RNA-Binding Proteins Chaperone Ribonucleoprotein Complex Assembly to Solve the RNA-Folding Problem

Katherine E Bohnsack; Markus T Bohnsack

doi:10.1016/j.cell.2019.11.011

RNA-Binding Proteins Chaperone Ribonucleoprotein Complex Assembly to Solve the RNA-Folding Problem

Cell. 2019 Nov 27;179(6):1248-1250. doi: 10.1016/j.cell.2019.11.011. Epub 2019 Nov 21.

Authors

Katherine E Bohnsack¹, Markus T Bohnsack²

Affiliations

¹ Department of Molecular Biology, University Medical Center Göttingen, 37073 Göttingen, Germany. Electronic address: katherine.bohnsack@med.uni-goettingen.de.
² Department of Molecular Biology, University Medical Center Göttingen, 37073 Göttingen, Germany; Göttingen Centre for Molecular Biosciences, Georg-August-University, 37077 Göttingen, Germany. Electronic address: markus.bohnsack@med.uni-goettingen.de.

PMID: 31761531
DOI: 10.1016/j.cell.2019.11.011

Abstract

The inherent tendency of RNAs to misfold is a major problem that can impede efficient assembly of essential ribonucleoprotein complexes (RNPs), such as ribosomes. In this issue of Cell, Duss et al., (2019) and Rodgers and Woodson (2019) reveal how transient RNA-protein interactions can chaperone RNA folding during RNP assembly.

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MeSH terms

RNA Folding*
RNA*
RNA, Ribosomal
RNA-Binding Proteins
Ribonucleoproteins
Ribosomes

Substances

RNA, Ribosomal
RNA-Binding Proteins
Ribonucleoproteins
RNA