Title : Binding of DNA quenches tyrosine fluorescence of RecA without energy transfer to DNA bases.

Pub. Date : 1993 Jan 25

PMID : 8420955






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Binding of DNA quenches tyrosine fluorescence of RecA without energy transfer to DNA bases. Tyrosine RAD51 recombinase Homo sapiens
2 The binding of single- as well as double-stranded DNA to RecA, in the presence of the cofactor analog ATP gamma S (adenosine 5"-O-(3-thiotriphosphate)), leads to about 20% quenching of the tyrosine fluorescence of the protein but to no essential change of the tryptophan fluorescence. Tyrosine RAD51 recombinase Homo sapiens
3 At high salt condition, which induces ATPase activity in RecA just as DNA binding does, the tyrosine fluorescence is more pronounced than at low salt conditions, indicating that the effect induced by high salt is different from the conformational change induced by DNA binding. Tyrosine RAD51 recombinase Homo sapiens