A new paper entitled “A retroelement-derived mammalian ARC protein exhibits selective RNA recognition and nucleic acid chaperone functions” by Julita Gumna-Mikina, Angelika Andrzejewska-Romanowska, Maciej Antczak, Ewa Tykwińska, Marta Szachniuk, and Katarzyna Pachulska-Wieczorek has been published in Nucleic Acids Research.

The ARC protein plays an important role in the functioning of the nervous system, including synaptic plasticity as well as learning and memory-related processes. A particularly remarkable feature of ARC is its ability to form virus-like structures that enable RNA transport between neurons. Despite the growing number of studies on ARC, the mechanism by which it recognizes RNA has remained poorly understood.

In this study, researchers from the Institute of Bioorganic Chemistry PAS demonstrated for the first time that mammalian ARC specifically binds its own mRNA, and that this selection mechanism is based on the recognition of specific RNA features. The study also showed that ARC can act as a robust nucleic acid chaperone, locally modulating RNA structure.

This research provides new insight into the molecular basis of RNA recognition by the ARC protein and represents an important step toward understanding how this protein may selectively package and transport RNA in neuronal cells.

Link to the publication: https://doi.org/10.1093/nar/gkag207