Results 51 to 60 of about 2,163,835 (311)
Proteins That Chaperone RNA Regulation [PDF]
Microbiology Spectrum, 2018 ABSTRACT RNA-binding proteins chaperone the biological functions of noncoding RNA by reducing RNA misfolding, improving matchmaking between regulatory RNA and targets, and exerting quality control over RNP biogenesis. Recent studies of Escherichia coli CspA, HIV NCp, and E. coli Hfq
Sarah A, Woodson +2 more
openaire +2 more sources
Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism [PDF]
, 2010 For a long time it has been assumed that the decay of RNA in eukaryotes is mainly carried out by exoribonucleases, which is in contrast to bacteria, where endoribonucleases are well documented to initiate RNA degradation.
Tomecki, Rafał, Dziembowski, Andrzej
core +3 more sources
Viruses, 2020 The 3′-terminal stem-loop (3′SL) of the RNA genome of the flavivirus West Nile (WNV) harbors, in its stem, one of the sequence elements that are required for genome cyclization.
Alexandra Meyer +7 more
doaj +1 more source
bioRxiv, 2020 RNA binding proteins play myriad roles in controlling and regulating RNAs and RNA-mediated functions, often through simultaneous binding to other cellular factors. In bacteria, the RNA chaperone Hfq modulates post-transcriptional gene regulation. Absence
Seongjin Park +7 more
semanticscholar +1 more source
Chaperoning 5S RNA assembly [PDF]
Genes & Development, 2015 In eukaryotes, three of the four ribosomal RNAs (rRNAs)—the 5.8S, 18S, and 25S/28S rRNAs—are processed from a single pre-rRNA transcript and assembled into ribosomes. The fourth rRNA, the 5S rRNA, is transcribed by RNA polymerase III and is assembled into the 5S ribonucleoprotein particle (RNP), containing ribosomal proteins Rpl5/uL18 and Rpl11/uL5 ...
Madru, Clément +7 more
openaire +3 more sources
Protein solubility and folding enhancement by interaction with RNA. [PDF]
PLoS ONE, 2008 While basic mechanisms of several major molecular chaperones are well understood, this machinery has been known to be involved in folding of only limited number of proteins inside the cells. Here, we report a chaperone type of protein folding facilitated
Seong Il Choi +12 more
doaj +1 more source
Nature Communications, 2022 In this work, the authors determine the crystal structure of a ProQ/FinO RNA chaperone bound to its RNA target. This provides insight into how this family of bacterial proteins recognize transcriptional terminator structures.
Hyeong Jin Kim +16 more
doaj +1 more source
Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq [PDF]
, 2011 The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily conserved core, whereas the C-terminus is variable in ...
Beich-Frandsen, Mads (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna) +46 more
core +1 more source
The yeast histone chaperone hif1p functions with RNA in nucleosome assembly. [PDF]
PLoS ONE, 2014 Hif1p is an H3/H4-specific histone chaperone that associates with the nuclear form of the Hat1p/Hat2p complex (NuB4 complex) in the yeast Saccharomyces cerevisiae. While not capable of depositing histones onto DNA on its own, Hif1p can act in conjunction
Amy R Knapp, Huanyu Wang, Mark R Parthun
doaj +1 more source
Study of E. coli Hfq's RNA annealing acceleration and duplex destabilization activities using substrates with different GC-contents [PDF]
, 2012 Folding of RNA molecules into their functional three-dimensional structures is often supported by RNA chaperones, some of which can catalyse the two elementary reactions helix disruption and helix formation.
Saxena, Krishna +6 more
core +1 more source