Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae

Autor: Coccetti P, Rossi RL, Sternieri F, Porro D, Russo GL, Di Fonzo A, Magni F, Vanoni M, Alberghina L.

Publikováno v: Molecular microbiology
51 (2004): 447–460. doi:10.1046/j.1365-2958.2003.03836.x
info:cnr-pdr/source/autori:Coccetti P, Rossi RL, Sternieri F, Porro D, Russo GL, Di Fonzo A, Magni F, Vanoni M, Alberghina L./titolo:Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae./doi:10.1046%2Fj.1365-2958.2003.03836.x/rivista:Molecular microbiology (Print)/anno:2004/pagina_da:447/pagina_a:460/intervallo_pagine:447–460/volume:51

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::7c39f0855eda87864cce98312d40549a
https://publications.cnr.it/doc/45606

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Mutations of the CK2 phosphorylation site of Sic1 affect cell size and S-Cdk kinase activity in Saccharomyces cerevisiae

Autor: Paola, Coccetti, Riccardo L, Rossi, Flora, Sternieri, Danilo, Porro, Gian Luigi, Russo, Andrea, di Fonzo, Fulvio, Magni, Marco, Vanoni, Lilia, Alberghina

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 w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::1331c8aee8c5026b8d2e5953fed8024a
http://hdl.handle.net/10281/614