Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-2-20
pubmed:abstractText
While considerable progress has been achieved in plant CDPK studies in the past decade, there is relatively no information about the potential substrates of CRKs. In this report, a yeast two-hybrid screen was performed with truncated form of AtCRK3 as bait to identify its interacting proteins in an effort to dissect its physiological roles. One gene encoding cytosolic glutamine synthetase AtGLN1;1 was isolated. Further analyses indicated that AtGLN1;1 could interact specifically with AtCRK3 and the kinase domain of AtCRK3 and the catalytic domain of AtGLN1;1 were responsible for such interaction, respectively. Furthermore, in vitro and in vivo co-immunoprecipitation results strongly supported that they could physically interact with each other. Phosphorylation assays revealed that AtGLN1;1 could be specifically phosphorylated by AtCRK3 in vitro. All the results demonstrate that AtGLN1;1 may be a substrate of AtCRK3. In addition, both AtGLN1;1 and AtCRK3 could be induced by natural or artificially induced leaf senescence, implying that such interaction may be involved in the regulation of nitrogen remobilization during leaf senescence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
342
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
119-26
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Arabidopsis cytosolic glutamine synthetase AtGLN1;1 is a potential substrate of AtCRK3 involved in leaf senescence.
pubmed:affiliation
Key Laboratory of MOE for Plant Developmental Biology, College of Life Sciences, Wuhan University, Wuhan 430072, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't