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Titolo:
Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirusmRNAs
Autore:
Bear, J; Tan, W; Zolotukhin, AS; Tabernero, C; Hudson, EA; Felber, BK;
Indirizzi:
NCI, Human Retrovirus Pathogenesis Sect, ABL Basic Res Program, Frederick Canc Res & Dev Ctr, Frederick, MD 21702 USA NCI Frederick MD USA 21702 ck Canc Res & Dev Ctr, Frederick, MD 21702 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 9, volume: 19, anno: 1999,
pagine: 6306 - 6317
SICI:
0270-7306(199909)19:9<6306:IONIAE>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; MESSENGER-RNA EXPORT; MEDIATED POSTTRANSCRIPTIONAL REGULATION; REV ACTIVATION DOMAIN; NUCLEAR EXPORT; LEPTOMYCIN-B; HNRNP A1; SECONDARY STRUCTURE; GENE-PRODUCT; I REX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Felber, BK NCI, Human Retrovirus Pathogenesis Sect, ABL Basic Res Program,Frederick Canc Res & Dev Ctr, Bldg 535,Rm 110, Frederick, MD 21702 USA NCIBldg 535,Rm 110 Frederick MD USA 21702 derick, MD 21702 USA
Citazione:
J. Bear et al., "Identification of novel import and export signals of human TAP, the protein that binds to the constitutive transport element of the type D retrovirusmRNAs", MOL CELL B, 19(9), 1999, pp. 6306-6317

Abstract

The nuclear export of the unspliced type D retrovirus mRNA depends on the cis-acting constitutive transport RNA element (CTE) that has been shown to interact with the human TAP (hTAP) protein promoting the export of the CTE-containing mRNAs. We report here that hTAP is a 619-amino-acid protein extending the previously identified protein by another 60 residues at the N terminus and that hTAP shares high homology with the predicted rat and mouse TAP proteins. We found that hTAP is a nuclear protein that accumulates in the nuclear rim and the nucleoplasm. We further demonstrated that hTAP is able to shuttle between the nucleus and the cytoplasm. Identification of the signals responsible for nuclear import (NLS) and export (NES) revealed that they are distinct but partially overlapping. NLS and NES of hTAP are activetransferable signals that do not share similarities with known elements. The C-terminal portion contributes further to hTAP's nuclear retention and contains a signal(s) for nuclear rim association. Taken together, our data show that hTAP is a dynamic protein capable of bidirectional trafficking across the nuclear envelope. These data further support hTAP's role as an export factor of the CTE-containing mRNAs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 04:20:33