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Published online 2 June 2004

Nucleic Acids Research, 2004, Vol. 32, No. 10 3033-3039
© 2004 Oxford University Press

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

Kishor K. Bhakat, Tapas K. Hazra and Sankar Mitra*

Sealy Center for Molecular Science and Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555-1079, USA

*To whom correspondence should be addressed. Tel: +1 409 772 1780; Fax: +1 409 747 8608; Email: samitra{at}utmb.edu

Received April 5, 2004; Revised and Accepted May 12, 2004

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.


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