Mycobacterial helicase Lhr abets resistance to DNA crosslinking agents mitomycin C and cisplatin
Author:
Affiliation:
1. Molecular Biology Program, Memorial Sloan Kettering Cancer Center , NY , NY 10065, USA
2. Immunology Program, Memorial Sloan Kettering Cancer Center , NY , NY 10065, USA
Abstract
Funder
National Institutes of Health
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
https://academic.oup.com/nar/article-pdf/51/1/218/48723211/gkac1222.pdf
Reference34 articles.
1. Mycobacterium smegmatis lhr is a DNA-dependent atpase and a 3′-to-5′ DNA translocase and helicase that prefers to unwind 3′-tailed RNA:DNA hybrids;Ordonez;J. Biol. Chem.,2013
2. Structure of mycobacterial 3′-to-5′ RNA:DNA helicase lhr bound to a ssDNA tracking strand highlights distinctive features of a novel family of bacterial helicases;Ejaz;Nucleic Acids Res.,2018
3. Oligomeric quaternary structure of Escherichia coli and Mycobacterium smegmatis lhr helicases is nucleated by a novel C-terminal domain composed of five winged-helix modules;Warren;Nucleic Acids Res.,2021
4. Characterization of a novel DNA glycosylase from S. sahachiroi involved in the reduction and repair of azinomycin B induced DNA damage;Wang;Nucleic Acids Res.,2016
5. Structure of a DNA glycosylase that unhooks interstrand cross-links;Mullins;Proc. Natl. Acad. Sci. U.S.A.,2017
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