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

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ID: 79487
2020
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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.
Reference Key
thakur2020decipheringbiochimie Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Thakur, Manoj;Muniyappa, K;
Journal biochimie
Year 2020
DOI
S0300-9084(20)30005-5
URL
Keywords
Mycobacterium tuberculosis atpase dna helicase sxsx motif nucleotide excision repair

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