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Titolo:
Sfl1 functions via the co-repressor Ssn6-Tup1 and the cAMP-dependent protein kinase Tpk2
Autore:
Conlan, RS; Tzamarias, D;
Indirizzi:
Fdn Res & Technol Hellas, Inst Mol Biol & Biotechnol, GR-71110 Iraklion, Greece Fdn Res & Technol Hellas Iraklion Greece GR-71110 71110 Iraklion, Greece
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 5, volume: 309, anno: 2001,
pagine: 1007 - 1015
SICI:
0022-2836(20010622)309:5<1007:SFVTCS>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
SACCHAROMYCES-CEREVISIAE; II HOLOENZYME; HEAT-SHOCK; YEAST; GENE; TRANSCRIPTION; EXPRESSION; COMPLEX; GLUCOSE; DOMAIN;
Keywords:
transcription repression; corepressor; cAMP signaling; phosphorylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Conlan, RS Univ Wales, Sch Biol Sci, Singleton Pk, Swansea SA2 8PP, W Glam, Wales Univ Wales Singleton Pk Swansea W Glam Wales SA2 8PP lam, Wales
Citazione:
R.S. Conlan e D. Tzamarias, "Sfl1 functions via the co-repressor Ssn6-Tup1 and the cAMP-dependent protein kinase Tpk2", J MOL BIOL, 309(5), 2001, pp. 1007-1015

Abstract

Ssn6 (Cyc8) is a component of the yeast general corepressor Ssn6-Tup1 thatinhibits the transcription of many diversely regulated genes. The corepressor does not interact directly with DNA but is recruited to different promoters through interactions with distinct pathway-specific, DNA-binding repressor proteins. Using yeast two-hybrid and GST chromatography interaction experiments, we have determined that Sfl1, a novel repressor protein, interacts directly with Ssn6, and in vivo repression data suggest that Sfl1 inhibits transcription by recruiting Ssn6-Tup1 via a specific domain in the Sfl1 protein. Sin4 and Srb10, components of specific RNA polymerase II sub-complexes that are required for Ssn6-Tup1 repression activity, are found to be required for Sfl1 repression function. These results indicate a possible mechanism for Sfl1-mediated repression via Ssn6-Tup1 and specific subunits of the RNA polymerase II holoenzyme. Electrophoretic mobility shift and chromatin immuno-precipitation assays demonstrate that Sfl1 is present at the promoters of three Ssn6-Tup1-repressible genes; namely, FLO11, HSP26, and SUC2. Sfl1 is known to interact with Tpk2, a cAMP-dependent protein kinase thatnegatively regulates Sfl1 function. Consistently, we show that phosphorylation by protein kinase A inhibits Sfl1 DNA binding in vitro, and that a tpk2 Delta mutation increases the levels of Sfl1 protein associated with specific promoter elements in vivo. These data indicate a possible mechanism forregulating Sfl1-mediated repression through modulation of DNA binding by cAMP-dependent protein kinase-dependent phosphorylation. Taken together withprevious data, these new observations suggest a link between cAMP signaling and Ssn6-Tup1-mediated transcriptional repression. (C) 2001 Academic Press.

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Documento generato il 14/08/20 alle ore 17:00:10