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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1997-1-7
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pubmed:abstractText |
ran1+ (pat1+) kinase inhibits exit from the mitotic cell cycle and entry into meiosis. Inactivation of ran1+ by mei3+ is sufficient to precipitate the entire meiotic developmental program. Here, we show that the ste11+ transcription factor is a substrate for ran1+ in vitro and that this reaction is directly inhibited by mei3+. Sequence comparison reveals that ste11+ contains two domains homologous to each other and to a domain of mei3+. Mutagenesis studies reveal that the regions of homology contain substrate specificity determinants. These results identify sequences critical for phosphorylation of ste11+ by ran1+ and suggest that mei3+ employs a pseudosubstrate mechanism for its inhibitory function.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MEI-3 protein, Neurospora crassa,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ran GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/ste11 protein, S pombe
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
869-80
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8945514-Alanine,
pubmed-meshheading:8945514-Arginine,
pubmed-meshheading:8945514-Aspartic Acid,
pubmed-meshheading:8945514-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:8945514-DNA Mutational Analysis,
pubmed-meshheading:8945514-Enzyme Inhibitors,
pubmed-meshheading:8945514-Fungal Proteins,
pubmed-meshheading:8945514-GTP Phosphohydrolases,
pubmed-meshheading:8945514-GTP-Binding Proteins,
pubmed-meshheading:8945514-Meiosis,
pubmed-meshheading:8945514-Mutagenesis, Site-Directed,
pubmed-meshheading:8945514-Nuclear Proteins,
pubmed-meshheading:8945514-Phosphorylation,
pubmed-meshheading:8945514-Schizosaccharomyces,
pubmed-meshheading:8945514-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:8945514-Sequence Homology, Amino Acid,
pubmed-meshheading:8945514-Serine,
pubmed-meshheading:8945514-Substrate Specificity,
pubmed-meshheading:8945514-Transcription Factors,
pubmed-meshheading:8945514-ran GTP-Binding Protein
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pubmed:year |
1996
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pubmed:articleTitle |
Molecular mimicry in development: identification of ste11+ as a substrate and mei3+ as a pseudosubstrate inhibitor of ran1+ kinase.
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pubmed:affiliation |
Department of Microbiology and Immunology, Morse Institute for Molecular Biology and Genetics, State University of New York Health Science Center at Brooklyn 11023, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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