Results 41 to 50 of about 6,780 (207)

Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex. [PDF]

open access: yesPLoS ONE, 2013
We report a crystal structure of Hfq and catalase HPII from Escherichia coli. The post-transcriptional regulator Hfq plays a key role in the survival of bacteria under stress.
Koji Yonekura   +5 more
doaj   +1 more source

Identifying and characterizing Hfq–RNA interactions [PDF]

open access: yesMethods, 2013
To regulate stress responses and virulence, bacteria use small regulatory RNAs (sRNAs). These RNAs can up or down regulate target mRNAs through base pairing by influencing ribosomal access and RNA decay. A large class of these sRNAs, called trans-encoded sRNAs, requires the RNA binding protein Hfq to facilitate base pairing between the regulatory RNA ...
M A, Faner, A L, Feig
openaire   +2 more sources

Hfq- and sRNA-mediated regulation in Neisseria meningitidis

open access: yes, 2021
Neisseria meningitidis, also known as the meningococcus, is a human-specific pathogen that commonly colonises the nasopharynx without causing disease. For reasons unknown, N.
Jens Karlsson (18677893)
core   +1 more source

Hfq mutation confers increased cephalosporin resistance in Klebsiella pneumoniae [PDF]

open access: yesArchives of Biological Sciences, 2017
Klebsiella pneumoniae (K. pneumoniae), is an opportunistic pathogen raising significant public health concerns owing to its multi-drug resistance. Hfq, one of the main RNA-binding proteins, is a key post-transcriptional regulator.
Li Xinran   +7 more
doaj   +1 more source

Clostridium difficile Hfq can replace Escherichia coli Hfq for most of its function [PDF]

open access: yesRNA, 2014
A gene for the Hfq protein is present in the majority of sequenced bacterial genomes. Its characteristic hexameric ring-like core structure is formed by the highly conserved N-terminal regions. In contrast, the C-terminal forms an extension, which varies in length, lacks homology, and is predicted to be unstructured.
J., Caillet   +3 more
openaire   +3 more sources

Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq [PDF]

open access: yesAntibiotics, 2021
Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance for bacterial adaptation and survival in hosts.
Florian Turbant   +6 more
openaire   +3 more sources

The Pleiotropic Phenotypes Caused by an hfq Null Mutation in Vibrio harveyi

open access: yesMicroorganisms, 2023
Hfq is a global regulator and can be involved in multiple cellular processes by assisting small regulatory RNAs (sRNAs) to target mRNAs. To gain insight into the virulence regulation of Hfq in Vibrio harveyi, the hfq null mutant, ∆hfq, was constructed in
Yiqin Deng   +5 more
doaj   +1 more source

Characterization of Vibrio cholerae Hfq Provides Novel Insights into the Role of the Hfq C-Terminal Region

open access: yesJournal of Molecular Biology, 2012
Hfq is a bacterial RNA binding protein that facilitates small RNA-mediated posttranscriptional gene regulation. In Vibrio cholerae, Hfq and four Hfq-dependent small RNAs are essential for the expression of virulence genes, but little is known about this mechanism at the molecular level. To better understand V.
Vincent, H.   +9 more
openaire   +4 more sources

Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure

open access: yesCommunications Biology, 2023
Hfq is a pleitropic actor that serves as stress response and virulence factor in the bacterial cell. To execute its multiple functions, Hfq assembles into symmetric torus-shaped hexamers.
Mélanie Berbon   +8 more
doaj   +1 more source

Central role for RNase YbeY in Hfq-dependent and Hfq-independent small-RNA regulation in bacteria [PDF]

open access: yesBMC Genomics, 2014
Conceptual parallels exist between bacterial and eukaryotic small-RNA (sRNA) pathways, yet relatively little is known about which protein may recognize and recruit bacterial sRNAs to interact with targets. In eukaryotes, Argonaute (AGO) proteins discharge such functions.
Pandey, Shree P.   +5 more
openaire   +4 more sources

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