In vitro analysis of the E1A-homologous sequences of RIZ.

La Jolla Cancer Research Center, Burnham Institute, California 92037, USA.
The RIZ (G3B/MTB-Zf) gene was first isolated based on its ability to bind to the retinoblastoma protein (Rb). An acidic, approximately 100-amino-acid region around the Rb-binding motif of RIZ has structural and antigenic similarity to the conserved sequences of the E1A viral oncogene. We show here that this region interacts specifically with the E1A-binding domain of Rb. This interaction could be disrupted by E1A or by a peptide of RIZ homologous to the CR2 motif of E1A which is involved in binding to Rb family proteins. Also like E1A, RIZ can form a ternary complex with Rb and E2F1. Despite this similarity to E1A, however, RIZ could not bind to the Rb family proteins p107 and p130 in vitro. The data show that the RIZ CR2 motif can mediate differential binding to Rb family proteins. We also mapped the shared antigenic determinant between RIZ and E1A to a conserved sequence, designated CE1, which is located in the C terminus of E1A. Unlike that of ETA, the CE1 motif of RIZ is located next to the CR2 motif. Despite this proximity, CE1 and CR2 appear to act independently. The data show similarities as well as differences between the homologous sequences of RIZ and E1A and contribute to an understanding of the biochemistry of these proteins.
Mesh Terms:
Adenovirus E1A Proteins, Amino Acid Sequence, Binding Sites, DNA-Binding Proteins, Histone-Lysine N-Methyltransferase, Molecular Sequence Data, Nuclear Proteins, Retinoblastoma Protein, Transcription Factors
J. Virol. Aug. 01, 1997; 71(8);6200-3 [PUBMED:9223517]
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