CONCR lncRNA organizes a 3´-end structural domain that engages DDX11 for DNA replication and sister chromatid cohesion

Despite its activity, it remains unknown whether it contains structural elements essential for its function. To address this gap, we determined CONCR structural organization and its functional relevance, by integrating SHAPE-MaP, AFM, evolutionary analyses, cryo-EM, and cellular genetic studies.

CONCR molecular topology is modular, with highly structured domains connected by flexible linkers. The longest and the most complex is the 3’-end domain, which comprises two helical arms connecting two multiway junctions with structural motifs conserved among all primate groups. This domain is responsible for binding to DDX11 helicase in vitro and in vivo, can trigger DDX11 ATPase activity, and is essential for proper DNA replication and sister chromatid cohesion.