Results 31 to 40 of about 11,459 (235)

Hfq Globally Binds and Destabilizes sRNAs and mRNAs in Yersinia pestis

open access: yesmSystems, 2019
Hfq is a ubiquitous Sm-like RNA-binding protein in bacteria involved in physiological fitness and pathogenesis, while its in vivo binding nature remains elusive. Here we reported genome-wide Hfq-bound RNAs in Yersinia pestis, a causative agent of plague,
Yanping Han   +7 more
doaj   +1 more source

Impact of Hfq on global gene expression and intracellular survival in Brucella melitensis. [PDF]

open access: yesPLoS ONE, 2013
Brucella melitensis is a facultative intracellular bacterium that replicates within macrophages. The ability of brucellae to survive and multiply in the hostile environment of host macrophages is essential to its virulence. The RNA-binding protein Hfq is
Mingquan Cui   +17 more
doaj   +1 more source

Hfq binding changes the structure of Escherichia coli small noncoding RNAs OxyS and RprA, which are involved in the riboregulation of rpoS [PDF]

open access: yes, 2013
OxyS and RprA are two small noncoding RNAs (sRNAs) that modulate the expression of rpoS, encoding an alternative sigma factor that activates transcription of multiple Escherichia coli stress-response genes. While RprA activates rpoS for translation, OxyS
Callaghan, Anastasia   +9 more
core   +1 more source

Cycling of RNAs on Hfq [PDF]

open access: yesRNA Biology, 2013
The RNA chaperone Hfq is a key player in small RNA (sRNA)-mediated regulation of target mRNAs in many bacteria. The absence of this protein causes pleiotropic phenotypes such as impaired stress regulation and, occasionally, loss of virulence. Hfq promotes rapid sRNA-target mRNA base pairing to allow for fast, adaptive responses.
openaire   +3 more sources

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   +4 more sources

Study of E. coli Hfq's RNA annealing acceleration and duplex destabilization activities using substrates with different GC-contents [PDF]

open access: yes, 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.
Beich-Frandsen, Mads   +6 more
core   +1 more source

Special Focus Hfq [PDF]

open access: yesRNA Biology, 2013
In all domains of life, non-coding RNAs (ncRNAs) play a central role in cellular biology. In bacteria, the systematic discovery and analysis of ncRNAs revealed a large repertoire of regulatory transcripts, which among other characteristics is responsible for the high adaptability of prokaryotes.
openaire   +2 more sources

The RNA chaperone Hfq is important for growth and stress tolerance in Francisella novicida.

open access: yesPLoS ONE, 2011
The RNA-binding protein Hfq is recognized as an important regulatory factor in a variety of cellular processes, including stress resistance and pathogenesis.
Jacob R Chambers, Kelly S Bender
doaj   +1 more source

A Unique cis-Encoded Small Noncoding RNA Is Regulating Legionella pneumophila Hfq Expression in a Life Cycle-Dependent Manner

open access: yesmBio, 2017
Legionella pneumophila is an environmental bacterium that parasitizes protozoa, but it may also infect humans, thereby causing a severe pneumonia called Legionnaires’ disease. To cycle between the environment and a eukaryotic host, L.
Giulia Oliva   +4 more
doaj   +1 more source

Equivariant aspects of Yang-Mills Floer theory [PDF]

open access: yes, 2001
We use Floer's exact triangle to study the u-map (cup product with the 4-dimensional class) in the Floer cohomology groups of admissible SO(3) bundles over closed, oriented 3-manifolds.
Froyshov, Kim A.
core   +2 more sources

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