ArticleRNA biology2015
M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding.
Article in RNA biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Article
- Suppression of theRNA (New York, N.Y.) · 2024Article
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- RNA-dependent proteome solubility maintenance inRNA biology · 2024Article
- RNA multimerization as an organizing force for liquid-liquid phase separation.RNA (New York, N.Y.) · 2022Review
- TAR RNA Mediated Folding of a Single-Arginine-Mutant HIV-1 Tat Protein within HeLa Cells Experiencing Intracellular Crowding.International journal of molecular sciences · 2021Article
- Chaperna: linking the ancient RNA and protein worlds.RNA biology · 2021Review
- G-Quadruplexes act as sequence-dependent protein chaperones.EMBO reports · 2020Article
- Built-in RNA-mediated chaperone (chaperna) for antigen folding tailored to immunized hosts.Biotechnology and bioengineering · 2020Article
- Generation of pre-tRNAs from polycistronic operons is the essential function of RNase P in Escherichia coli.Nucleic acids research · 2020Article
- Stabilization of Intrinsically Disordered DKK2 Protein by Fusion to RNA-Binding Domain.International journal of molecular sciences · 2019Article
- Bacterial ribonucleases and their roles in RNA metabolism.Critical reviews in biochemistry and molecular biology · 2019Review
- Conversion of a soluble protein into a potent chaperone in vivo.Scientific reports · 2019Article
- Quality Screening of Incorrectly Folded Soluble Aggregates from Functional Recombinant Proteins.International journal of molecular sciences · 2019Article
- Nucleic Acid-Dependent Structural Transition of the Intrinsically Disordered N-Terminal Appended Domain of Human Lysyl-tRNA Synthetase.International journal of molecular sciences · 2018Article
- Harnessing an RNA-mediated chaperone for the assembly of influenza hemagglutinin in an immunologically relevant conformation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Chaperna-Mediated Assembly of Ferritin-Based Middle East Respiratory Syndrome-Coronavirus Nanoparticles.Frontiers in immunology · 2018Article
- Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
It is one of the fundamental questions in biology how proteins efficiently fold into their native conformations despite off-pathway events such as misfolding and aggregation in living cells. Although molecular chaperones have been known to assist the de novo folding of certain types of proteins, the role of a binding partner (or a ligand) in the folding and in-cell solubility of its interacting protein still remains poorly defined. RNase P is responsible for the maturation of tRNAs as adaptor molecules of amino acids in ribosomal protein synthesis. The RNase P from Escherichia coli, composed of M1 RNA and C5 protein, is a prototypical ribozyme in which the RNA subunit contains the catalytic activity. Using E. coli RNase P, we demonstrate that M1 RNA plays a pivotal role in the in-cell solubility of C5 protein both in vitro and in vivo. Mutations in either the C5 protein or M1 RNA that affect their interactions significantly abolished the folding of C5 protein. Moreover, we find that M1 RNA provides quality insurance of interacting C5 protein, either by promoting the degradation of C5 mutants in the presence of functional proteolytic machinery, or by abolishing their solubility if the machinery is non-functional. Our results describe a crucial role of M1 RNA in the folding, in-cell solubility, and, consequently, the proteostasis of the client C5 protein, giving new insight into the biological role of RNAs as chaperones and mediators that ensure the quality of interacting proteins.
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