Interaction of DNA polymerase alpha-primase with cellular replication protein A and SV40 T antigen.
The purified human single-stranded DNA binding protein, replication protein A (RP-A), forms specific complexes with purified SV40 large T antigen and with purified DNA polymerase alpha-primase, as shown by ELISA and a modified immunoblotting technique. RP-A associated efficiently with the isolated primase, as well as with intact polymerase alpha-primase. The 70 kDa subunit of RP-A was sufficient for association with polymerase alpha-primase. Purified SV40 large T antigen bound to intact RP-A and to polymerase-primase, but not to any of the separated subunits of RP-A or to the isolated primase. These results suggest that the specific protein-protein interactions between RP-A, polymerase-primase and T antigen may play a role in the initiating of SV40 DNA replication.
Dornreiter
I
I
Institute for Biochemistry, Munich, Germany.
Erdile
L F
LF
Gilbert
I U
IU
von Winkler
D
D
Kelly
T J
TJ
Fanning
E
E
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism*; D002417:Cattle; D019915:DNA Primase; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000378:metabolism*; D015151:Immunoblotting; D007700:Kinetics; D046911:Macromolecular Substances; D008961:Models, Structural; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D012316:RNA Nucleotidyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D051716:Replication Protein A; D013539:Simian virus 40 / Q000378:metabolism*; D013950:Thymus Gland / Q000201:enzymology
D000911:Antibodies, Monoclonal; D000952:Antigens, Polyomavirus Transforming; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D051716:Replication Protein A; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases