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Evidence for direct contact between the RPA3 subunit of the human replication protein A and single-stranded DNA.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2009 Jan; Vol. 37 (1), pp. 38-46. Date of Electronic Publication: 2008 Nov 14. - Publication Year :
- 2009
-
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.
- 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
Subjects
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 37
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 19010961
- Full Text :
- https://doi.org/10.1093/nar/gkn895