PMID:7724585
| Citation |
Kowalczykowski, SC and Krupp, RA (1995) DNA-strand exchange promoted by RecA protein in the absence of ATP: implications for the mechanism of energy transduction in protein-promoted nucleic acid transactions. Proc. Natl. Acad. Sci. U.S.A. 92:3478-82 |
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| Abstract |
DNA-strand exchange promoted by Escherichia coli RecA protein normally requires the presence of ATP and is accompanied by ATP hydrolysis, thereby implying a need for ATP hydrolysis. Previously, ATP hydrolysis was shown not to be required; here we demonstrate furthermore that a nucleoside triphosphate cofactor is not required for DNA-strand exchange. A gratuitous allosteric effector consisting of the noncovalent complex of ADP and aluminum fluoride, ADP.AIF4-, can both induce the high-affinity DNA-binding state of RecA protein and support the homologous pairing and exchange of up to 800-900 bp of DNA. These results demonstrate that induction of the functionally active, high-affinity DNA-binding state of RecA protein is needed for RecA protein-promoted DNA-strand exchange and that there is no requirement for a high-energy nucleotide cofactor for the exchange of DNA strands. Consequently, the free energy needed to activate the DNA substrates for DNA-strand exchange is not derived from ATP hydrolysis. Instead, the needed free energy is derived from ligand binding and is transduced to the DNA via the associated ligand-induced structural transitions of the RecA protein-DNA complex; ATP hydrolysis simply destroys the effector ligand. This concept has general applicability to the mechanism of energy transduction by proteins. |
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| Keywords |
Adenosine Diphosphate/metabolism; Adenosine Diphosphate/pharmacology; Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/metabolism; Aluminum Compounds/metabolism; Aluminum Compounds/pharmacology; DNA-Binding Proteins/drug effects; DNA-Binding Proteins/metabolism; Energy Metabolism; Fluorides/metabolism; Fluorides/pharmacology; Models, Genetic; Nucleic Acid Heteroduplexes/metabolism; Protein Binding/drug effects; Rec A Recombinases/drug effects; Rec A Recombinases/metabolism; Recombination, Genetic/physiology; Sodium Chloride/pharmacology |
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