Hydrolysis of nucleoside triphosphates catalyzed by the recA protein of Escherichia coli. Steady state kinetic analysis of ATP hydrolysis.
Open Access
- 1 August 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (16) , 8845-8849
- https://doi.org/10.1016/s0021-9258(19)68922-2
Abstract
No abstract availableThis publication has 11 references indexed in Scilit:
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- Binding of the recA protein of Escherichia coli to single- and double-stranded DNA.Journal of Biological Chemistry, 1981
- Interaction of the recA protein of Escherichia coli with adenosine 5'-O-(3-thiotriphosphate).Journal of Biological Chemistry, 1981
- DNA and Nucleoside Triphosphate Binding Properties of recA Protein from Escherichia coliProgress in Nucleic Acid Research and Molecular Biology, 1981
- Homologous pairing in genetic recombination: complexes of recA protein and DNA.Proceedings of the National Academy of Sciences, 1979
- Single strands induce recA protein to unwind duplex DNA for homologous pairingNature, 1979
- Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli.Proceedings of the National Academy of Sciences, 1979
- Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments.Proceedings of the National Academy of Sciences, 1979
- ATP-dependent renaturation of DNA catalyzed by the recA protein of Escherichia coli.Proceedings of the National Academy of Sciences, 1979
- Characteristics of Purified recA Protein and the Regulation of Its Synthesis In VivoPublished by Cold Spring Harbor Laboratory ,1979