Results 21 to 30 of about 92,611 (279)

RNA modification enzyme TruB is a tRNA chaperone [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2016
Significance RNAs are intimately involved in numerous cellular functions such as gene expression. Typically, RNAs adopt a 3D fold, and their sequences may be chemically altered to contain modified nucleotides such as pseudouridines. There are many RNA modification enzymes, but often their cellular functions remain unknown.
Govardhan Reddy Veerareddygari   +2 more
exaly   +3 more sources

Functional Characterization of Acinetobacter baumannii Lacking the RNA Chaperone Hfq [PDF]

open access: yesFrontiers 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   +2 more sources

Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry [PDF]

open access: yesProceedings of the National Academy of Sciences of the United States of America, 2022
Samantha Sarni   +2 more
exaly   +2 more sources

Transcription complexes as RNA chaperones [PDF]

open access: yesTranscription, 2021
To exert their functions, RNAs adopt diverse structures, ranging from simple secondary to complex tertiary and quaternary folds. In vivo, RNA folding starts with RNA transcription, and a wide variety of processes are coupled to co-transcriptional RNA folding events, including the regulation of fundamental transcription dynamics, gene regulation by ...
Nelly Said, Markus C. Wahl
openaire   +3 more sources

SARS-CoV-2 nucleocapsid protein variants have differential RNA chaperone activity. [PDF]

open access: yesFEBS J
The single-stranded RNA genome of the SARS-CoV-2 virus is characterized by a complex secondary structure formed by patches of intramolecular RNA double-strands.
Babl S   +11 more
europepmc   +2 more sources

RNAs as chaperones [PDF]

open access: yesRNA Biology, 2016
Recently, we found that RNA is a remarkably powerful chaperone that can bind to unfolded proteins and transfer them to Hsp70 for refolding. Combined with past studies on RNA-chaperone interactions, we propose a model for how chaperone RNA activity may contribute to the cellular response to stress.
Scott, Horowitz, James C A, Bardwell
openaire   +2 more sources

Rotavirus RNA chaperone mediates global transcriptome-wide increase in RNA backbone flexibility. [PDF]

open access: yesNucleic Acids Res, 2022
In molecular biology, ribonucleic acid (RNA) has long been an underrated and under-estimated macromolecule. RNA was once thought of as merely a messenger between DNA(deoxyribose nucleic acid), its chemical cousin, and protein.
Coria A   +5 more
europepmc   +2 more sources

RNA chaperones encoded by RNA viruses [PDF]

open access: yesVirologica Sinica, 2015
RNAs are functionally diverse macromolecules whose proper functions rely strictly upon their correct tertiary structures. However, because of their high structural flexibility, correct folding of RNAs is challenging and slow. Therefore, cells and viruses encode a variety of RNA remodeling proteins, including helicases and RNA chaperones. In RNA viruses,
Yang, Jie   +3 more
openaire   +2 more sources

RNA Chaperones, RNA Annealers and RNA Helicases [PDF]

open access: yesRNA Biology, 2007
RNA molecules face difficulties when folding into their native structures. In the cell, proteins can assist RNAs in reaching their functionally active states by binding and stabilizing a specific structure or, in a quite opposite way, by interacting in a non-specific manner. These proteins can either facilitate RNA-RNA interactions in a reaction termed
Rajkowitsch, Lukas   +9 more
openaire   +3 more sources

The ribosome can prevent aggregation of partially folded protein intermediates: studies using the Escherichia coli ribosome. [PDF]

open access: yesPLoS ONE, 2014
BACKGROUND: Molecular chaperones that support de novo folding of proteins under non stress condition are classified as chaperone 'foldases' that are distinct from chaperone' holdases' that provide high affinity binding platform for unfolded proteins and ...
Bani Kumar Pathak   +3 more
doaj   +1 more source

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