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Single‐molecule analysis reveals two distinct states of the compressed RecA filament on single‐stranded DNA
Author(s) -
Alekseev Aleksandr,
Serdakov Maksim,
Pobegalov Georgii,
Yakimov Alexandr,
Bakhlanova Irina,
Baitin Dmitry,
Khodorkovskii Mikhail
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13922
Subject(s) - protein filament , nucleoprotein , dna , atp hydrolysis , biophysics , homologous recombination , monomer , chemistry , molecule , recombination , crystallography , biology , biochemistry , enzyme , polymer , atpase , organic chemistry , gene
The RecA protein plays a key role in bacterial homologous recombination (HR) and acts through assembly of long helical filaments around single‐stranded DNA in the presence of ATP. Large‐scale conformational changes induced by ATP hydrolysis result in transitions between stretched and compressed forms of the filament. Here, using a single‐molecule approach, we show that compressed RecA nucleoprotein filaments can exist in two distinct interconvertible states depending on the presence of ADP in the monomer–monomer interface. Binding of ADP promotes cooperative conformational transitions and directly affects mechanical properties of the filament. Our findings reveal that RecA nucleoprotein filaments are able to continuously cycle between three mechanically distinct states that might have important implications for RecA‐mediated processes of HR.