Results 31 to 40 of about 10,886 (208)

Adaptive remodeling of the bacterial proteome by specific ribosomal modification regulates Pseudomonas infection and niche colonisation [PDF]

open access: yes, 2016
Post-transcriptional control of protein abundance is a highly important, underexplored regulatory process by which organisms respond to their environments.
A Brencic   +83 more
core   +3 more sources

Lsm proteins and Hfq [PDF]

open access: yesRNA Biology, 2013
The bacterial Hfq protein is a versatile modulator of RNA function and is particularly important for regulation mediated by small non-coding RNAs. Hfq is a bacterial Sm protein but bears more similarity to the eukaryotic Sm-like (Lsm) family of proteins than the prototypical Sm proteins.
Wilusz, Carol J., Wilusz, Jeffrey
openaire   +2 more sources

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

CRP-cAMP mediates silencing of Salmonella virulence at the post-transcriptional level [PDF]

open access: yes, 2018
Invasion of epithelial cells by Salmonella enterica requires expression of genes located in the pathogenicity island I (SPI-1). The expression of SPI-1 genes is very tightly regulated and activated only under specific conditions.
Balsalobre, Carlos   +6 more
core   +4 more sources

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

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

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. Previous proteome and transcriptome studies of Neisseria meningitidis have generated limited insight into differential ...
Robert A. G. Huis in ‘t Veld   +4 more
openaire   +3 more sources

Models of Hfq interactions with small non-coding RNA in Gram-negative and Gram-positive bacteria

open access: yesFrontiers in Cellular and Infection Microbiology, 2023
Hfq is required by many Gram-negative bacteria to chaperone the interaction between small non-coding RNA (sRNA) and mRNA to facilitate annealing. Conversely and despite the presence of Hfq in many Gram-positive bacteria, sRNAs in Gram-positive bacteria ...
Derrick Watkins, Dev Arya
doaj   +1 more source

Discovery Of Ethanol-Responsive Small Rnas In Zymomonas Mobilis [PDF]

open access: yes, 2014
Zymomonas mobilis is a bacterium that can produce ethanol by fermentation. Due to its unique metabolism and efficient ethanol production, Z. mobilis has attracted special interest for biofuel energy applications; an important area of study is the ...
Cho, Seung Hee   +3 more
core   +1 more source

Hfq variant with altered RNA binding functions [PDF]

open access: yesNucleic Acids Research, 2006
The interaction between Hfq and RNA is central to multiple regulatory processes. Using site-directed mutagenesis, we have found a missense mutation in Hfq (V43R) which strongly affects2 the RNA binding capacity of the Hfq protein and its ability to stimulate poly(A) tail elongation by poly(A)-polymerase in vitro.
Ziolkowska, K.   +6 more
openaire   +3 more sources

Home - About - Disclaimer - Privacy