Inactivation of oncoprotein binding by a single Cys706-to-Tyr substitution in the retinoblastoma protein.
We previously found a new single amino acid substitution at codon 706 (Cys-to-Tyr) of the retinoblastoma (RB) gene in a sporadic retinoblastoma patient. The glutathione S-transferase-RB fused protein containing this mutation was here tested for binding to SV40 large T antigen and adenovirus E1A protein, and was shown to have lost its binding affinity. Thus, Tyr, as well as Phe, residues substituted for Cys706 were found to abolish the RB protein activity.
Saijo
M
M
Biology Division, National Cancer Center Research Institute, Tokyo, Japan.
Kato
M V
MV
Sasaki
M S
MS
Ishizaki
K
K
Taya
Y
Y
D017500:Adenovirus E1A Proteins / Q000378:metabolism; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism; D001483:Base Sequence; D003545:Cysteine / Q000378:metabolism*; D017931:DNA Primers; D016161:Genes, Retinoblastoma; D005978:Glutathione / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012175:Retinoblastoma / Q000235:genetics / Q000378:metabolism; D016160:Retinoblastoma Protein / Q000737:chemistry / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
D017500:Adenovirus E1A Proteins; D000952:Antigens, Polyomavirus Transforming; D017931:DNA Primers; D011993:Recombinant Fusion Proteins; D016160:Retinoblastoma Protein; D014443:Tyrosine; D005978:Glutathione; D003545:Cysteine