Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein

Lien B Lai¹, Hong-Duc Phan², Walter J Zahurancik¹, Venkat Gopalan³

Affiliations

¹ Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
² Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA; Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.
³ Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA; Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. Electronic address: gopalan.5@osu.edu.

PMID: 32891515
DOI: 10.1016/j.tibs.2020.08.002

Comment

Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein

Lien B Lai et al. Trends Biochem Sci. 2020 Oct.

. 2020 Oct;45(10):825-828.

doi: 10.1016/j.tibs.2020.08.002. Epub 2020 Sep 2.

Authors

Lien B Lai¹, Hong-Duc Phan², Walter J Zahurancik¹, Venkat Gopalan³

Affiliations

¹ Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA.
² Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA; Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA.
³ Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Center for RNA Biology, The Ohio State University, Columbus, OH 43210, USA; Ohio State Biochemistry Program, The Ohio State University, Columbus, OH 43210, USA. Electronic address: gopalan.5@osu.edu.

PMID: 32891515
DOI: 10.1016/j.tibs.2020.08.002

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.

Keywords: RNase MRP; RNase P; alternative topologies; neofunctionalization.

PubMed Disclaimer

Comment on

Structural insight into precursor ribosomal RNA processing by ribonuclease MRP.
Lan P, Zhou B, Tan M, Li S, Cao M, Wu J, Lei M. Lan P, et al. Science. 2020 Aug 7;369(6504):656-663. doi: 10.1126/science.abc0149. Epub 2020 Jun 25. Science. 2020. PMID: 32586950
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.
Perederina A, Li D, Lee H, Bator C, Berezin I, Hafenstein SL, Krasilnikov AS. Perederina A, et al. Nat Commun. 2020 Jul 10;11(1):3474. doi: 10.1038/s41467-020-17308-z. Nat Commun. 2020. PMID: 32651392 Free PMC article.

Publication types

Actions
Actions
Actions

MeSH terms

Actions
Actions
Actions
Actions
Actions
Actions
Actions
Actions

Substances

Actions
Actions
Actions
Actions
Actions
Actions
Actions

LinkOut - more resources

Molecular Biology Databases
- Saccharomyces Genome Database

Save citation to file

Email citation

Add to Collections

Add to My Bibliography

Your saved search

Create a file for external citation management software

Your RSS Feed

Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein

Affiliations

Alternative Protein Topology-Mediated Evolution of a Catalytic Ribonucleoprotein

Authors

Affiliations

Abstract

Comment on

Publication types

MeSH terms

Substances

LinkOut - more resources

Molecular Biology Databases