ATP induces the assembly of polyoma large tumor antigen into hexamers.
Using zone velocity sedimentation and nondenaturing polyacrylamide gel electrophoresis, we have determined that purified polyoma large tumor antigen (Py T Ag) consists of discrete forms ranging from more abundant monomers and dimers to several higher but clearly distinguishable oligomeric species. Addition of ATP and MgCl2 to Py T Ag caused a dramatic increase in the appearance of Py T Ag hexamers, a form that, based on its SV40 T Ag counterpart, is likely to play a crucial role in its DNA replication functions. Other nucleotides in addition to ATP, as well as a nonhydrolyzable ATP derivative, were capable of inducing hexamer formation. This approach may further elucidate the role(s) of different forms of Py T Ag in viral regulatory processes.
Wang
E H
EH
Department of Biological Sciences, Columbia University, New York, New York 10027.
Prives
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D000255:Adenosine Triphosphate / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000737:chemistry* / Q000502:physiology; D016367:Baculoviridae / Q000235:genetics; D002460:Cell Line; D002501:Centrifugation, Zonal; D004261:DNA Replication; D000939:Epitopes / Q000032:analysis; D046911:Macromolecular Substances; D015636:Magnesium Chloride / Q000494:pharmacology; D051379:Mice; D009711:Nucleotides / Q000378:metabolism; D013539:Simian virus 40 / Q000235:genetics / Q000502:physiology*
D000952:Antigens, Polyomavirus Transforming; D000939:Epitopes; D046911:Macromolecular Substances; D009711:Nucleotides; D015636:Magnesium Chloride; D000255:Adenosine Triphosphate