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Interaction of DNA polymerase alpha‐primase with cellular replication protein A and SV40 T antigen.
Author(s) -
Dornreiter I.,
Erdile L.F.,
Gilbert I.U.,
Winkler D.,
Kelly T.J.,
Fanning E.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05110.x
Subject(s) - biology , primase , dna polymerase , dna replication , dna polymerase ii , polymerase , microbiology and biotechnology , dna clamp , dna , replisome , genetics , polymerase chain reaction , reverse transcriptase , eukaryotic dna replication , gene
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.