Document Detail


Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae.
MedLine Citation:
PMID:  14756785     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
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:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular microbiology     Volume:  51     ISSN:  0950-382X     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2004 Jan 
Date Detail:
Created Date:  2004-02-03     Completed Date:  2004-04-27     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  447-60     Citation Subset:  IM    
Affiliation:
Dipartimento di Biotecnologie e Bioscienze, Università degli Studi Milano-Bicocca, P. zza della Scienza 2, 20126 Milano, Italy.
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MeSH Terms
Descriptor/Qualifier:
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:
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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