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Titolo:
THE BPV-1 E2 DNA-CONTACT HELIX CYSTEINE IS REQUIRED FOR TRANSCRIPTIONAL ACTIVATION BUT NOT REPLICATION IN MAMMALIAN-CELLS
Autore:
GROSSEL MJ; BARSOUM J; PRAKASH SS; ANDROPHY EJ;
Indirizzi:
TUFTS UNIV NEW ENGLAND MED CTR,DEPT DERMATOL,750 WASHINGTON ST,BOX 166 BOSTON MA 02111 TUFTS UNIV NEW ENGLAND MED CTR,DEPT DERMATOL BOSTON MA 02111 TUFTS UNIV,SCH MED,DEPT MOLEC BIOL & MICROBIOL BOSTON MA 02111 BIOGEN INC CAMBRIDGE MA 02142
Titolo Testata:
Virology
fascicolo: 1, volume: 217, anno: 1996,
pagine: 301 - 310
SICI:
0042-6822(1996)217:1<301:TBEDHC>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
BINDING ACTIVITY INVITRO; BOVINE PAPILLOMAVIRUS; SACCHAROMYCES-CEREVISIAE; RECOGNITION SEQUENCE; REDOX REGULATION; TRANS-ACTIVATOR; TERMINAL DOMAIN; E1 PROTEIN; E2-PROTEIN; ORIGIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
M.J. Grossel et al., "THE BPV-1 E2 DNA-CONTACT HELIX CYSTEINE IS REQUIRED FOR TRANSCRIPTIONAL ACTIVATION BUT NOT REPLICATION IN MAMMALIAN-CELLS", Virology, 217(1), 1996, pp. 301-310

Abstract

The papillomavirus E2 protein contains an amino-terminal region thought necessary and sufficient to support transcriptional activation and a carboxy-terminal region shown to direct sequence-specific DNA binding and dimerization. A cysteine residue in the center of the E2 DNA recognition helix is highly conserved among papillomavirus E2 proteins. Mutations of this cysteine in bovine papillomavirus type 1 E2 to serineand glycine resulted in proteins which failed to activate E2-dependent promoters in mammalian cells. These E2 mutants were DNA-binding competent, dimeric, and nuclear. When fused to the VP16 transactivation domain, C-terminal regions of E2 containing the mutations at 340 supported transcriptional activation, indicating that the heterologous Irans-activation domain did not require cysteine in the DNA-binding helix asdid the full-length E2 transactivating protein. Although cysteine-340was required for transcriptional activation it was not required for DNA replication in vivo. Together, these results suggest that the E2 DNA-binding domain may directly contribute to functions of transcriptional activation previously thought limited to the N-terminal domain. (C)1996 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 06:30:10