1. Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA.
- Author
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Salas TR, Petruseva I, Lavrik O, and Saintomé C
- Subjects
- Binding Sites, DNA, Single-Stranded chemistry, Humans, Oligonucleotides chemistry, Oligonucleotides metabolism, Oligonucleotides radiation effects, Protein Binding, Protein Subunits chemistry, Protein Subunits metabolism, Thymidine analogs & derivatives, Thymidine chemistry, Thymidine radiation effects, DNA, Single-Stranded metabolism, DNA-Binding Proteins metabolism, Replication Protein A metabolism
- Abstract
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.
- Published
- 2009
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