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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1993-1-7
|
| pubmed:databankReference | |
| pubmed:abstractText |
During the course of characterizing polymerase chain reaction products corresponding to protein kinases of a higher plant, Arabidopsis thaliana, we found a DNA fragment that potentially codes for a polypeptide with mosaic sequences of two classes of protein kinases, a tyrosine-specific and a serine/threonine-specific one. Overlapping complementary DNA (cDNA) clones coinciding with this fragment were isolated from an A. thaliana cDNA library. From their sequence analyses a protein kinase was predicted composed of 410 amino acid residues (APK1, Arabidopsis protein kinase 1), in which the kinase domain was flanked by short non-kinase domains. Upon expression of APK1 in Escherichia coli cells, several bacterial proteins became reactive with anti-phosphotyrosine antibody but not with the same antibody preincubated with phosphotyrosine, convincing us that APK1 phosphorylated tyrosine residues. APK1 purified from an over-producing E. coli strain showed serine/threonine kinase activity, and no tyrosine kinase activity, towards APK1 itself, casein, enolase, and myosin light chains. APK1 was thus concluded to be a novel type of protein kinase, which could phosphorylate tyrosine, serine, and threonine residues, though tyrosine phosphorylation seemed to occur only on limited substrates. Since the structure of the APK1 N-terminal portion was indicative of N-myristoylation, APK1 might associate with membranes and thereby contribute to signal transduction. The A. thaliana genome contained two APK1 genes close to each other (APK1a and APK1b).
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0167-4412
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
20
|
| pubmed:geneSymbol |
APK1a,
APK1b
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
653-62
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1450380-Amino Acid Sequence,
pubmed-meshheading:1450380-Arabidopsis,
pubmed-meshheading:1450380-Arabidopsis Proteins,
pubmed-meshheading:1450380-Base Sequence,
pubmed-meshheading:1450380-Blotting, Southern,
pubmed-meshheading:1450380-Cloning, Molecular,
pubmed-meshheading:1450380-DNA,
pubmed-meshheading:1450380-Escherichia coli,
pubmed-meshheading:1450380-Humans,
pubmed-meshheading:1450380-Immunoblotting,
pubmed-meshheading:1450380-Molecular Sequence Data,
pubmed-meshheading:1450380-Phosphorylation,
pubmed-meshheading:1450380-Protein Kinases,
pubmed-meshheading:1450380-Protein-Serine-Threonine Kinases,
pubmed-meshheading:1450380-Protein-Tyrosine Kinases,
pubmed-meshheading:1450380-Sequence Homology, Amino Acid,
pubmed-meshheading:1450380-Serine,
pubmed-meshheading:1450380-Threonine,
pubmed-meshheading:1450380-Tyrosine
|
| pubmed:year |
1992
|
| pubmed:articleTitle |
Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine, serine and threonine.
|
| pubmed:affiliation |
Laboratory of Molecular Genetics, Institute for Chemical Research, Kyoto University, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|