Poster abstracts
Poster number 19 submitted by Daniel Binzel
Sterical configuration beyond conformation to RNA-protein interaction for executing functions in biological systems
Aliza Klein (Center for RNA Nanobiotechnology and Nanomedicine; College of Pharmacy, Division of Pharmaceutics and Pharmacology; College of Medicine and James Comprehensive Cancer Center. The Ohio State University), Daniel W Binzel (Center for RNA Nanobiotechnology and Nanomedicine; College of Pharmacy, Division of Pharmaceutics and Pharmacology; College of Medicine and James Comprehensive Cancer Center. The Ohio State University), Peixuan Guo (Center for RNA Nanobiotechnology and Nanomedicine; College of Pharmacy, Division of Pharmaceutics and Pharmacology; College of Medicine and James Comprehensive Cancer Center. The Ohio State University)
Abstract:
RNA has been known to regulate cellular functions in part by interacting with protein through mechanisms of electrostatic interaction, conformation capture, and induced fit. Most of the human genome that does not code for proteins codes for non-coding RNA. One non-coding RNA from bacterial virus phi29 has been shown to form a hexameric ring that gears the phi29 DNA packaging motor by interacting with the motor connector protein. Here we report that configuration instead of conformation plays a key role in governing the RNA/protein interaction to make the packing motor work. Configuration is the spatial arrangement of molecules that cannot be easily interconverted, while conformation is the arrangement of molecules that can easily interconvert. The connector is promiscuous toward any form of RNA and DNA, whether single or double stranded, sequence-specific or nonspecific. It was found that the interaction of the connector with these nucleotides resulted in the formation of a heptameric rosette rather than a hexameric ring of pRNA. Since there is no conformational change in the connector before and after rosette assembly, the rosette formation depends on spatial configuration. However, pRNA interaction with the connector while the procapsid protein shell is present results in the formation of a functional hexameric RNA ring that gears DNA into the procapsid. This is because the capsid’s configuration enables the 5'-3' paired domain of the pRNA to extend away from the capsid protein, enabling intermolecular hand-in-hand interaction between the pRNA molecules. These findings highlight the importance of spatial configuration rather than conformation in the RNA protein interaction process. It is expected that configuration might play an essential role in the assembly of RNA protein machinery in human or animal cells.
Keywords: Steric Configuration, RNA-protein interactions