Viral growth, origin binding, and p53 binding properties of simian virus 40 large T antigen transformation and replication mutants.
The viability, p53 binding, and SV40 origin binding of a series of SV40 large T antigen point mutants, which map to the amino terminal one-third of the molecule, were examined. Two mutants which yield small plaques were found to have altered kinetics of replication upon infection of permissive cells. Mutants which did not bind to the origin of replication were not able to replicate, but the reverse was not always true. Replication defective mutants which bound the SV40 origin were found; these map both inside and outside of the origin binding domain. All the transformation defective mutants bound the cellular protein, p53.
Rutila
J E
JE
Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor 48109-0620.
Christensen
J B
JB
Imperiale
M J
MJ
D000818:Animals; D002478:Cells, Cultured; D004261:DNA Replication; D005455:Fluorescent Antibody Technique; D000882:Haplorhini; D007700:Kinetics; D009154:Mutation; D009363:Neoplasm Proteins / Q000235:genetics / Q000378:metabolism*; D010641:Phenotype; D010750:Phosphoproteins / Q000235:genetics / Q000378:metabolism*; D010957:Plasmids; D051381:Rats; D013539:Simian virus 40 / Q000235:genetics* / Q000254:growth & development / Q000276:immunology; D014162:Transfection; D014170:Transformation, Genetic; D016159:Tumor Suppressor Protein p53
D009363:Neoplasm Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53