Format

Send to

Choose Destination
Nucleic Acids Res. 2004 Jun 2;32(10):3033-9. Print 2004.

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

Author information

1
Sealy Center for Molecular Science and Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, TX 77555-1079, USA.

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.

PMID:
15175427
PMCID:
PMC434438
DOI:
10.1093/nar/gkh632
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Silverchair Information Systems Icon for PubMed Central
Loading ...
Support Center