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A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily

Sang, Pau Biak and Srinath, Thiruneelakantan and Patil, Aravind Goud and Woo, Eui-Jeon and Varshney, Umesh (2015) A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily. In: NUCLEIC ACIDS RESEARCH, 43 (17). pp. 8452-8463.

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Official URL: http://dx.doi.org/10.1093/nar/gkv854

Abstract

Uracil DNA glycosylases (UDGs) are an important group of DNA repair enzymes, which pioneer the base excision repair pathway by recognizing and excising uracil from DNA. Based on two short conserved sequences (motifs A and B), UDGs have been classified into six families. Here we report a novel UDG, UdgX, from Mycobacterium smegmatis and other organisms. UdgX specifically recognizes uracil in DNA, forms a tight complex stable to sodium dodecyl sulphate, 2-mercaptoethanol, urea and heat treatment, and shows no detectable uracil excision. UdgX shares highest homology to family 4 UDGs possessing Fe-S cluster. UdgX possesses a conserved sequence, KRRIH, which forms a flexible loop playing an important role in its activity. Mutations of H in the KRRIH sequence to S, G, A or Q lead to gain of uracil excision activity in MsmUdgX, establishing it as a novel member of the UDG superfamily. Our observations suggest that UdgX marks the uracil-DNA for its repair by a RecA dependent process. Finally, we observed that the tight binding activity of UdgX is useful in detecting uracils in the genomes.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the OXFORD UNIV PRESS, GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Depositing User: Id for Latest eprints
Date Deposited: 14 Jan 2016 05:42
Last Modified: 14 Jan 2016 05:42
URI: http://eprints.iisc.ac.in/id/eprint/53100

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