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Titolo:
A CRITICAL PROTEOLYTIC CLEAVAGE SITE NEAR THE C-TERMINUS OF THE YEASTRETROTRANSPOSON TY1 GAG PROTEIN
Autore:
MERKULOV GV; SWIDEREK KM; BRACHMANN CB; BOEKE JD;
Indirizzi:
JOHNS HOPKINS UNIV,SCH MED,DEPT MOLEC BIOL & GENET,617 HUNTERIAN BLDG,725 N WOLFE ST BALTIMORE MD 21205 JOHNS HOPKINS UNIV,SCH MED,DEPT MOLEC BIOL & GENET BALTIMORE MD 21205 CITY HOPE NATL MED CTR,BECKMAN RES INST,DIV IMMUNOL DUARTE CA 91010
Titolo Testata:
Journal of virology
fascicolo: 8, volume: 70, anno: 1996,
pagine: 5548 - 5556
SICI:
0022-538X(1996)70:8<5548:ACPCSN>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
VIRUS-LIKE PARTICLES; LINKER INSERTION MUTAGENESIS; SACCHAROMYCES-CEREVISIAE; ELEMENT TRANSPOSITION; REVERSE-TRANSCRIPTASE; INTERMEDIATE; MUTATIONS; OCCURS; RNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
G.V. Merkulov et al., "A CRITICAL PROTEOLYTIC CLEAVAGE SITE NEAR THE C-TERMINUS OF THE YEASTRETROTRANSPOSON TY1 GAG PROTEIN", Journal of virology, 70(8), 1996, pp. 5548-5556

Abstract

Cleavage of the Gag and Gag-Pol polyprotein precursors is a critical step in proliferation of retroviruses and retroelements. The Ty1 retroelement of Saccharomyces cerevisiae forms virus-like particles (VLPs) made of the Gag protein. Ty1 Gag is not obviously homologous to the Gag proteins of retroviruses. The apparent molecular mass of Gag is reduced from 58 to 54 kDa during particle maturation. Antibodies raised against the C-terminal peptide of Gag react with the 58-kDa polypeptide but not with the 54-kDa one, indicating that Gag is proteolytically processed at the C terminus. A protease cleavage site between positions 401 and 402 of the Gag precursor was defined by carboxy-terminal sequencing of the processed form of Gag. Certain deletion and substitution mutations in the C terminus of the Gag precursor result in particles that are two-thirds the diameter of the wild-type VLPs, While the Ty1 protease is active in these mutants, their transposition rates are decreased 20 fold compared with that of wild-type Ty1. Thus, the Gag C-terminal portion, released in the course of particle maturation, probablyplays a significant role in VLP morphogenesis and Ty1 transposition.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:27:49