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  • Title: Transient DNA binding by a proteolytic peptide from m5C-DNA methyltransferase MspI.
    Author: Bhattacharya SK, Dubey AK.
    Journal: J Biochem Mol Biol Biophys; 2002 Oct; 6(5):357-64. PubMed ID: 12385973.
    Abstract:
    A peptide fragment (p26) generated as a result of limited tryptic proteolysis of methyltransferase MspI retains transient but non-specific DNA binding capability. The transient DNA binding by p26 was characterized with respect to physicochemical factors. Limited proteolysis was performed to probe gross structural deviation from the reported two-domain organization for m5C-MTases, in light of topoisomerase activity shown by MspI, resulted in two peptide fragments; a large fragment p26 and a small fragment p18, consistent with the other reported m5C-MTase structures. The purified large peptide fragment p26, spans between 6 and 251 in the amino acid sequence of M.MspI. The peptide p26 does not bind S-adenosylmethionine, although in the intact protein the AdoMet binding region can be mapped to a region in the protein that is present in this peptide. Such transient DNA binding has not been reported for other protolytic product of any other m5C-DNA methyltransferase.
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