Title : Role of tyrosine residue 264 of RecA for the binding of cofactor and DNA.

Pub. Date : 1993 Jan 25

PMID : 8420956






7 Functional Relationships(s)
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1 Role of tyrosine residue 264 of RecA for the binding of cofactor and DNA. Tyrosine RAD51 recombinase Homo sapiens
2 The tyrosine fluorescence of the RecA protein is quenched by about 15% upon binding of the cofactor analog adenosine 5"-O-(3-thiotriphosphate) (ATP gamma S). Tyrosine RAD51 recombinase Homo sapiens
3 Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264. Tyrosine RAD51 recombinase Homo sapiens
4 Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264. Tyrosine RAD51 recombinase Homo sapiens
5 Upon DNA binding, a change of tyrosine fluorescence is observed both with the modified protein and with wild type RecA, indicating that DNA binding affects the environment of other tyrosine residues than Tyr-264. Tyrosine RAD51 recombinase Homo sapiens
6 Tyr-264 may be an important residue for the allosteric effect induced by the cofactor for the binding of DNA to RecA. Tyrosine RAD51 recombinase Homo sapiens
7 The fact that we observe no interaction of ATP gamma S with Tyr-103 (as evidenced from absence of fluorescence change) but instead with Tyr-264 may suggest an important conformational difference between the RecA complexes with, respectively, ADP and ATP. Tyrosine RAD51 recombinase Homo sapiens