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Photoreactive DNA as a Tool to Study Replication Protein A Functioning in DNA Replication and Repair
Author(s) -
Rechkunova Nadejda I.,
Lavrik Olga I.
Publication year - 2020
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/php.13222
Subject(s) - replication protein a , dna replication , eukaryotic dna replication , dna repair , dna , origin recognition complex , replication factor c , dna clamp , control of chromosome duplication , biology , dna mismatch repair , chemistry , microbiology and biotechnology , biochemistry , dna binding protein , gene , rna , transcription factor , reverse transcriptase
Replication protein A (RPA), eukaryotic single‐stranded DNA‐binding protein, is a key player in multiple processes of DNA metabolism including DNA replication, recombination and DNA repair. Human RPA composed of subunits of 70‐, 32‐ and 14‐kDa binds ssDNA with high affinity and interacts specifically with multiple proteins. The RPA heterotrimer binds ssDNA in several modes, with occlusion lengths of 8–10, 13–22 and 30 nucleotides corresponding to global, transitional and elongated conformations of protein. Varying the structure of photoreactive DNA, the intermediates of different stages of DNA replication or DNA repair were designed and applied to identify positioning of the RPA subunits on the specific DNA structures. Using this approach, RPA interactions with various types of DNA structures attributed to replication and DNA repair intermediates were examined. This review is dedicated to blessed memory of Prof. Alain Favre who contributed to the development of photoreactive nucleotide derivatives and their application for the study of protein–nucleic acids interactions.