NYMC Faculty Publications

Identification of RNF8 as a Ubiquitin Ligase Involved in Targeting the p12 Subunit of DNA Polymerase δ for Degradation in Response to DNA Damage

Author Type(s)

Faculty

DOI

10.1074/jbc.M112.423392

Journal Title

The Journal of Biological Chemistry

First Page

2941

Last Page

2950

Document Type

Article

Publication Date

2-1-2013

Department

Biochemistry and Molecular Biology

Keywords

Animals, DNA Damage, DNA Polymerase III, DNA-Binding Proteins, Half-Life, HeLa Cells, Histones, Humans, Mice, Mice, Knockout, Models, Biological, Polyubiquitin, Protein Transport, Proteolysis, RNA, Small Interfering, Recombinant Fusion Proteins, Subcellular Fractions, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases, Ubiquitination, Ultraviolet Rays

Disciplines

Medicine and Health Sciences

Abstract

DNA polymerase δ consists of four subunits, one of which, p12, is degraded in response to DNA damage through the ubiquitin-proteasome pathway. However, the identities of the ubiquitin ligase(s) that are responsible for the proximal biochemical events in triggering proteasomal degradation of p12 are unknown. We employed a classical approach to identifying a ubiquitin ligase that is involved in p12 degradation. Using UbcH5c as ubiquitin-conjugating enzyme, a ubiquitin ligase activity that polyubiquitinates p12 was purified from HeLa cells. Proteomic analysis revealed that RNF8, a RING finger ubiquitin ligase that plays an important role in the DNA damage response, was the only ubiquitin ligase present in the purified preparation. In vivo, DNA damage-induced p12 degradation was significantly reduced by shRNA knockdown of RNF8 in cultured human cells and in RNF8(-/-) mouse epithelial cells. These studies provide the first identification of a ubiquitin ligase activity that is involved in the DNA damage-induced destruction of p12. The identification of RNF8 allows new insights into the integration of the control of p12 degradation by different DNA damage signaling pathways.

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