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Titolo:
Characterization of Sm-like proteins in yeast and their association with U6 snRNA
Autore:
Mayes, AE; Verdone, L; Legrain, P; Beggs, JD;
Indirizzi:
Univ Edinburgh, Inst Cell & Mol Biol, Edinburgh EH9 3JR, Midlothian, Scotland Univ Edinburgh Edinburgh Midlothian Scotland EH9 3JR Midlothian, Scotland ARN, Lab Metab, Inst Pasteur, F-75724 Paris 15, France ARN Paris France 15 N, Lab Metab, Inst Pasteur, F-75724 Paris 15, France
Titolo Testata:
EMBO JOURNAL
fascicolo: 15, volume: 18, anno: 1999,
pagine: 4321 - 4331
SICI:
0261-4189(19990802)18:15<4321:COSPIY>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
COMPLETE GENOME SEQUENCE; SACCHAROMYCES-CEREVISIAE; FUNCTIONAL-ANALYSIS; CORE PROTEINS; PRP24 BINDING; U1 SNRNP; RNA; IDENTIFICATION; U4; CAP;
Keywords:
Lsm; Sm proteins; snRNP; splicing; U6 snRNP;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Beggs, JD Univ Edinburgh, Inst Cell & Mol Biol, Kings Bldg,Mayfield Rd, Edinburgh EH9 3JR, Midlothian, Scotland Univ Edinburgh Kings Bldg,Mayfield RdEdinburgh Midlothian Scotland EH9 3JR
Citazione:
A.E. Mayes et al., "Characterization of Sm-like proteins in yeast and their association with U6 snRNA", EMBO J, 18(15), 1999, pp. 4321-4331

Abstract

Seven Sm proteins associate with U1, U2, U4 and U5 spliceosomal snRNAs andinfluence snRNP biogenesis. Here we describe a novel set of Sm-like (Lsm) proteins in Saccharomyces cerevisiae that interact with each other and withU6 snRNA, Seven Lsm proteins coimmunoprecipitate with the previously characterized Lsm4p (Uss1p) and interact with each other in two-hybrid analyses. Free U6 and U4/U6 duplexed RNAs co-immunoprecipitate with seven of the Lsmproteins that are essential for the stable accumulation of U6 snRNA, Analyses of U4/U6 di-snRNPs and U4/U6 U5 tri-snRNPs in Lsm-depleted strains suggest that Lsm proteins may play a role in facilitating conformational rearrangements of the U6 snRNP in the association-dissociation cycle of spliceosome complexes. Thus, Lsm proteins form a complex that differs from the canonical Sm complex in its RNA association(s) and function. We discuss the possible existence and functions of alternative Lsm complexes, including the likelihood that they are involved in processes other than pre-mRNA splicing.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:16:31