Results 21 to 30 of about 6,261 (210)

The Hfq regulon of Neisseria meningitidis

open access: yesFEBS Open Bio, 2017
The conserved RNA-binding protein, Hfq, has multiple regulatory roles within the prokaryotic cell, including promoting stable duplex formation between small RNAs and mRNAs, and thus hfq deletion mutants have pleiotropic phenotypes.
van der Ende, Arie   +4 more
core   +4 more sources

RNA binding of Hfq monomers promotes RelA-mediated hexamerization in a limiting Hfq environment [PDF]

open access: yesNature Communications, 2021
RelA stimulates RyhB small RNA–target mRNA interaction by promoting assembly of Hfq monomers into hexamers. Here the authors show that RelA-mediated Hfq hexamerization requires an initial binding of RNA to Hfq monomers.
Pallabi Basu   +5 more
doaj   +4 more sources

Defining a role for Hfq in Gram-positive bacteria: evidence for Hfq-dependent antisense regulation in Listeria monocytogenes [PDF]

open access: yesNucleic Acids Research, 2009
Small trans-encoded RNAs (sRNAs) modulate the translation and decay of mRNAs in bacteria. In Gram-negative species, antisense regulation by trans-encoded sRNAs relies on the Sm-like protein Hfq.
Poul Valentin-hansen   +13 more
core   +3 more sources

The RNA chaperone Hfq is involved in stress tolerance and virulence in uropathogenic Proteus mirabilis. [PDF]

open access: yesPLoS ONE, 2014
Hfq is a bacterial RNA chaperone involved in the riboregulation of diverse genes via small noncoding RNAs. Here, we show that Hfq is critical for the uropathogenic Proteus mirabilis to effectively colonize the bladder and kidneys in a murine urinary ...
Min-Cheng Wang   +4 more
doaj   +1 more source

The RNA chaperone Hfq impacts growth, metabolism and production of virulence factors in Yersinia enterocolitica. [PDF]

open access: yesPLoS ONE, 2014
To adapt to changes in environmental conditions, bacteria regulate their gene expression at the transcriptional but also at the post-transcriptional level, e.g. by small RNAs (sRNAs) which modulate mRNA stability and translation.
Tamara Kakoschke   +6 more
doaj   +1 more source

444 Post-translational role of RNA modifications in sRNA chaperone Hfq

open access: yesJournal of Clinical and Translational Science, 2022
OBJECTIVES/GOALS: The goal of this study is to determine the role of the tRNA modifications in the translation of Hfq. Hfq is an RNA chaperone that acts as a co-factor for the action of the largest class of small RNAs in E. coli.
Jalisa Nurse   +2 more
doaj   +1 more source

Hfq is a global regulator that controls the pathogenicity of Staphylococcus aureus. [PDF]

open access: yesPLoS ONE, 2010
The Hfq protein is reported to be an RNA chaperone, which is involved in the stress response and the virulence of several pathogens. In E. coli, Hfq can mediate the interaction between some sRNAs and their target mRNAs.
Yu Liu   +7 more
doaj   +1 more source

RNA reflections: converging on Hfq [PDF]

open access: yesRNA, 2015
As the journal RNA celebrates its 20th anniversary, the role of non-coding RNAs as regulators is firmly established in a broad range of organisms. Among these are the many bacterial RNAs that pair with their targets and regulate mRNA stability and translation. In Escherichia coli and other gram-negative organisms, these small RNAs (sRNAs) depend on Hfq,
Gottesman, Susan, Storz, Gisela
openaire   +2 more sources

Dynamic interactions between the RNA chaperone Hfq, small regulatory RNAs, and mRNAs in live bacterial cells

open access: yeseLife, 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.
Seongjin Park   +8 more
doaj   +1 more source

Hfq: the flexible RNA matchmaker [PDF]

open access: yesCurrent Opinion in Microbiology, 2016
The RNA chaperone protein Hfq is critical to the function of small, base pairing RNAs in many bacteria. In the past few years, structures and modeling of wild type Hfq and assays of various mutants have documented that the homohexameric Hfq ring can contact RNA at four sites (proximal face, distal face, rim and C-terminal tail) and that different RNAs ...
Taylor B Updegrove   +2 more
openaire   +2 more sources

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