Results 61 to 70 of about 11,806 (233)

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

Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein [PDF]

open access: yesThe EMBO Journal, 2002
In prokaryotes, Hfq regulates translation by modulating the structure of numerous RNA molecules by binding preferentially to A/U-rich sequences. To elucidate the mechanisms of target recognition and translation regulation by Hfq, we determined the crystal structures of the Staphylococcus aureus Hfq and an Hfq-RNA complex to 1.55 and 2.71 A resolution ...
Schumacher, M.A.   +4 more
openaire   +3 more sources

The Escherichia coli Hfq protein: an unattended DNA-transactions regulator

open access: yesFrontiers in Molecular Biosciences, 2016
The Hfq protein was discovered in Escherichia coli as a host factor for bacteriophage Qβ RNA replication. Subsequent studies indicated that Hfq is a pleiotropic regulator of bacterial gene expression.
Grzegorz M Cech   +6 more
doaj   +1 more source

Bacterial nitrate assimilation: gene distribution and regulation [PDF]

open access: yes, 2011
In the context of the global nitrogen cycle, the importance of inorganic nitrate for the nutrition and growth of marine and freshwater autotrophic phytoplankton has long been recognized.
Andrew J. Gates   +44 more
core   +1 more source

A quantitative comparison of sRNA-based and protein-based gene regulation [PDF]

open access: yes, 2008
Small, non-coding RNAs (sRNAs) play important roles as genetic regulators in prokaryotes. sRNAs act post-transcriptionally via complementary pairing with target mRNAs to regulate protein expression.
Berg HC   +5 more
core   +3 more sources

An unexpected co-crystal structure of the calpain PEF(S) domain with Hfq reveals a potential chaperone function of Hfq [PDF]

open access: yesActa Crystallographica Section F Structural Biology Communications, 2020
Calpain is a Ca2+-activated, heterodimeric cysteine protease consisting of a large catalytic subunit and a small regulatory subunit. Dysregulation of this enzyme is involved in a range of pathological conditions such as cancer, Alzheimer's disease and rheumatoid arthritis, and thus calpain I is a drug target with potential therapeutic applications ...
Cresser-Brown, Joel   +5 more
openaire   +5 more sources

No detectable effect of RNA-binding protein Hfq absence in Staphylococcus aureus

open access: yesBMC Microbiology, 2007
Background The RNA-binding protein Hfq is involved in stress and virulence of several pathogens, probably due to its role as mediator in small RNA (sRNA)-mRNA interactions.
Bouloc Philippe   +2 more
doaj   +1 more source

Reduced heme levels underlie the exponential growth defect of the Shewanella oneidensis hfq mutant. [PDF]

open access: yesPLoS ONE, 2014
The RNA chaperone Hfq fulfills important roles in small regulatory RNA (sRNA) function in many bacteria. Loss of Hfq in the dissimilatory metal reducing bacterium Shewanella oneidensis strain MR-1 results in slow exponential phase growth and a reduced ...
Christopher M Brennan   +9 more
doaj   +1 more source

Orthogonality of Hermite polynomials in superspace and Mehler type formulae [PDF]

open access: yes, 2011
In this paper, Hermite polynomials related to quantum systems with orthogonal O(m)-symmetry, finite reflection group symmetry G < O(m), symplectic symmetry Sp(2n) and superspace symmetry O(m) x Sp(2n) are considered.
Coulembier, Kevin   +2 more
core   +3 more sources

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

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