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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 |
2001-3-12
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pubmed:abstractText |
As part of a nutrient-responsive signaling pathway, the budding yeast cyclin-CDK complex Pho80-Pho85 phosphorylates the transcription factor Pho4 on five sites and inactivates it. Here, we describe the kinetic reaction between Pho80-Pho85 and Pho4. Through experimentation and computer modeling we have determined that Pho80-Pho85 phosphorylates Pho4 in a semi-processive fashion that results from a balance between kcat and k(off). In addition, we show that Pho80-Pho85 phosphorylates certain sites preferentially. Phosphorylation of the site with the highest preference inhibits the transcriptional activity of Pho4 when it is in the nucleus, while phosphorylation of the lowest-preference sites is required for export of Pho4 from the nucleus. This method of phosphorylation may allow Pho80-Pho85 to quickly inactivate Pho4 in the nucleus and efficiently phosphorylate Pho4 to completion.
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pubmed:grant |
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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/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PHO4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/PHO80 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/PHO85 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
306
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
997-1010
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11237614-Binding Sites,
pubmed-meshheading:11237614-Computer Simulation,
pubmed-meshheading:11237614-Cyclin-Dependent Kinases,
pubmed-meshheading:11237614-Cyclins,
pubmed-meshheading:11237614-DNA-Binding Proteins,
pubmed-meshheading:11237614-Dipeptides,
pubmed-meshheading:11237614-Escherichia coli,
pubmed-meshheading:11237614-Fungal Proteins,
pubmed-meshheading:11237614-Mutation,
pubmed-meshheading:11237614-Phosphorylation,
pubmed-meshheading:11237614-Recombinant Proteins,
pubmed-meshheading:11237614-Repressor Proteins,
pubmed-meshheading:11237614-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11237614-Substrate Specificity,
pubmed-meshheading:11237614-Transcription Factors,
pubmed-meshheading:11237614-Trypsin
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pubmed:year |
2001
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pubmed:articleTitle |
Multi-site phosphorylation of Pho4 by the cyclin-CDK Pho80-Pho85 is semi-processive with site preference.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA 94143, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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