Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA

被引：30

作者：

Salas, Tonatiuh Romero ^{[1
]}

Petruseva, Irina ^{[2
]}

Lavrik, Olga ^{[2
]}

Saintome, Carole ^{[1
]}

机构：

[1] CNRS Paris 6 Paris 8, UMR 7033, Lab Biophys Mol Cellulaire & Tissulaire, F-75251 Paris 05, France

[2] Inst Chem Biol & Fundamental Med, Novosibirsk 630090, Russia

来源：

NUCLEIC ACIDS RESEARCH | 2009年 / 37卷 / 01期

关键词：

BINDING DOMAIN; MECHANISM; SSDNA; POLARITY; COMPLEX; PRIMER; RECOGNITION; INSIGHTS; 3'-END; LENGTH;

D O I：

10.1093/nar/gkn895

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 Protein A is a single-stranded (ss) DNA-binding protein that is highly conserved in eukaryotes and plays essential roles in many aspects of nucleic acid metabolism, including replication, recombination, DNA repair and telomere maintenance. It is a heterotrimeric complex consisting of three subunits: RPA1, RPA2 and RPA3. It possesses four DNA-binding domains (DBD), DBD-A, DBD-B and DBD-C in RPA1 and DBD-D in RPA2, and it binds ssDNA via a multistep pathway. Unlike the RPA1 and RPA2 subunits, no ssDNA-RPA3 interaction has as yet been observed although RPA3 contains a structural motif found in the other DBDs. We show here using 4-thiothymine residues as photoaffinity probe that RPA3 interacts directly with ssDNA on the 3-side on a 31 nt ssDNA.

引用

页码：38 / 46

页数：9

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