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Titolo:
Interactions and nuclear import of the N and P proteins of sonchus yellow net virus, a plant nucleorhabdovirus
Autore:
Goodin, MM; Austin, J; Tobias, R; Fujita, M; Morales, C; Jackson, AO;
Indirizzi:
Univ Calif Berkeley, Dept Plant & Microbial Biol, Berkeley, CA 94720 USA Univ Calif Berkeley Berkeley CA USA 94720 al Biol, Berkeley, CA 94720 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 19, volume: 75, anno: 2001,
pagine: 9393 - 9406
SICI:
0022-538X(200110)75:19<9393:IANIOT>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
VESICULAR STOMATITIS-VIRUS; NUCLEOCAPSID PROTEIN; PHOSPHOPROTEIN-P; 2-HYBRID SYSTEM; SACCHAROMYCES-CEREVISIAE; SUBCELLULAR-LOCALIZATION; COILED COILS; LIVING CELLS; GENE; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Jackson, AO Univ Calif Berkeley, Dept Plant & Microbial Biol, 111 KoshlandHall, Berkeley, CA 94720 USA Univ Calif Berkeley 111 Koshland Hall Berkeley CA USA 94720 SA
Citazione:
M.M. Goodin et al., "Interactions and nuclear import of the N and P proteins of sonchus yellow net virus, a plant nucleorhabdovirus", J VIROLOGY, 75(19), 2001, pp. 9393-9406

Abstract

We have characterized the interaction and nuclear localization of the nucleocapsid (N) protein and phosphoprotein (P) of sonchus yellow net nucleorhabdovirus. Expression studies with plant and yeast cells revealed that both N and P are capable of independent nuclear import. Site-specific mutagenesis and deletion analyses demonstrated that N contains a carboxy-terminal bipartite nuclear localization signal (NLS) located between amino acids 465 and 481 and that P contains a karyophillic region between amino acids 40 and 124. The N NLS was fully capable of functioning outside of the context of the N protein and was able to direct the nuclear import of a synthetic protein fusion consisting of green fluorescent protein fused to glutathione S-transferase (GST). Expression and mapping studies suggested that the karyophillic domain in P is located within the N-binding domain. Coexpression of N and P drastically affected their localization patterns relative to those ofindividually expressed proteins and resulted in a shift of both proteins to a subnuclear region. Yeast two-hybrid and GST pulldown experiments verified the N-P and P-P interactions, and deletion analyses have identified the N and P interacting domains. N NLS mutants were not transported to the nucleus by import-competent P, presumably because N binding masks the P NLS. Taken together, our results support a model for independent entry of N and P into the nucleus followed by associations that mediate subnuclear localization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 06:33:21