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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1997-10-6
|
| pubmed:databankReference | |
| pubmed:abstractText |
Three types of Arabidopsis cDNA (cANP1, cANP2 and cANP3) have been isolated that encode putative protein kinases, designated ANP1, ANP2 and ANP3. These kinases exhibit a high degree of homology to NPK1, a tobacco protein that is a member of the family of mitogen-activated protein kinase kinase kinases (MAPKKKs), which appears to function in the proliferation of tobacco cells. The predicted amino acid sequences of the kinase domains in the amino-terminal halves of the ANPs were more than 80% identical to that of NPK1, while the kinase-unrelated regions in the carboxy-terminal halves exhibited relatively low homology. Two species of cANP1 were identified, ANP1L cDNA (cANP1L) and ANP1S cDNA (cANP1S), which were derived from a single ANP1 gene: the former had an intron-like sequence in the coding region for the kinase-unrelated region, while the latter did not include such an intron-like sequence. cANP1L encoded a putative protein with both kinase and kinase-unrelated domains, resembling NPK1, whereas cANP1S encoded only the amino-terminal kinase domain because the intron-like sequence was absent, with resulting elimination of most of the kinase-unrelated region. Genetic analysis with mutant yeast cells showed that over-expression of cANP1L or of cANP1S activated the mating pheromone-responsive signal pathway which is mediated by a MAP kinase cascade. Moreover, the extent of such activation by cANP1S was greater than that by cANP1L. These results predict that differential splicing of the intron-like sequence in the ANP1 transcript might be at least one of the molecular mechanisms involved in the generation of active ANP1 protein kinase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0960-7412
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
12
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
39-48
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9263451-Alternative Splicing,
pubmed-meshheading:9263451-Amino Acid Sequence,
pubmed-meshheading:9263451-Arabidopsis,
pubmed-meshheading:9263451-Base Sequence,
pubmed-meshheading:9263451-Cloning, Molecular,
pubmed-meshheading:9263451-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9263451-Gene Expression Regulation, Plant,
pubmed-meshheading:9263451-Genes, Plant,
pubmed-meshheading:9263451-MAP Kinase Kinase Kinases,
pubmed-meshheading:9263451-Molecular Sequence Data,
pubmed-meshheading:9263451-Plants, Toxic,
pubmed-meshheading:9263451-Protein Kinases,
pubmed-meshheading:9263451-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9263451-Recombinant Proteins,
pubmed-meshheading:9263451-Sequence Alignment,
pubmed-meshheading:9263451-Sequence Homology, Amino Acid,
pubmed-meshheading:9263451-Tobacco,
pubmed-meshheading:9263451-Transcription, Genetic
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
Possible involvement of differential splicing in regulation of the activity of Arabidopsis ANP1 that is related to mitogen-activated protein kinase kinase kinases (MAPKKKs).
|
| pubmed:affiliation |
Division of Biological Science, Graduate School of Science, Nagoya University, Japan.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|