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

Biochemical and Biophysical Research Communications
Samia HamimesEric Van Dyck

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.

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Citations

May 12, 2007·Investigational New Drugs·Sibgat A ChoudhuryTerry Y-K Chow
Oct 22, 2011·International Journal of Molecular Sciences·Wei Zhang, Yingyan Yu
Mar 15, 2019·FEBS Open Bio·Guojin XieYong Chang
May 29, 2021·Frontiers in Cell and Developmental Biology·Fan PanRui Wang
Jul 16, 2021·Journal of Cellular and Molecular Medicine·Jun ShengZhengfeng Zhang

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