Complexes of RecA protein in solution. A study by small angle neutron scattering.
RecA complexes on DNA and self-polymers were analysed by small-angle neutron scattering in solution. By Guinier analysis at small angles and by model analysis of a subsidiary peak at wider angles, we find that the filaments fall into two groups: the DNA complex in the presence of ATP gamma S, an open helix with pitch 95 A, a cross-sectional radius of gyration of 33 A and a mass per length of about six RecA units per turn, which corresponds to the state of active enzyme; and the compact form (bound to single-stranded DNA in the absence of ATP, or binding ATP gamma S in the absence of DNA, or just the protein on its own), a helical structure with pitch 70 A, cross-sectional radius of gyration 40 A and mass per length about five RecA units per turn, which corresponds to the conditions of inactive enzyme. The results are discussed in the perspective of unifying previous conflicting structural results obtained by electron microscopy.
DiCapua
E
E
Institut Laue-Langevin, Grenoble, France.
Schnarr
M
M
Ruigrok
R W
RW
Lindner
P
P
Timmins
P A
PA
D000255:Adenosine Triphosphate; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004247:DNA; D008854:Microscopy, Electron; D009502:Neutrons; D011938:Rec A Recombinases / Q000648:ultrastructure; D012542:Scattering, Radiation
D000255:Adenosine Triphosphate; D004247:DNA; D011938:Rec A Recombinases