Characterization of the Escherichia coliDamage-independent UvrBC Endonuclease Activity
Open Access
- 1 December 1998
- journal article
- research article
- Published by Elsevier
- Vol. 273 (52) , 34896-34903
- https://doi.org/10.1074/jbc.273.52.34896
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- Identification of the different intermediates in the interaction of (A)BC excinuclease with its substrates by DNase I footprinting on two uniquely modified oligonucleotidesPublished by Elsevier ,2004
- Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC–DNA complex and in 3′-incisionMutation Research/DNA Repair, 1997
- Formation of DNA Repair Intermediates and Incision by the ATP-dependent UvrB-UvrC EndonucleaseJournal of Biological Chemistry, 1997
- DNA EXCISION REPAIRAnnual Review of Biochemistry, 1996
- The C-terminal Region of the UvrB Protein of Escherichia coli Contains an Important Determinant for UvrC Binding to the Preincision Complex but Not the Catalytic Site for 3′-IncisionJournal of Biological Chemistry, 1995
- Human DNA Repair Excision NucleaseJournal of Biological Chemistry, 1995
- Helicase Motifs V and VI of the Escherichia coli UvrB Protein of the UvrABC Endonuclease Are Essential for the Formation of the Preincision ComplexJournal of Molecular Biology, 1994
- The (A)BC excinuclease of Escherichia coli has only the UvrB and UvrC subunits in the incision complex.Proceedings of the National Academy of Sciences, 1989
- DNA REPAIR ENZYMESAnnual Review of Biochemistry, 1988
- Enzymatic properties of purified Escherichia coli uvrABC proteins.Proceedings of the National Academy of Sciences, 1983