Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae. (Articolo in rivista)

Type
Label
  • Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae. (Articolo in rivista) (literal)
Anno
  • 2004-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1046/j.1365-2958.2003.03836.x (literal)
Alternative label
  • Coccetti P, Rossi RL, Sternieri F, Porro D, Russo GL, Di Fonzo A, Magni F, Vanoni M, Alberghina L. (2004)
    Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae.
    in Molecular microbiology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Coccetti P, Rossi RL, Sternieri F, Porro D, Russo GL, Di Fonzo A, Magni F, Vanoni M, Alberghina L. (literal)
Pagina inizio
  • 447 (literal)
Pagina fine
  • 460 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • L'articolo è open access su: http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2958.2003.03836.x/pdf (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 51 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 2 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biotecnologie e Bioscienze, Università degli Studi Milano-Bicocca Dipartimento di Medicina Sperimentale, Ambientale e Biotecnologie Mediche, Università degli Studi Milano Bicocca Istituto di Scienze dell'Alimentazione, CNR, Avellino (literal)
Titolo
  • Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae. (literal)
Abstract
  • By sequence analysis we found an amino acid stretch centred on Serine 201 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, Sic1 S201A , 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 Sic1 S201A protein. A strong reduction of the same parameters is observed in cells harbouring Sic1 S201E . The deregulated coordination between cell size and cell cycle is also apparent at the level of SCdk activity. (literal)
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