Transient DNA binding by a proteolytic peptide from m5C-DNA methyltransferase Msp I

Sanjoy K Bhattacharya, Ashok K. Dubey

Research output: Contribution to journalArticle

Abstract

A peptide fragment (p26) generated as a result of limited tryptic proteolysis of methyltransferase Msp I 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 Msp I, 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.Msp I. 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.

Original languageEnglish
Pages (from-to)357-364
Number of pages8
JournalJournal of Biochemistry, Molecular Biology and Biophysics
Volume6
Issue number5
DOIs
StatePublished - Oct 1 2002
Externally publishedYes

Fingerprint

Methyltransferases
Peptide Fragments
Proteolysis
S-Adenosylmethionine
Peptides
DNA
Protein Binding
Amino Acid Sequence
Proteins
Amino Acids
m(5)C rRNA methyltransferase

Keywords

  • DNA binding
  • Methyltransferase Msp I
  • Protein
  • Proteolysis

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics
  • Biophysics

Cite this

Transient DNA binding by a proteolytic peptide from m5C-DNA methyltransferase Msp I. / Bhattacharya, Sanjoy K; Dubey, Ashok K.

In: Journal of Biochemistry, Molecular Biology and Biophysics, Vol. 6, No. 5, 01.10.2002, p. 357-364.

Research output: Contribution to journalArticle

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N2 - A peptide fragment (p26) generated as a result of limited tryptic proteolysis of methyltransferase Msp I 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 Msp I, 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.Msp I. 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.

AB - A peptide fragment (p26) generated as a result of limited tryptic proteolysis of methyltransferase Msp I 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 Msp I, 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.Msp I. 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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