RAD52 motif-containing protein 1 (RDM1) is involved in DNA damage repair pathway and the cell response to the anti-cancer drug cisplatin [, ]. RDM1 contains a small RD motif that is shared with the recombination and repair protein RAD52, and an RNA recognition motif (RRM). The RD motif is responsible for the acidic pH-dependent DNA-binding properties of RDM1. It interacts with ss- and dsDNA, and may act as a DNA-damage recognition factor by recognizing the distortions of the double helix caused by cisplatin-DNA adducts in vitro. In addition, due to the presence of RRM, RDM1 can bind to RNA as well as DNA [].
This superfamily includes protein RDM1 from Arabidopsis, which is a a small protein that binds single-stranded methyl DNA, and associates and co-localises with RNA polymerase II, AGO4 and DRM2 in the nucleus. RDM1 is a component of the RNA-directed DNA methylation effector complex and may have a role in linking siRNA production with pre-existing or de novo cytosine methylation [].
This family includes protein RDM1 from Arabidopsis, which is a a small protein that binds single-stranded methyl DNA, and associates and co-localises with RNA polymerase II, AGO4 and DRM2 in the nucleus. RDM1 is a component of the RNA-directed DNA methylation effector complex and may have a role in linking siRNA production with pre-existing or de novo cytosine methylation [].
This entry represents the RNA recognition motif (RRM) of RDM1, also termed RAD52 homologue B, a novel factor involved in the cellular response to the anti-cancer drug cisplatin in vertebrates []. RDM1 contains a small RD motif that is shared with the recombination and repair protein RAD52, and an RNA recognition motif (RRM). The RD motif is responsible for the acidic pH-dependent DNA-binding properties of RDM1. It interacts with ss- and dsDNA, and may act as a DNA-damage recognition factor by recognizing the distortions of the double helix caused by cisplatin-DNA adducts in vitro. In addition, due to the presence of RRM, RDM1 can bind to RNA as well as DNA [].
