Purification and functional characterization of bovine RP-A in an in vitro SV40 DNA replication system.

Abstract:

:The single-stranded DNA binding protein RP-A is required in SV40 DNA in vitro replication. The RP-A purified from calf thymus contains 4 polypeptides with molecular weights 70kDa, 53kDa, 32kDa, and 14kDa. The p70 subunit and its proteolysed form p53 are recognized by the monoclonal antibody 70C (Kenny et al. (1990)) and bind to ssDNA. The p70 and p32 subunits of bovine RP-A are phosphorylated by CDC2-cyclin B kinase. Bovine RP-A supports the origin dependent unwinding of SV40 DNA by T antigen. Furthermore, bovine RP-A can efficiently substitute for human RP-A in SV40 DNA replication in vitro. A modified blotting technique revealed that RP-A interacts specifically and directly with the p48 subunit of DNA polymerase alpha-primase complex.

journal_name

Chromosoma

journal_title

Chromosoma

authors

Nasheuer HP,von Winkler D,Schneider C,Dornreiter I,Gilbert I,Fanning E

doi

10.1007/BF02451786

subject

Has Abstract

pub_date

1992-01-01 00:00:00

pages

S52-9

issue

1 Suppl

eissn

0009-5915

issn

1432-0886

journal_volume

102

pub_type

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