Damke, Prashant P and Dhanaraju, Rajkumar and Marsin, Stephanie and Radicella, Juan Pablo and Rao, Desirazu N (2015) The nuclease activities of both the Smr domain and an additional LDLK motif are required for an efficient anti-recombination function of Helicobacter pyloriMutS2. In: MOLECULAR MICROBIOLOGY, 96 (6). pp. 1240-1256.
Full text not available from this repository. (Request a copy)Abstract
Helicobacter pylori, a human pathogen, is a naturally and constitutively competent bacteria, displaying a high rate of intergenomic recombination. While recombination events are essential for evolution and adaptation of H.pylori to dynamic gastric niches and new hosts, such events should be regulated tightly to maintain genomic integrity. Here, we analyze the role of the nuclease activity of MutS2, a protein that limits recombination during transformation in H.pylori. In previously studied MutS2 proteins, the C-terminal Smr domain was mapped as the region responsible for its nuclease activity. We report here that deletion of Smr domain does not completely abolish the nuclease activity of HpMutS2. Using bioinformatics analysis and mutagenesis, we identified an additional and novel nuclease motif (LDLK) at the N-terminus of HpMutS2 unique to Helicobacter and related epsilon-proteobacterial species. A single point mutation (D30A) in the LDLK motif and the deletion of Smr domain resulted in approximate to 5-10-fold loss of DNA cleavage ability of HpMutS2. Interestingly, the mutant forms of HpMutS2 wherein the LDLK motif was mutated or the Smr domain was deleted were unable to complement the hyper-recombination phenotype of a mutS2(-) strain, suggesting that both nuclease sites are indispensable for an efficient anti-recombinase activity of HpMutS2.
| Item Type: | Journal Article |
|---|---|
| Publication: | MOLECULAR MICROBIOLOGY |
| Publisher: | WILEY-BLACKWELL |
| Additional Information: | Copy right for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA |
| Department/Centre: | Division of Biological Sciences > Biochemistry |
| Date Deposited: | 19 Jul 2015 09:38 |
| Last Modified: | 19 Jul 2015 09:38 |
| URI: | http://eprints.iisc.ac.in/id/eprint/51882 |
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