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Titolo:
Nuclear export factor CRM1 interacts with nonstructural proteins NS2 from parvovirus minute virus of mice
Autore:
Bodendorf, U; Cziepluch, C; Jauniaux, JC; Rommelaere, J; Salome, N;
Indirizzi:
Deutsch Krebsforschungszentrum, Dept Appl Tumor Virol, INSERM, U375,Abt F0100, D-69120 Heidelberg, Germany Deutsch Krebsforschungszentrum Heidelberg Germany D-69120 lberg, Germany
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 9, volume: 73, anno: 1999,
pagine: 7769 - 7779
SICI:
0022-538X(199909)73:9<7769:NEFCIW>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFORMED RAT-CELLS; MURINE CELLS; LEPTOMYCIN-B; AUTONOMOUS PARVOVIRUSES; DNA-REPLICATION; MESSENGER-RNA; REX PROTEIN; BINDING; SIGNAL; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Salome, N Deutsch Krebsforschungszentrum, Dept Appl Tumor Virol, INSERM, U375,Abt F0100, Neuenheimer Feld 242, D-69120 Heidelberg, Germany Deutsch Krebsforschungszentrum Neuenheimer Feld 242 Heidelberg Germany D-69120
Citazione:
U. Bodendorf et al., "Nuclear export factor CRM1 interacts with nonstructural proteins NS2 from parvovirus minute virus of mice", J VIROLOGY, 73(9), 1999, pp. 7769-7779

Abstract

The nonstructural NS2 proteins of autonomous parvoviruses are known to actin a host cell-dependent manner and to play a role in viral DNA replication, efficient translation of viral mRNA, and/or encapsidation. Their exact function during the parvovirus life cycle remains, however, still obscure. We report here the characterization of the interaction with the NS2 proteinsfrom the parvovirus minute virus of mice (MVM) and rat as well as mouse homologues of the human CRM1 protein, a member of the importin-beta family recently identified as an essential nuclear export factor. Using the two-hybrid system, we could detect the interaction between the carboxy-terminal region of rat CRM1 and each of the three isoforms of NS2 (P [or major], Y [or minor], and L [or rare]). NS2 proteins were further shown to interact with the full-length CRM1 by coimmunoprecipitation experiments using extracts from both mouse and rat cell lines. Our data show that CRM1 preferentially binds to the nonphosphorylated isoforms of NS2. Moreover, we observed that the treatment of MVM-infected cells with leptomycin B, a drug that specifically inhibits the CRM1-dependent nuclear export pathway, leads to a drastic accumulation of NS2 proteins in the nucleus. Both NS2 interaction with CRM1 and nuclear accumulation upon leptomycin B treatment strongly suggest that these nonstructural viral proteins are actively exported out of the nuclei of infected cells via a CRM1-mediated nuclear export pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 10:20:25