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Evidence for Elongation of the Helical Pitch of the RecA Filament Upon ATP and ADP Binding Using Small-Angle Neutron Scattering

C. Ellouze ; M. Takahashi ; Pernilla Wittung (Institutionen för fysikalisk kemi) ; K. Mortensen ; M. Schnarr ; Bengt Nordén (Institutionen för fysikalisk kemi)
European Journal of Biochemistry (0014-2956). Vol. 233 (1995), 2, p. 579-583.
[Artikel, refereegranskad vetenskaplig]

Structural changes of the RecA filament upon binding of cofactors have been investigated by small-angle neutron scattering. Both ATP and ADP increased the helical pitch of the RecA homopolymer, which is observed to be 7 nm in the absence of any cofactor. The binding of ATP altered the pitch to 9 nm, whereas the binding of ADP only produced a pitch of 8.2 nm. The pitch determined for the RecA complex with the ATP analog adenosine 5'-[gamma-thio]triphosphate was similar to that found with ATP. Thus, at least three, somewhat different, RecA helical filamentous structures may form in solution. The binding of DNA to RecA did not alter the pitch significantly, indicating that the cofactor binding is the determining factor for the size of the helical pitch of the RecA filament. We also found that elongation of the helical pitch is a necessary, but not a sufficient condition, for the coprotease activity of RecA. The presence of acetate or glutamate ions is also required. The pitch of the ADP . RecA filament is in agreement with that found in the crystal structure. This correlation indicates that this structure corresponds to that of the ADP . RecA filament in solution, although this is not the species active in recombination.

Nyckelord: reca, lexa, small-angle neutron scattering, cofactor, reca filament, double-stranded dna, escherichia-coli, linear dichroism, dependent, proteolysis, electron-microscopy, lambda repressor, cofactor binding, lexa repressor, protein, complexes



Denna post skapades 2011-08-17.
CPL Pubid: 144394

 

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Institutioner (Chalmers)

Institutionen för fysikalisk kemi (1900-2003)

Ämnesområden

Biokemi
Molekylärbiologi

Chalmers infrastruktur