Ontology highlight
ABSTRACT:
SUBMITTER: Slyvka A
PROVIDER: S-EPMC7145662 | biostudies-literature | 2019 Dec
REPOSITORIES: biostudies-literature
Slyvka Anton A Zagorskaitė Evelina E Czapinska Honorata H Sasnauskas Giedrius G Bochtler Matthias M
Nucleic acids research 20191201 22
EcoKMcrA from Escherichia coli restricts CpG methylated or hydroxymethylated DNA, and may act as a barrier against host DNA. The enzyme consists of a novel N-terminal specificity domain that we term NEco, and a C-terminal catalytic HNH domain. Here, we report that NEco and full-length EcoKMcrA specificities are consistent. NEco affinity to DNA increases more from hemi- to full-methylation than from non- to hemi-methylation, indicating cooperative binding of the methyl groups. We determined the c ...[more]