Mycobacterium tuberculosisRuvX is a Holliday junction resolvase formed by dimerisation of the monomeric YqgF nuclease domain
Author:
Affiliation:
1. Department of Biochemistry; Indian Institute of Science; Bangalore Karnataka 560012 India
2. Department of Chemistry, School of Biological and Biomedical Sciences; Biophysical Sciences Institute, University of Durham; DH1 3LE UK
Funder
Council of Scientific and Industrial Research, New Delhi
Center of Excellence and Innovation program of the Department of Biotechnology, New Delhi
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Reference69 articles.
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3. Single-molecule height measurements on microsomal cytochrome P450 in nanometer-scale phospholipid bilayer disks;Bayburt;Proc Natl Acad Sci U S A,2002
4. Resolution of Holliday junctions by RuvC resolvase: cleavage specificity and DNA distortion;Bennett;Cell,1993
5. Substrate specificity of the Escherichia coli RuvC protein. Resolution of three- and four-stranded recombination intermediates;Benson;J Biol Chem,1994
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3. Biochemical and Structural Study of RuvC and YqgF from Deinococcus radiodurans;mBio;2022-10-26
4. Novel insights into ATP-Stimulated Cleavage of branched DNA and RNA Substrates through Structure-Guided Studies of the Holliday Junction Resolvase RuvX;Journal of Molecular Biology;2021-06
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