DNA recognition properties of the N-terminal DNA binding domain within the large subunit of Replication Factor C

被引:25
作者
Allen, BL
Uhlmann, F
Gaur, LK
Mulder, BA
Posey, KL
Jones, LB
Hardin, SH
机构
[1] Texas A&M Univ, Dept Biol, College Stn, TX 77843 USA
[2] Mem Sloan Kettering Canc Ctr, Sloan Kettering Inst, New York, NY 10021 USA
[3] Univ Houston, Dept Biol & Biochem, Houston, TX 77204 USA
关键词
D O I
10.1093/nar/26.17.3877
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
Replication Factor C (RFC) is a five-subunit protein complex required for eukaryotic DNA replication and repair. The large subunit within this complex contains a C-terminal DNA binding domain which provides specificity for PCNA loading at a primer-template and a second, N-terminal DNA binding domain of unknown function. We isolated the N-terminal DNA binding domain from Drosophila melanogaster and defined the region within this polypeptide required for DNA binding. The DNA determinants most efficiently recognized by both the Drosophila minimal DNA binding domain and the N-terminal half of the human large subunit consist of a double-stranded DNA containing a recessed 5' phosphate. DNA containing a recessed 5' phosphate was preferred 5-fold over hairpined DNA containing a recessed 3' hydroxyl, Combined with existing data, these DNA binding properties suggest a role for the N-terminal DNA binding domain in the recognition of phosphorylated DNA ends.
引用
收藏
页码:3877 / 3882
页数:6
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