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Titolo:
GENETIC AND BIOCHEMICAL-EVIDENCE THAT EBNA-2 INTERACTION WITH A 63-KDA CELLULAR GTG-BINDING PROTEIN IS ESSENTIAL FOR B-LYMPHOCYTE GROWTH TRANSFORMATION BY EBV
Autore:
YALAMANCHILI R; TONG X; GROSSMAN S; JOHANNSEN E; MOSIALOS G; KIEFF E;
Indirizzi:
HARVARD UNIV,SCH MED,DEPT MICROBIOL & MOLEC GENET,THORN-12,75 FRANCISST BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT MICROBIOL & MOLEC GENET BOSTON MA 02115 HARVARD UNIV,SCH MED,DEPT MED BOSTON MA 02115
Titolo Testata:
Virology
fascicolo: 2, volume: 204, anno: 1994,
pagine: 634 - 641
SICI:
0042-6822(1994)204:2<634:GABTEI>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPSTEIN-BARR-VIRUS; LATENT MEMBRANE-PROTEIN; BAMHI C-PROMOTER; NUCLEAR ANTIGEN-2; BURKITTS-LYMPHOMA; EXPRESSION; ELEMENT; CD23; TRANSACTIVATION; TRANSCRIPTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
R. Yalamanchili et al., "GENETIC AND BIOCHEMICAL-EVIDENCE THAT EBNA-2 INTERACTION WITH A 63-KDA CELLULAR GTG-BINDING PROTEIN IS ESSENTIAL FOR B-LYMPHOCYTE GROWTH TRANSFORMATION BY EBV", Virology, 204(2), 1994, pp. 634-641

Abstract

Epstein-Barr virus (EBV) nuclear protein 2 (EBNA 2) is an acidic transcriptional transactivator of virus and cell gene expression and is essential for growth transformation of primary a lymphocytes. EBNA 2 transactivation of response elements (E2REs) can be mediated by interaction with a GTGGGAA-specific DNA-binding factor(s). We now purify the factor by S-sepharose and EBNA 2 affinity chromatography and identify itas a single 63-kDa protein. The protein is shown to specifically coimmunoprecipitate with EBNA 2 from lymphoblasts transfected with an EBNA2 FLAG expression vector. Mutation of GTG to TCT in a GTGGGAA motif common to the Cp, LMP2, and LMP1 promoters results in loss of recognition by p63. EBNA 2 amino acids 310-336 are sufficient for p63 binding. The only motif in this 27 amino acid sequence which is common to the EBNA 2 genes of EBV types 1 and 2 is GPPWWPP (IN) (C/R) DP, which is therefore likely to mediate p63 interaction. Mutation of WW to SS or FF ablates interaction with p63, indicating that both the hydrophobic andaromatic characteristics of WW are essential for its ''key'' interaction with p63. EBNA 2 with a WW mutated to SS is also unable to marker rescue primary a lymphocyte transforming virus from cells infected with an EBNA 2-deleted virus, while otherwise isogeneic wild-type EBNA 2 readily marker rescues transforming virus in parallel experiments. EBNA 2 transactivation through the Cp E2RE is completely abolished by theWW to SS mutation while transactivation of -234 to +40 LMP1 E2RE is only partially affected. These genetic and biochemical experiments support the hypothesis that EBNA 2 WW interaction with a p63 GTGGGAA-binding protein is essential for EBV-mediated cell growth transformation because it specifically associates EBNA 2 with its response elements. This enables the EBNA 2 acidic domain to transcriptionally transactivatespecific genes. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 11:05:04