Ontology highlight
ABSTRACT:
SUBMITTER: Mulligan EA
PROVIDER: S-EPMC2847215 | biostudies-literature | 2010 Apr
REPOSITORIES: biostudies-literature
Mulligan Elizabeth A EA Hatchwell Eli E McCorkle Sean R SR Dunn John J JJ
Nucleic acids research 20091216 6
The Escherichia coli McrA protein, a putative C(5)-methylcytosine/C(5)-hydroxyl methylcytosine-specific nuclease, binds DNA with symmetrically methylated HpaII sequences (Cm5CGG), but its precise recognition sequence remains undefined. To determine McrA's binding specificity, we cloned and expressed recombinant McrA with a C-terminal StrepII tag (rMcrA-S) to facilitate protein purification and affinity capture of human DNA fragments with m5C residues. Sequence analysis of a subset of these fragm ...[more]