An engineered split M.HhaI-zinc finger fusion lacks the intended methyltransferase specificity

Glenna E. Meister, Srinivasan Chandrasegaran, Marc Ostermeier

Research output: Contribution to journalArticlepeer-review

Abstract

The ability to site-specifically methylate DNA in vivo would have wide applicability to the study of basic biomedical problems as well as enable studies on the potential of site-specific DNA methylation as a therapeutic strategy for the treatment of diseases. Natural DNA methyltransferases lack the specificity required for these applications. Nomura and Barbas [W. Nomura, C.F. Barbas 3rd, In vivo site-specific DNA methylation with a designed sequence-enabled DNA methylase, J. Am. Chem. Soc. 129 (2007) 8676-8677] have reported that an engineered DNA methyltransferase comprised of fragments of M.HhaI methyltransferase and zinc finger proteins has very high specificity for the chosen target site. Our analysis of this engineered enzyme shows that the fusion protein methylates target and non-target sites with similar efficiency.

Original languageEnglish (US)
Pages (from-to)226-230
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume377
Issue number1
DOIs
StatePublished - Dec 5 2008

Keywords

  • DNA methylation
  • Protein engineering
  • Zinc fingers

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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