Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein. Issue 10 (October 2020)

• Record Type: Journal Article
• Authors: Lai, Lien B.; Phan, Hong-Duc; Zahurancik, Walter J.; Gopalan, Venkat
• Is Part Of: Trends in biochemical sciences. Volume 45:Issue 10(2020)
• Page Start: 825
• Page End: 828
• Publication Date: 2020-10
• Subjects: RNase MRP -- RNase P -- neofunctionalization -- alternative topologies; Biochemistry -- Periodicals; 572
• DOI: 10.1016/j.tibs.2020.08.002
• Languages: English
• ISSNs: 0968-0004

Abstract

Abstract : The high-resolution structures of yeast RNase for mitochondrial RNA processing (MRP), a catalytic ribonucleoprotein (RNP), recently reported by Lan et al. and Perederina et al. illustrate how RNA-mediated selection of alternative protein conformations, sampled during stochastic excursions by polymorphic/metamorphic proteins, enabled RNAs and proteins to mutually influence their functional repertoires and shape RNP evolution.