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Titolo:
Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins
Autore:
Fromont-Racine, M; Mayes, AE; Brunet-Simon, A; Rain, JC; Colley, A; Dix, I; Decourty, L; Joly, N; Ricard, F; Beggs, JD; Legrain, P;
Indirizzi:
Inst Pasteur, CNRS URA 1300, F-75724 Paris 15, France Inst Pasteur ParisFrance 15 ur, CNRS URA 1300, F-75724 Paris 15, France Univ Edinburgh, Inst Cell & Mol Biol, Edinburgh EH9 3JR, Midlothian, Scotland Univ Edinburgh Edinburgh Midlothian Scotland EH9 3JR Midlothian, Scotland Inst Pasteur, Serv Informat Sci, F-75724 Paris 15, France Inst Pasteur Paris France 15 Serv Informat Sci, F-75724 Paris 15, France
Titolo Testata:
YEAST
fascicolo: 2, volume: 17, anno: 2000,
pagine: 95 - 110
SICI:
0749-503X(20000630)17:2<95:GPISRF>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR RIBONUCLEOPROTEIN PARTICLE; RNA-POLYMERASE-III; SACCHAROMYCES-CEREVISIAE; U6 SNRNA; CORE PROTEINS; PRP24 BINDING; TRI-SNRNP; YEAST; U4; IDENTIFICATION;
Keywords:
two-hybrid; splicing; mRNA degradation; yeast; proteome; snRNP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
58
Recensione:
Indirizzi per estratti:
Indirizzo: Legrain, P Inst Pasteur, CNRS URA 1300, 25-28 Rue Dr Roux, F-75724 Paris 15, France Inst Pasteur 25-28 Rue Dr Roux Paris France 15 aris 15, France
Citazione:
M. Fromont-Racine et al., "Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins", YEAST, 17(2), 2000, pp. 95-110

Abstract

A set of seven structurally related Sm proteins forms the core of the snRNP particles containing the spliceosomal U1, U2, U4 and U5 snRNAs, A search of the genomic sequence of Saccharomyces cerevisiae has identified a numberof open reading frames that potentially encode structurally similar proteins termed Lsm (Like Sm) proteins. With the aim of analysing all possible interactions between the Lsm proteins and any protein encoded in the yeast genome, we performed exhaustive and iterative genomic two-hybrid screens, starting with the Lsm proteins as baits. Indeed, extensive interactions amongst eight Lsm proteins were found that suggest the existence of a Lsm complexor complexes, These Lsm interactions apparently involve the conserved Sm domain that also mediates interactions between the Sm proteins. The screens also reveal functionally significant interactions with splicing factors, inparticular with Prp4 and Prp24, compatible with genetic studies and with the reported association of Lsm proteins with spliceosomal U6 and U4/U6 particles. In addition, interactions with proteins involved in mRNA turnover, such as Mrt1, Dcp1, Dcp2 and Xrn1, point to roles for Lsm complexes in distinct RNA metabolic processes, that are confirmed in independent functional studies. These results provide compelling evidence that two-hybrid screens yield functionally meaningful information about protein-protein interactionsand can suggest functions for uncharacterized proteins, especially when they are performed on a genome-wide scale. Copyright (C) 2000 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 16:32:53