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Nucleic Acids Research, 1987, Vol. 15, No. 16 6607-6624
© 1987

Articles

DNA glycosylase enzymes induced during chemical adaptation of M. luteus

S. Riazuddin, A. Athar, Z. Ahmed, S.M. Lali and A. Sohail

Centre for Advanced Molecular Biology, University of the Punjab Lahore, Pakistan

Received May 18, 1987. Revised July 27, 1987. Accepted July 27, 1987.

Five peaks of DNA glycosylase activity showing a preference for MNNG alkylated DNA have been identified from extracts of adapted M. luteus. They are numerically designated as GI to GV in order of their decreasing molecular weights. The first two of these peaks have been highly purified. GI, is a constitutive heat labile protein, 35% stimulated by the presence of 50 mM NaCl, acts exclusively on 3 MeA residues in alkylated DNA, 60–70% inhibited by the presence of 2mM free 3MeA and has been designated as 3MeA DNA glycosylase enzyme. GII, which is an inducible protein, is heat stable, 28% inhibited by the presence of 50 mM NaCl, removes 3MeA, 3MeG, 7MeA & 7MeG with different efficiency, and has been designated as 3, 7 methylpurine DNA glycosylase enzyme. The rate of release of 3 methylpurines is 30 times that of 7MeG. There is no activity of either enzyme on 02 -MeC, O2 -MeT, 04 -MeT or 06 -MeG. The apparent molecular weights of GI and GIl proteins are 28Kd and 22Kd respectively.


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