The Binding of UvrAB Proteins to Bubble and Loop Regions in Duplex DNA
Open Access
- 1 August 1996
- journal article
- Published by Elsevier
- Vol. 271 (35), 21462-21470
- https://doi.org/10.1074/jbc.271.35.21462
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Dimerization of Escherichia coli UvrA and its binding to undamaged and ultraviolet light damaged DNABiochemistry, 1991
- Mutations in the Escherichia coli UvrB ATPase motif compromise excision repair capacity.Proceedings of the National Academy of Sciences, 1989
- 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
- ATPase activity of the UvrA and UvrAB protein complexes of theEscherichia coliUvrABC endonucleaseNucleic Acids Research, 1989
- Involvement of a cryptic ATPase activity of UvrB and its proteolysis product, UvrB* in DNA repairNucleic Acids Research, 1988
- The effect ofEscherichia coliUvr protein binding on the topology of supercoiled DNANucleic Acids Research, 1986
- Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease.Proceedings of the National Academy of Sciences, 1985
- Involvement of helicase II (uvrD gene product) and DNA polymerase I in excision mediated by the uvrABC protein complex.Proceedings of the National Academy of Sciences, 1985
- Enzymatic properties of purified Escherichia coli uvrABC proteins.Proceedings of the National Academy of Sciences, 1983
- A novel repair enzyme: UVRABC excision nuclease of Escherichia coli cuts a DNA strand on both sides of the damaged regionCell, 1983