| Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae. | |
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MedLine Citation:
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PMID: 14756785 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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By sequence analysis we found an amino acid stretch centred on Serine201 matching a stringent CK2 consensus site within the C-terminal, inhibitory domain of Sic1. Here we show by direct mass spectrometry analysis that Sic1, but not a mutant protein whose CK2 phospho-acceptor site has been mutated to alanine, Sic1S201A, is actually phosphorylated in vitro by CK2 on Serine 201. Mutation of Serine 201 alters the coordination between growth and cell cycle progression. A significant increase of average protein content and of the average protein content at the onset of DNA synthesis is observed for exponentially growing cells harbouring the Sic1S201A protein. A strong reduction of the same parameters is observed in cells harbouring Sic1S201E. The deregulated coordination between cell size and cell cycle is also apparent at the level of S-Cdk activity. |
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Authors:
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Paola Coccetti; Riccardo L Rossi; Flora Sternieri; Danilo Porro; Gian Luigi Russo; Andrea di Fonzo; Fulvio Magni; Marco Vanoni; Lilia Alberghina |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular microbiology Volume: 51 ISSN: 0950-382X ISO Abbreviation: Mol. Microbiol. Publication Date: 2004 Jan |
Date Detail:
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Created Date: 2004-02-03 Completed Date: 2004-04-27 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 8712028 Medline TA: Mol Microbiol Country: England |
Other Details:
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Languages: eng Pagination: 447-60 Citation Subset: IM |
Affiliation:
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Dipartimento di Biotecnologie e Bioscienze, Università degli Studi Milano-Bicocca, P. zza della Scienza 2, 20126 Milano, Italy. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Base Sequence Casein Kinase II Cyclin-Dependent Kinase Inhibitor Proteins Cyclin-Dependent Kinases / genetics* Flow Cytometry Genetic Vectors Haploidy Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides / chemistry Plasmids / genetics Protein-Serine-Threonine Kinases / genetics S Phase Saccharomyces cerevisiae / cytology, enzymology*, genetics* Saccharomyces cerevisiae Proteins / genetics* Serine Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| Chemical | |
Reg. No./Substance:
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0/Cyclin-Dependent Kinase Inhibitor Proteins; 0/Oligodeoxyribonucleotides; 0/SIC1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 56-45-1/Serine; EC 2.7.11.1/Casein Kinase II; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.22/Cyclin-Dependent Kinases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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