The RNA chaperone StpA enables fast RNA refolding by destabilization of mutually exclusive base pairs within competing secondary structure elements. [PDF]
Nucleic Acids Res, 2021 In bacteria RNA gene regulatory elements refold dependent on environmental clues between two or more long-lived conformational states each associated with a distinct regulatory state.
Hohmann KF +3 more
europepmc +2 more sources
Dynamic interactions between the RNA chaperone Hfq, small regulatory RNAs, and mRNAs in live bacterial cells. [PDF]
Elife, 2021 RNA-binding proteins play myriad roles in regulating RNAs and RNA-mediated functions. In bacteria, the RNA chaperone Hfq is an important post-transcriptional gene regulator.
Park S +8 more
europepmc +2 more sources
The Sac10b homolog from Sulfolobus islandicus is an RNA chaperone. [PDF]
Nucleic Acids Res, 2020 Nucleic acid-binding proteins of the Sac10b family, also known as Alba, are widely distributed in Archaea. However, the physiological roles of these proteins have yet to be clarified.
Zhang N, Guo L, Huang L.
europepmc +2 more sources
CISP, an Intrinsically Disordered Cold‐Inducible Barley Protein, Functions as a Small RNA Chaperone [PDF]
Plant DirectLow temperatures are a major environmental stress that limits plant growth and development. Understanding the molecular mechanism of cold tolerance is therefore essential for improving crop performance through molecular breeding.
Yutaro Okumura +2 more
doaj +2 more sources
Dissecting RNA chaperone activity [PDF]
RNA, 2007 Many RNA-binding proteins help RNAs to fold via their RNA chaperone activity. This term has been used widely without accounting for the diversity of the observed reactions, which include complex events like restructuring of misfolded catalytic RNAs, promoting the assembly of RNA-protein complexes, and mediating RNA–RNA interactions.
Rajkowitsch, Lukas, Schroeder, Renée
openaire +3 more sources
Conserved TRAM Domain Functions as an Archaeal Cold Shock Protein via RNA Chaperone Activity
Frontiers in Microbiology, 2017 Cold shock proteins (Csps) enable organisms to acclimate to and survive in cold environments and the bacterial CspA family exerts the cold protection via its RNA chaperone activity.
Bo Zhang +10 more
doaj +2 more sources
Neuron, 2017 Summary Microsatellite expansion disorders are pathologically characterized by RNA foci formation and repeat-associated non-AUG (RAN) translation. However, their underlying pathomechanisms and regulation of RAN translation remain unknown.
Christopher Pearson +2 more
exaly +2 more sources
Structural and functional analysis of a plant nucleolar RNA chaperone-like protein [PDF]
Scientific Reports, 2023 Ribosome biogenesis is a key process in all eukaryotic cells that requires hundreds of ribosome biogenesis factors (RBFs), which are essential to build the mature ribosomes consisting of proteins and rRNAs.
Rita Fernandes +8 more
doaj +2 more sources
The bacterial endoribonuclease RNase E can cleave RNA in the absence of the RNA chaperone Hfq. [PDF]
J Biol Chem, 2019 RNase E is a component of the RNA degradosome complex and plays a key role in RNA degradation and maturation in Escherichia coli. RNase E–mediated target RNA degradation typically involves the RNA chaperone Hfq and requires small guide RNAs (sRNAs ...
Baek YM +6 more
europepmc +2 more sources
The DEAD-box helicase eIF4A1/2 acts as RNA chaperone during mitotic exit enabling chromatin decondensation [PDF]
Nature CommunicationsDuring mitosis, chromosomes condense and decondense to segregate faithfully and undamaged. The exact molecular mechanisms are not well understood. We identify the DEAD-box helicase eIF4A1/2 as a critical factor in this process.
Ramona Jühlen +15 more
doaj +2 more sources