01756nas a2200241   4500000000100000008004100001653001500042653000900057653001200066653001500078653001600093653001100109653002500120100001300145700001200158700001200170700001200182700001000194700001400204245014700218520113500365022001401500       2019                            d10aAlkylation10aAlkB10aleprosy10aDNA Repair10aDioxygenase10aML019010aMycobacterium leprae1 aSharma M1 aAkula D1 aMohan M1 aNigam R1 aDas M1 aAnindya R00aHeteroexpression of Mycobacterium leprae hypothetical protein ML0190 provides protection against DNA-alkylating agent methyl methanesulfonate.3 a<p>Repair of DNA alkylation damage is essential for maintaining genome integrity and Fe(II)/2-oxoglutarate(2OG)-dependent dioxygenase family of enzymes play crucial role in repairing some of the alkylation damages. Alkylation repair protein-B (AlkB) of Escherichia coli belongs to Fe(II)/2OG-dependent dioxygenase family and carries out DNA dealkylation repair. We report here identification of a hypothetical Mycobacterium leprae protein (accession no. ML0190) from the genomic database and show that this 615-bp open reading frame encodes a protein with sequence and structural similarity to Fe(II)/2OG-dependent dioxygenase AlkB. We identified mRNA transcript of this gene in the M.&nbsp;leprae infected clinical skin biopsy samples isolated from the leprosy patients. Heterologous expression of ML0190 in methyl methane sulfonate (MMS) sensitive and DNA repair deficient strain of Saccharomyces cerevisiae and Escherichia coli resulted in resistance to alkylating agent MM. The results of the present study imply that Mycobacterium leprae ML0190 is involved in protecting the bacterial genome from DNA alkylation damage.</p>
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