Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity

Kishor K Bhakat, Tapas K. Hazra, Sankar Mitra

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

Post-translational modifications of proteins, including acetylation, modulate their cellular functions. Several human DNA replication and repair enzymes have recently been shown to be acetylated, leading to their inactivation in some cases. Here we show that the transcriptional coactivator p300 stably interacts with, and acetylates, the recently discovered human DNA glycosylase NEIL2, involved in the repair of oxidized bases both in vivo and in vitro. Lys49 and Lys153 were identified as the major acetylation sites in NEIL2. Acetylation of Lys49, conserved among Nei orthologs, or its mutation to Arg inactivates both base excision and AP lyase activities, while acetylation of Lys153 has no effect. Reversible acetylation of Lys49 could thus regulate the repair activity of NEIL2 in vivo.

Original languageEnglish (US)
Pages (from-to)3033-3039
Number of pages7
JournalNucleic Acids Research
Volume32
Issue number10
DOIs
StatePublished - Aug 16 2004

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DNA Glycosylases
Acetylation
DNA-(Apurinic or Apyrimidinic Site) Lyase
DNA Repair Enzymes
Post Translational Protein Processing
DNA Replication
Mutation

ASJC Scopus subject areas

  • Genetics

Cite this

Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity. / Bhakat, Kishor K; Hazra, Tapas K.; Mitra, Sankar.

In: Nucleic Acids Research, Vol. 32, No. 10, 16.08.2004, p. 3033-3039.

Research output: Contribution to journalArticle

Bhakat, Kishor K ; Hazra, Tapas K. ; Mitra, Sankar. / Acetylation of the human DNA glycosylase NEIL2 and inhibition of its activity. In: Nucleic Acids Research. 2004 ; Vol. 32, No. 10. pp. 3033-3039.
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