A distinct physiological role of MutY in mutation prevention in mycobacteria
Microbiology & Cell Biology
DNA, Bacterial
0301 basic medicine
Guanine
DNA Repair
Mycobacterium smegmatis
500
Hydrogen Peroxide
Biochemistry
Cell Line
DNA Glycosylases
Substrate Specificity
3. Good health
Mice
03 medical and health sciences
Bacterial Proteins
Mutation
Animals
Rifampin
DNA Damage
DOI:
10.1099/mic.0.033621-0
Publication Date:
2009-11-03T22:52:21Z
AUTHORS (8)
ABSTRACT
Oxidative damage to DNA results in the occurrence of 7,8-dihydro-8-oxoguanine (8-oxoG) genome. In eubacteria, repair such is initiated by two major base-excision enzymes, MutM and MutY. We generated a MutY-deficient strain Mycobacterium smegmatis investigate role this enzyme repair. The MutY deficiency M. did not result either noteworthy susceptibility oxidative stress or an increase mutation rate. However, rifampicin-resistant isolates showed distinct mutations rifampicin-resistance-determining region rpoB . Besides expected C A (or G T) mutations, T G) was also observed. Biochemical characterization mycobacterial ( tuberculosis ) revealed excision opposite 8-oxoG DNA. Additionally, detected. formed complexes with containing : A, but pairs. Primer extension reactions cell-free extracts suggested error-prone incorporation nucleotides into Based on these observations, we discuss physiological specific prevention mycobacteria.
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