protein Transport
|
pubmed:year |
2003
|
pubmed:articleTitle |
Rice C2-domain proteins are induced and translocated to the plasma membrane in response to a fungal elicitor.
|
pubmed:affiliation |
Division of Applied Life Science, Gyeongsang National University, Jinju, Korea.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|