Both an altered DNA structure and cellular proteins are involved in protecting a triplex forming an oligopurine-rich sequence from Dam methylation in E. coli.

Abstract:

:When the 4-bp Dam recognition sequence was placed between two d(GA)7 tracts, it became severely undermethylated in JM101 Escherichia coli cells compared to other Dam sequences in the same plasmid DNA. This site specific undermethylation was also detected on supercoiled molecules in vitro. Mutational analysis indicated that undermethylation is related to the capacity of the oligopurine tract to adopt the H-DNA conformation. In addition, chemical probing of the cells was consistent with a cellular protein bound to the DNA. Therefore it is likely that the combination of altered DNA conformation and a cellular protein leads to Dam-site protection. We also found that the site-specific undermethylation is detectable in certain E. coli strains only.

journal_name

Biochem Genet

journal_title

Biochemical genetics

authors

Klysik J

doi

10.1007/BF02407017

subject

Has Abstract

pub_date

1996-06-01 00:00:00

pages

165-78

issue

5-6

eissn

0006-2928

issn

1573-4927

journal_volume

34

pub_type

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