The Human RNA Helicase DDX21 Presents a Dimerization Interface Necessary for Helicase Activity
María J. Marcaida, Annamaria Kauzlaric, Alice Duperrex, Jenny Sülzle, Martin C. Moncrieffe, Damilola Adebajo, Suliana Manley, Didier Trono, Matteo Dal Peraro
Abstract
helicase assays indicate that an intact dimer is essential for both DDX21 ATP-dependent double-stranded RNA unwinding and ATP-independent G-quadruplex remodeling activities. Our results suggest that oligomerization plays a key role in regulating RNA DEAD-box helicase activity.
Topics & Concepts
RNA Helicase AHelicaseRNACell biologyDEAD boxChemistryBiologyBiochemistryComputational biologyGeneRNA and protein synthesis mechanismsRNA Research and SplicingRNA modifications and cancer