[Dynamic properties of recA protein filaments from E. coli and P. aeruginosa investigated by neutron spin-echo].
Bacterial RecA protein is the key enzyme in the processes of homologous recombination, post-replication repair and induction of SOS-repair functions. While a significant amount of data on the structure of RecA protein and its functional analogs has been obtained, there is little information about the molecular dynamics of this protein. In this work we present the results of neutron spin-echo measurements of the relaxation kinetics of filaments formed by RecA proteins from E. coli and P. aeruginosa. The results suggest that the protein filaments exhibit both diffusion and internal relaxation modes, which change during the formation of complexes of these proteins with ATP and single-stranded DNA.
Lebedev
D V
DV
Monkenbusch
M
M
Shalguev
V I
VI
Lantsov
V A
VA
Isaev-Ivanov
V V
VV
D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D004260:DNA Repair / Q000502:physiology; D004261:DNA Replication / Q000502:physiology; D004277:DNA, Single-Stranded / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D009502:Neutrons; D020836:Protein Structure, Quaternary; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011938:Rec A Recombinases / Q000737:chemistry* / Q000378:metabolism; D011995:Recombination, Genetic / Q000502:physiology; D013329:Structure-Activity Relationship
D004277:DNA, Single-Stranded; D029968:Escherichia coli Proteins; D000255:Adenosine Triphosphate; D011938:Rec A Recombinases