Structural basis of rotavirus RNA chaperone displacement and RNA annealing. [PDF]
Proc Natl Acad Sci U S A, 2021 Significance Accurate RNA folding is essential for virus replication. Rotaviruses are viruses infecting humans and animals. Rotavirus genome comprises 11 distinct RNAs, and successful replication requires the incorporation of all 11 RNAs into a virion ...
Bravo JPK +10 more
europepmc +7 more sources
Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2022 RNA-binding proteins contain intrinsically disordered regions whose functions in RNA recognition are poorly understood. The RNA chaperone Hfq is a homohexamer that contains six flexible C-terminal domains (CTDs). The effect of the CTDs on Hfq’s integrity
Samantha Sarni, Jorjethe Roca, Chen Du
exaly +3 more sources
The archaeal RNA chaperone TRAM0076 shapes the transcriptome and optimizes the growth of Methanococcus maripaludis. [PDF]
PLoS Genetics, 2019 TRAM is a conserved domain among RNA modification proteins that are widely distributed in various organisms. In Archaea, TRAM occurs frequently as a standalone protein with in vitro RNA chaperone activity; however, its biological significance and ...
Jie Li +8 more
doaj +3 more sources
Acidic C-terminal domains autoregulate the RNA chaperone Hfq [PDF]
eLife, 2017 The RNA chaperone Hfq is an Sm protein that facilitates base pairing between bacterial small RNAs (sRNAs) and mRNAs involved in stress response and pathogenesis. Hfq possesses an intrinsically disordered C-terminal domain (CTD) that may tune the function
Andrew Santiago-Frangos +3 more
doaj +3 more sources
The RGG/RG motif of AUF1 isoform p45 is a key modulator of the protein’s RNA chaperone and RNA annealing activities [PDF]
RNA Biology, 2019 The RNA-binding protein AUF1 regulates post-transcriptional gene expression by affecting the steady state and translation levels of numerous target RNAs.
Tobias Schmidt +2 more
exaly +3 more sources
Functional Characterization of Acinetobacter baumannii Lacking the RNA Chaperone Hfq [PDF]
Frontiers in Microbiology, 2017 The RNA chaperone Hfq is involved in the riboregulation of diverse genes via small RNAs. Recent studies have demonstrated that Hfq contributes to the stress response and the virulence of several pathogens, and the roles of Hfq vary among bacterial ...
Han-Yueh Kuo +9 more
doaj +3 more sources
Crosstalk between the tRNA methyltransferase Trm1 and RNA chaperone La influences eukaryotic tRNA maturation. [PDF]
J Biol Chem, 2023 tRNAs undergo an extensive maturation process involving post-transcriptional modifications often associated with tRNA structural stability and promoting the native fold.
Porat J +5 more
europepmc +2 more sources
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