RAD18-dependent recruitment of SNM1A to DNA repair complexes by a ubiquitin-binding zinc finger

Kailin Yang, George Lucian Moldovan, Alan D. D'Andrea

Research output: Contribution to journalArticlepeer-review

41 Scopus citations

Abstract

SNM1A is a member of the SNM1 family of nucleases required for cellular processing of interstrand DNA crosslinks (ICLs). Little is known about the molecular function of SNM1A, in terms of its recruitment to ICL lesions or its DNA damage processing activity. Here we show that SNM1A contains a functional PIP box (PCNA-interacting protein box) and a UBZ (ubiquitin binding zinc finger), required for assembly ofSNM1A into nuclear focus. Moreover, RAD18-dependent monoubiquitination of PCNA is required for Mitomycin C and Ultraviolet Light inducible SNM1A nuclear focus assembly. Taken together, our results identify a novel RAD18-PCNA(Ub)-SNM1A pathway required for nuclear focus formation and ICL resistance.

Original languageEnglish (US)
Pages (from-to)19085-19091
Number of pages7
JournalJournal of Biological Chemistry
Volume285
Issue number25
DOIs
StatePublished - Jun 18 2010

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'RAD18-dependent recruitment of SNM1A to DNA repair complexes by a ubiquitin-binding zinc finger'. Together they form a unique fingerprint.

Cite this