The DNA-binding domain of simian virus 40 tumor antigen has been previ
ously shown to participate in a number of different activities. Beside
s being involved in binding to sequences at the viral replication orig
in, this domain appears to be required for nonspecific DNA binding, fo
r structurally distorting origin DNA (melting and untwisting), and pos
sibly for oligomerization of the protein into hexamers and double hexa
mers. We now provide evidence that it also takes part in unwinding ori
gin DNA sequences, contributes a function specifically related to in v
ivo DNA replication, and perhaps supports the assembly of the virus or
release of the virus from the cell. This 100-amino-acid domain appear
s to be an excellent model system for studying how a small region of a
protein could have a number of distinct activities.