The nucleotide binding site detected by affinity labeling in the large T proteins of polyoma and SV40 viruses is distinct from their ATPase catalytic site

• Published in: The Journal of biological chemistry Vol. 259; no. 24; pp. 15196 - 15203
• Main Authors: Clertant, P, Gaudray, P, May, E, Cuzin, F
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 25.12.1984; American Society for Biochemistry and Molecular Biology
• Subjects: Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - analogs & derivatives; Adenosine Triphosphate - metabolism; Affinity Labels - metabolism; Animals; Antibodies; Antigen-Antibody Complex; Antigens, Polyomavirus Transforming; Antigens, Viral, Tumor - metabolism; Binding Sites; Biological and medical sciences; Cell Line; Cell Transformation, Neoplastic; Cells, Cultured; Chlorocebus aethiops; Fundamental and applied biological sciences. Psychology; Kidney; Kinetics; Mice; Microbiology; Polyomavirus - enzymology; Protein Binding; Protein Kinases - metabolism; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; Simian virus 40 - enzymology; Viral Proteins - metabolism; Virology; Molecular structure; Affinity labelling; ATPase; Polyomavirus; Identification; Binding site; Papovaviridae; Structure function relationship; Virus; Oncogenic virus; Nucleotide; Catalytic site; Mechanism of action; SV40 virus; Catalyst activity; T antigen

Binding of nucleotides to a specific site of the large T proteins of polyoma and SV40 viruses was demonstrated by covalent affinity labeling with periodate-oxidized [alpha-32P]ATP (oxATP) (Clertant, P., and Cuzin, F. (1982) J. Biol. Chem. 257, 6300-6305). This site appears different from the catalyt...