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Titolo:
CONSERVATION OF FUNCTIONAL DOMAINS INVOLVED IN RNA-BINDING AND PROTEIN-PROTEIN INTERACTIONS IN HUMAN AND SACCHAROMYCES-CEREVISIAE PRE-MESSENGER-RNA SPLICING FACTOR SF1
Autore:
RAIN JC; RAFI Z; RHANI Z; LEGRAIN P; KRAMER A;
Indirizzi:
UNIV GENEVA,DEPT BIOL CELLULAIRE SCI 3,30 QUAI ERNEST ANSERMET CH-1211 GENEVA 4 SWITZERLAND UNIV GENEVA,DEPT BIOL CELLULAIRE CH-1211 GENEVA 4 SWITZERLAND INST PASTEUR,CNRS,URA 1300,ARN,LAB METAB,DEPT BIOTECHNOL F-75724 PARIS 15 FRANCE
Titolo Testata:
RNA
fascicolo: 5, volume: 4, anno: 1998,
pagine: 551 - 565
SICI:
1355-8382(1998)4:5<551:COFDII>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
SMALL NUCLEAR RIBONUCLEOPROTEIN; FRAGILE-X-SYNDROME; SPLICEOSOME ASSEMBLY PATHWAY; MESSENGER-RNA; KH DOMAIN; BRANCHPOINT SEQUENCE; COILED COILS; FMR-1 GENE; U2 SNRNP; IN-VIVO;
Keywords:
COMMITMENT COMPLEX; KH DOMAIN; MUD2P; SPLICEOSOME ASSEMBLY; 2-HYBRID SYSTEM; U2AF(65);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
84
Recensione:
Indirizzi per estratti:
Citazione:
J.C. Rain et al., "CONSERVATION OF FUNCTIONAL DOMAINS INVOLVED IN RNA-BINDING AND PROTEIN-PROTEIN INTERACTIONS IN HUMAN AND SACCHAROMYCES-CEREVISIAE PRE-MESSENGER-RNA SPLICING FACTOR SF1", RNA, 4(5), 1998, pp. 551-565

Abstract

The modular structure of splicing factor SF1 is conserved from yeast to man and SF1 acts at early stages of spliceosome assembly in both organisms, The hnRNP K homology (KH) domain of human (h) SF1 is the major determinant for RNA binding and is essential for the activity of hSF1 in spliceosome assembly, supporting the view that binding of SF1 to RNA is essential for its function, Sequences N-terminal to the KH domain mediate the interaction between hSF1 and U2AF(65), which binds to the polypyrimidine tract upstream of the 3' splice site, Moreover, yeast (y) SF1 interacts with Mud2p, the presumptive U2AF(65) homologue in yeast, and the interaction domain is conserved in ySF1, The C-terminaldegenerate RRMs in U2AF(65) and Mud2p mediate the association with hSF1 and ySF1, respectively. Analysis of chimeric constructs of hSF1 andySF indicates that the KH domain may serve a similar function in bothsystems, whereas sequences C-terminal to the KH domain are not exchangeable, Thus, these results argue for hSF1 and ySF1, as well as U2AF(65) and Mud2p, being functional homologues.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 15:19:14