PURIFICATION AND FUNCTIONAL-CHARACTERIZATION OF BOVINE RP-A IN AN INVITRO SV40-DNA REPLICATION SYSTEM

被引：49

作者：

NASHEUER, HP

VONWINKLER, D

SCHNEIDER, C

DORNREITER, I

GILBERT, I

FANNING, E

机构：

[1] LMU MUNCHEN,INST BIOCHEM,KARLSTR 23,W-8000 MUNICH 2,GERMANY

[2] STANFORD UNIV,MED CTR,SCH MED,DEPT PATHOL,STANFORD,CA 94305

来源：

CHROMOSOMA | 1992年 / 102卷 / 01期

关键词：

D O I：

10.1007/BF02451786

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：S52 / S59

页数：8

共 41 条

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