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Titolo:
Nuclear localization and shuttling of herpes simplex virus tegument protein VP13/14
Autore:
Donnelly, M; Elliott, G;
Indirizzi:
Marie Curie Res Inst, Virus Assembly Grp, Surrey RH8 0TL, England Marie Curie Res Inst Surrey England RH8 0TL Grp, Surrey RH8 0TL, England
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 6, volume: 75, anno: 2001,
pagine: 2566 - 2574
SICI:
0022-538X(200103)75:6<2566:NLASOH>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
REV TRANS-ACTIVATOR; HIV-1 REV; GENE-EXPRESSION; TAT PROTEIN; NUCLEOCYTOPLASMIC TRANSPORT; NUCLEOLAR LOCALIZATION; SEQUENCE REQUIREMENTS; REGULATORY PROTEIN; BINDING-PROTEINS; DELETION MUTANTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Elliott, G Marie Curie Res Inst, Virus Assembly Grp, The Chart, Surrey RH80TL, England Marie Curie Res Inst The Chart Surrey England RH8 0TL England
Citazione:
M. Donnelly e G. Elliott, "Nuclear localization and shuttling of herpes simplex virus tegument protein VP13/14", J VIROLOGY, 75(6), 2001, pp. 2566-2574

Abstract

The herpes simplex virus type 1 gene UL47 encodes the tegument proteins referred to collectively as VP13/14, which are believed to be differentially modified forms of the same protein. Here we show that the major product of the UL47 gene during transient expression is VP14, suggesting that some feature of virus infection is required to produce VP13, We have tagged VP13/14with green fluorescent protein and have demonstrated that the protein is targeted efficiently to the nucleus, where it often localizes in numerous punctate domains. Furthermore, me shaw that removal of the N-terminal 127 residues of the protein abrogates nuclear accumulation, and we have identifieda 14-amino-acid peptide from this region that is sufficient to function asa nuclear targeting signal and transport a heterologous protein to the nucleus, This short peptide contains two runs of four arginine residues, suggesting that the VP13/14 nuclear localization signal may behave in a manner similar to that of the arginine-rich nuclear localization signals of the retrovirus transactivator proteins Tat, Rev, and Rex, In addition, by using heterokaryon assays,,ve show that VP13/14 is capable of shuttling between thenucleus and cytoplasm of the cell, a property that may be attributed to three leucine-rich stretches in the C-terminal half of the protein that againbear similarity to the nuclear export signals of Rev and Rex, This is the first demonstration of a tegument protein that is specifically targeted to the nucleus, a feature which may be relevant both during virus entry, when VP13/14 enters the cell as a component of the tegument, and at later times,when large amounts of newly synthesized VP13/14 are present within the cell.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 04:02:02