Role of the nucleotide excision repair pathway proteins (UvrB and UvrD2) in recycling UdgB, a base excision repair enzyme in Mycobacterium smegmatis

Kapoor, I and Shaw, A and Naha, A and Emam, E A F and Varshney, U (2022) Role of the nucleotide excision repair pathway proteins (UvrB and UvrD2) in recycling UdgB, a base excision repair enzyme in Mycobacterium smegmatis. In: DNA Repair, 113 .

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Abstract

Cross-talks between DNA repair pathways are emerging as a crucial strategy in the maintenance of the genomic integrity. A double-stranded (ds) DNA specific DNA glycosylase, UdgB is known to excise uracil, hypoxanthine and ethenocytosine. We earlier showed that Mycobacterium smegmatis (Msm) UdgB stays back on the AP-sites it generates in the DNA upon excision of the damaged bases. Here, we show that in an Msm strain deleted for a nucleotide excision repair (NER) protein, UvrB (uvrB�), UdgB expression is toxic, and its deletion from the genome (udgB�) rescues the strain from the genotoxic stress. However, UdgB bound AP-site is not a direct substrate for NER in vitro. We show that UvrD2 and UvrB, known helicases with single-stranded (ss) DNA translocase activity, facilitate recycling of UdgB from AP-DNA. Our studies reveal that the helicases play an important role in exposing the AP-sites in DNA and make them available for further repair. © 2022 Elsevier B.V.

Item Type:	Journal Article
Publication:	DNA Repair
Publisher:	Elsevier B.V.
Additional Information:	The copyright for this article belongs to the Elsevier B.V.
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	15 May 2022 08:15
Last Modified:	15 May 2022 08:15
URI:	https://eprints.iisc.ac.in/id/eprint/71681

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