Nucleic acid-binding properties of the RRM-containing protein RDM1

Samia Hamimes, Dominique Bourgeon, Alicja Z. Stasiak, Andrzej Stasiak, Eric Van Dyck*

*Corresponding author for this work

Research output: Contribution to journalArticleResearchpeer-review

12 Citations (Scopus)

Abstract

RDM1 (RAD52 Motif 1) is a vertebrate protein involved in the cellular response to the anti-cancer drug cisplatin. In addition to an RNA recognition motif, RDM1 contains a small amino acid motif, named RD motif, which it shares with the recombination and repair protein, RAD52. RDM1 binds to single- and double-stranded DNA, and recognizes DNA distortions induced by cisplatin adducts in vitro. Here, we have performed an in-depth analysis of the nucleic acid-binding properties of RDM1 using gel-shift assays and electron microscopy. We show that RDM1 possesses acidic pH-dependent DNA-binding activity and that it binds RNA as well as DNA, and we present evidence from competition gel-shift experiments that RDM1 may be capable of discrimination between the two nucleic acids. Based on reported studies of RAD52, we have generated an RDM1 variant mutated in its RD motif. We find that the L119GF → AAA mutation affects the mode of RDM1 binding to single-stranded DNA.

Original languageEnglish
Pages (from-to)87-94
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume344
Issue number1
DOIs
Publication statusPublished - 26 May 2006
Externally publishedYes

Keywords

  • Acidic pH
  • Gel-shift assays
  • Nucleic acid binding
  • RAD52
  • RDM1
  • RRM

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