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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Abstract
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 |
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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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