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  • Title: [The role of oligophosphate and nucleoside fragments upon the interaction of a nucleotide with RecA protein].
    Author: Kachurin AM, Golubev AM.
    Journal: Mol Biol (Mosk); 1993; 27(2):290-8. PubMed ID: 8487759.
    Abstract:
    Pyrophosphate and 1-pyrophospho-5-phosphoribose displace the nucleotide from the complex with RecA protein (in the absence of DNA). Adenosine, AMP, inorganic phosphate riboso-5-phosphate have no effect. Pyrophosphate causes the dissociation of RecA-ssDNA-complex in the same manner as ADP, circular hexaphosphate has no effect. In the complex with RecA protein the dissociation constant for pyrophosphate is 1.6 mM and 710 mM for adenosine. It is proposed that the oligophosphate is the main binding group in the RecA-nucleotide interaction. Two vicinal "closed" -O and one terminal "open" oxygenous =O-groups of oligophosphate take part in the binding. The nucleoside fragment alone cannot provide the firm binding of the nucleotide with the protein, but probably is responsible for the specificity of the nucleotide to protein binding.
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