Results 11 to 20 of about 92,611 (279)
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
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Proteins with RNA Chaperone Activity: A World of Diverse Proteins with a Common Task—Impediment of RNA Misfolding [PDF]
Biochemistry Research International, 2011 Proteins with RNA chaperone activity are ubiquitous proteins that play important roles in cellular mechanisms. They prevent RNA from misfolding by loosening misfolded structures without ATP consumption.
Katharina Semrad
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A Guanosine-Centric Mechanism for RNA Chaperone Function [PDF]
Science, 2013 Simply Folding RNA chaperones simplify what would otherwise be complex and slow RNA folding events. Grohman et al. (p. 190 , published online 7 March) show that the Moloney murine leukemia virus (MuLV) nucleocapsid (NC) protein, which ...
Jacob K, Grohman +6 more
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New Methods in RNA Structural Biology: TELSAM Protein Chaperone Crystallography Applications to Folded RNA [PDF]
Structural DynamicsThe multifaceted roles of RNA in cellular function are becoming increasingly apparent, and the importance of deepening our understanding of the function and structure of ribozymes and non-enzymatic RNAs will continue to grow.
Jacob C Averett +4 more
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Conserved TRAM Domain Functions as an Archaeal Cold Shock Protein via RNA Chaperone Activity [PDF]
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
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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
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BioTechniques, 2007 Proteins with RNA chaperone activity help RNAs to obtain their native conformations, and many of them are active in the two basic reactions—RNA annealing and strand displacement.
Lukas Rajkowitsch, Renée Schroeder
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FinO is an RNA chaperone that facilitates sense-antisense RNA interactions [PDF]
EMBO Journal, 2003 The protein FinO represses F-plasmid conjugative transfer by facilitating interactions between the mRNA of the major F-plasmid transcriptional activator, TraJ, and an antisense RNA, FinP. FinO is known to bind stem-loop structures in both FinP and traJ RNAs; however, the mechanism by which FinO facilitates sense-antisense pairing is poorly understood ...
Ross A Edwards +2 more
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Silencing of natural transformation by an RNA chaperone and a multitarget small RNA [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2016 Significance Natural transformation is a major mechanism of horizontal gene transfer (HGT) by which bacteria take up exogenous DNA directly in their environment and integrate it in their genome. Acquiring new genetic information may confer an adaptive advantage but an uncontrolled uptake of foreign DNA may be harmful. We document
Laetitia Attaiech +2 more
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On the facultative requirement of the bacterial RNA chaperone, Hfq [PDF]
Trends in Microbiology, 2009 The pleiotropic post-transcriptional regulator Hfq is an RNA chaperone that facilitates pairing interactions between small regulatory RNAs (sRNAs) and their mRNA targets in several bacteria. However, this classical pattern, derived from the Escherichia coli model, is not applicable to the whole bacterial kingdom.
Jousselin, Ambre +2 more
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