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Titolo:
FUNCTIONAL CONSERVATION OF THE TRANSPORTIN NUCLEAR IMPORT PATHWAY IN DIVERGENT ORGANISMS
Autore:
SIOMI MC; FROMONT M; RAIN JC; WAN LL; WANG F; LEGRAIN P; DREYFUSS G;
Indirizzi:
UNIV PENN,SCH MED,HOWARD HUGHES MED INST PHILADELPHIA PA 19104 UNIV PENN,SCH MED,HOWARD HUGHES MED INST PHILADELPHIA PA 19104 UNIV PENN,SCH MED,DEPT BIOCHEM & BIOPHYS PHILADELPHIA PA 19104 INST PASTEUR,LAB METAB ARN,CNRS,URA 1300 F-75724 PARIS FRANCE
Titolo Testata:
Molecular and cellular biology
fascicolo: 7, volume: 18, anno: 1998,
pagine: 4141 - 4148
SICI:
0270-7306(1998)18:7<4141:FCOTTN>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-BINDING-PROTEINS; MESSENGER-RNA; HNRNP PROTEINS; A1; LOCALIZATION; SEQUENCES; EXPORT; SPECIFICITY; RECEPTOR; SIGNAL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
M.C. Siomi et al., "FUNCTIONAL CONSERVATION OF THE TRANSPORTIN NUCLEAR IMPORT PATHWAY IN DIVERGENT ORGANISMS", Molecular and cellular biology, 18(7), 1998, pp. 4141-4148

Abstract

Human transportin1 (hTRN1) is the nuclear import receptor for a groupof pre-mRNA/mRNA-binding proteins (heterogeneous nuclear ribonucleoproteins [hnRNP]) represented by hnRNP A1, which shuttle continuously between the nucleus and the cytoplasm. hTRN1. interacts with the M9 region of hnRNP A1, a 38-amino-acid domain rich in Gly, Ser, and Asn, and mediates the nuclear import of M9-bearing proteins in vitro. Saccharomyces cerevisiae transportin (yTRN; also known as YBR017c or Kap104p) has been identified and cloned. To understanding the nuclear import mediated by yTRN, we searched with a yeast two-hybrid system for proteinsthat interact with it. In an exhaustive screen of the S. cerevisiae genome, the most frequently selected open reading frame was the nuclearmRNA-binding protein, Nab2p. We delineated a ca.50-amino-acid region in Nab2p, termed NAB35, which specifically binds yTRN and is similar to the M9 motif. NAB35 also interacts with hTRN1 and functions as a nuclear localization signal in mammalian cells. Interestingly, yTRN can also mediate the import of NAB35-bearing proteins into mammalian nucleiin vitro. We also report on additional substrates for TRN as well as sequences of Drosophila melanogaster, Xenopus laevis, and Schizosaccharomyces pombe TRNs. Together, these findings demonstrate that both theM9 signal and the nuclear import machinery utilized by the transportin pathway are conserved in evolution.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:42:51