Functions of the ATP hydrolysis subunits (RecB and RecD) in the nuclease reactions catalyzed by the RecBCD enzyme fromEscherichia coli
- 24 April 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 278 (1) , 89-104
- https://doi.org/10.1006/jmbi.1998.1694
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health
This publication has 34 references indexed in Scilit:
- The RecD Subunit of the RecBCD Enzyme from Escherichia coli Is a Single-stranded DNA-dependent ATPasePublished by Elsevier ,1997
- Interactions of the RecBCD Enzyme from Escherichia coli and Its Subunits with DNA, Elucidated from the Kinetics of ATP and DNA Hydrolysis with Oligothymidine SubstratesBiochemistry, 1996
- Role of the Escherichia coli Recombination Hotspot, χ, in RecABCD-dependent Homologous PairingPublished by Elsevier ,1995
- Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot chi in vitro: evidence for functional inactivation or loss of the RecD subunit.Proceedings of the National Academy of Sciences, 1994
- The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzymeCell, 1993
- Resolution of Holliday junctions in vitro requires the Escherichia coli ruvC gene product.Proceedings of the National Academy of Sciences, 1991
- Homologous pairing in vitro stimulated by the recombination Hotspot, ChiCell, 1991
- Escherichia coli RecBCD enzyme: inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunitsGene, 1991
- recD: the gene for an essential third subunit of exonuclease V.Proceedings of the National Academy of Sciences, 1986
- Oligonucleotide interactions. III. Circular dichroism studies of the conformation of deoxyoligonucleolidesBiopolymers, 1970