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Titolo:
MOLECULAR-CLONING AND CHARACTERIZATION OF A CELLULAR PHOSPHOPROTEIN THAT INTERACTS WITH A CONSERVED C-TERMINAL DOMAIN OF ADENOVIRUS E1A INVOLVED IN NEGATIVE MODULATION OF ONCOGENIC TRANSFORMATION
Autore:
SCHAEPER U; BOYD JM; VERMA S; UHLMANN E; SUBRAMANIAN T; CHINADURAI G;
Indirizzi:
ST LOUIS UNIV,MED CTR,INST MOLEC VIROL,3681 PK AVE ST LOUIS MO 63110 ST LOUIS UNIV,MED CTR,INST MOLEC VIROL ST LOUIS MO 63110
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 23, volume: 92, anno: 1995,
pagine: 10467 - 10471
SICI:
0027-8424(1995)92:23<10467:MACOAC>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PRIMARY EPITHELIAL-CELLS; D-LACTATE DEHYDROGENASE; RAT EMBRYO CELLS; ESCHERICHIA-COLI; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; LACTOBACILLUS-PLANTARUM; PROTEIN; GENE; EXPRESSION; REGION;
Keywords:
2-HYBRID ANALYSIS; TUMORIGENESIS; DEHYDROGENASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
U. Schaeper et al., "MOLECULAR-CLONING AND CHARACTERIZATION OF A CELLULAR PHOSPHOPROTEIN THAT INTERACTS WITH A CONSERVED C-TERMINAL DOMAIN OF ADENOVIRUS E1A INVOLVED IN NEGATIVE MODULATION OF ONCOGENIC TRANSFORMATION", Proceedings of the National Academy of Sciences of the United Statesof America, 92(23), 1995, pp. 10467-10471

Abstract

The adenovirus type 2/5 EIA proteins transform primary baby rat kidney (BRK) cells in cooperation with the activated Ras (T24 ras) oncoprotein. The N-terminal half of E1A (exon 1) is essential for this transformation activity. While the C-terminal half of E1A (exon 2) is dispensable, a region located between residues 225 and 238 of the 243R E1A protein negatively modulates in vitro T24 ras cooperative transformationas well as the tumorigenic potential of E1A/T24 ras-transformed cells. The same C-terminal domain is also required for binding of a cellular 48-kDa phosphoprotein, C-terminal binding protein (CtBP). We have cloned the cDNA for CtBP via yeast two-hybrid interaction cloning. The cDNA encodes a 439-amino acid (48 kDa) protein that specifically interacts with exon 2 in yeast two-hybrid, in vitro protein binding, and in vivo coimmunoprecipitation analyses. This protein requires residues 225-238 of the 243B E1A protein for interaction. The predicted protein sequence of the isolated cDNA is identical to amino acid sequences obtained from peptides prepared from biochemically purified CtBP. Fine mapping of the CtBP-binding domain revealed that a 6-amino acid motif highly conserved among the ELA proteins of various human and animal adenoviruses is required for this interaction. These results suggest that interaction of CtBP with the E1A proteins may play a critical role in adenovirus replication and oncogenic transformation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:31:01