DNA glycosylase enzymes induced during chemical adaptation of M. luteus.

Abstract:

: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 2 mM 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 O2-MeC, O2-MeT, O4-MeT or O6-MeG. The apparent molecular weights of GI and GII proteins are 28 Kd and 22 Kd respectively.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Riazuddin S,Athar A,Ahmed Z,Lali SM,Sohail A

doi

10.1093/nar/15.16.6607

subject

Has Abstract

pub_date

1987-08-25 00:00:00

pages

6607-24

issue

16

eissn

0305-1048

issn

1362-4962

journal_volume

15

pub_type

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