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Titolo:
ESSENTIAL DOMAINS OF THE PRP21 SPLICING FACTOR ARE IMPLICATED IN THE BINDING TO PRP9 AND PRP11 PROTEINS AND ARE CONSERVED THROUGH EVOLUTION
Autore:
RAIN JC; TARTAKOFF AM; KRAMER A; LEGRAIN P;
Indirizzi:
INST PASTEUR,DEPT BIOTECHNOL,CNRS,URA 1149,LAB METAB ARN,28 RUE DR ROUX F-75724 PARIS 15 FRANCE INST PASTEUR,DEPT BIOTECHNOL,CNRS,URA 1149,LAB METAB ARN F-75724 PARIS 15 FRANCE CASE WESTERN RESERVE UNIV,INST PATHOL CLEVELAND OH 44106 CASE WESTERN RESERVE UNIV,CELL BIOL PROGRAM CLEVELAND OH 44106 UNIV GENEVA,DEPT BIOL CELLULAIRE CH-1211 GENEVA 4 SWITZERLAND
Titolo Testata:
RNA
fascicolo: 6, volume: 2, anno: 1996,
pagine: 535 - 550
SICI:
1355-8382(1996)2:6<535:EDOTPS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRE-MESSENGER-RNA; SMALL NUCLEAR RIBONUCLEOPROTEIN; U2 SNRNP BINDING; SACCHAROMYCES-CEREVISIAE; YEAST PRP9; COMPLEX; PRESPLICEOSOME; COMMITMENT; COMPONENTS; SEQUENCE;
Keywords:
MUTAGENIC PCR; PLASMID SHUFFLING; SURP MODULE; 2-HYBRID; YEAST;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
J.C. Rain et al., "ESSENTIAL DOMAINS OF THE PRP21 SPLICING FACTOR ARE IMPLICATED IN THE BINDING TO PRP9 AND PRP11 PROTEINS AND ARE CONSERVED THROUGH EVOLUTION", RNA, 2(6), 1996, pp. 535-550

Abstract

The yeast Prp9p, Prp11p, Prp21p proteins form a multimolecular complex identified as the SF3a splicing factor in higher eukaryotes, This factor is required for the assembly of the prespliceosome. Prp21p interacts with both Prp9p and Prp11p, but the molecular basis of these interactions is unknown. Prp21p, its human homologue, and the so-called SWAP proteins share a tandemly repeated motif, the surp module, Given theevolutionary conservation and the role of SWAP proteins as splicing regulators, it has been proposed that surp motifs are essential for interactions between Prp21p and other splicing factors, In order to characterize functional domains of Prp21p and to identify potential additional functions of this protein, we isolated a series of heat-sensitive prp21 mutants. Our results indicate that prp21 heat-sensitive mutations are associated with defects in the interaction with Prp9p, but not with Prp11p, Interestingly, most heat-sensitive point mutants associatea strong splicing defect with a pre-mRNA nuclear export phenotype, asdoes the prp9-1 heat-sensitive mutant, Deletion analyses led to the definition of domains required for viability, These domains are responsible for the interaction with Prp9p and Prp11p and are conserved through evolution, They do not include the most conserved surp1 module, suggesting that the conservation of this motif in two families of proteins may reflect a still unknown function dispensable in yeast under standard conditions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 13:29:43