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Deciphering the essentiality and function of SxSx motif in Mycobacterium tuberculosis UvrB

Thakur, M and Muniyappa, K (2020) Deciphering the essentiality and function of SxSx motif in Mycobacterium tuberculosis UvrB. In: Biochimie, 170 . pp. 94-105.

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Official URL: https://dx.doi.org/10.1016/j.biochi.2020.01.003


The UvrB subunit is a central component of the UvrABC incision complex and plays a pivotal role in damage recognition, strand excision and repair synthesis. A conserved structural motif (the SxSx motif) present in UvrB is analogous to a similar motif (TxGx) in the helicases of superfamily 2, whose function is not fully understood. To elucidate the significance of the SxSx (Ser143-Val144-Ser145-Cys146) motif in Mycobacterium tuberculosis UvrB (MtUvrB), different variants of MtUvrB subunit were constructed and characterized. The SxSx motif indeed was found to be essential for MtUvrB function: while Ser143 and Cys146 residues within this motif were crucial for MtUvrB function, Ser145 plays an important but less essential role. The SxSx motif-deleted mutant was drastically attenuated and three single (S143A, S145A and C146A) mutants and a double (S143A/S145A) mutant exhibited various degrees of severity in their DNA-binding, DNA helicase and ATPase activities. Taken together, these results highlight a hitherto unrecognized role for SxSx motif in the catalytic activities of UvrB. © 2020 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)

Item Type: Journal Article
Publication: Biochimie
Publisher: Elsevier B.V.
Additional Information: Copyright of this article belongs to Elsevier B.V.
Keywords: Mycobacterium tuberculosis; Nucleotide excision repair; SxSx motif; ATPase; DNA helicase; TxGx motif
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 03 Feb 2020 11:38
Last Modified: 03 Feb 2020 11:38
URI: http://eprints.iisc.ac.in/id/eprint/64392

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