Results 221 to 230 of about 11,380 (233)

Function and mechanism of action of the small regulatory RNA ArcZ in Enterobacterales. [PDF]

RNA
Dubois Q, Brual T, Oriol C, Mandin P, Condemine G, Gueguen E.   +5 more
europepmc   +1 more source

Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation

Luisi B, Roske J, Paris G, Goyal A, Rodnina M, Zenkin N, Bandyra K.   +6 more
europepmc   +1 more source

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The role of Hfq in bacterial pathogens

Current Opinion in Microbiology, 2010
The ubiquitous RNA-binding protein, Hfq, has been shown to be required for the fitness and virulence of an increasing number of bacterial pathogens. Mutants lacking Hfq are often sensitive to host defense mechanisms and highly attenuated in animal models, albeit there is considerable variation in both severity and extent of phenotypes. RNomics and deep
Jörg Vogel, Yanjie Chao
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Supramolecular organization of Hfq-like proteins [PDF]

Biochemistry (Moscow), 2015
Bacterial Hfq proteins are structural homologs of archaeal and eukaryotic Sm/Lsm proteins, which are characterized by a 5-stranded β-sheet and an N-terminal α-helix. Previously, it was shown that archaeal Lsm proteins (SmAP) could produce long fibrils spontaneously, in contrast to the Hfq from Escherichia coli that could form similar fibrils only after
Alexei S. Kazakov, N. V. Lekontseva, Victoriia Murina, Alexey D. Nikulin, Olga M. Selivanova, E. Yu. Nikonova, Svetlana Tishchenko, Alisa Mikhaylina   +7 more
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Structure ofPseudomonas aeruginosaHfq protein

Acta Crystallographica Section D Biological Crystallography, 2005
The structure of the Hfq protein from Pseudomonas aeruginosa was determined using two different ionic conditions. In both cases the molecules formed identical hexameric rings, but some variations in the crystal packing were revealed. Hfq belongs to the family of Sm/LSm proteins, the members of which can form hexameric as well as heptameric rings ...
Anna Perederina, Isabella Moll, Maria Garber, Udo Blaesi, Galina Kachalova, Shigeyuki Yokoyama, Dmitry G. Vassylyev, Stanislav Nikonov, Ioulia M. Vassilieva, Elena Stolboushkina, Alexey D. Nikulin   +10 more
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Hfq structure, function and ligand binding

Current Opinion in Microbiology, 2007
Recent studies on Hfq have provided a deeper understanding of the multiple functions of this pleiotropic post-transcriptional regulator. Insights into the mechanism of Hfq action have come from a variety of approaches. A key finding was the characterization of two RNA binding sites: the Proximal Site, which binds sRNA and mRNA; and the Distal Site ...
Richard G. Brennan, Todd M. Link
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Lack of interchangeability of Hfq-like proteins

Biochimie, 2012
Hfq is an RNA-binding protein that participates in the regulatory activity of small non-coding RNAs (sRNAs) in many species of bacteria. Hfq protein was first crystallized from Staphylococcus aureus and this crystal structure constitutes a hallmark for bacterial Sm-like proteins. Paradoxically, however, the functional relevance/role of S.
Nara Figueroa-Bossi, Lionello Bossi, Qi Yang, Tatiana Rochat, Philippe Bouloc   +4 more
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Bacterial Small Regulatory RNAs and Hfq Protein

Biochemistry (Moscow), 2015
Small regulatory RNA (sRNA) is a unique noncoding RNA involved in regulation of gene expression in both eukaryotic and bacterial cells. This short review discusses examples of positive and negative translation regulation by sRNAs in bacteria and participation of Hfq in these processes. The importance of structure investigation of nucleotide-protein and
Victoriia Murina, Alexey D. Nikulin
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RNA Chaperones Step Out of Hfq’s Shadow

Trends in Microbiology, 2017
The stability and function of regulatory small RNAs (sRNAs) often require a specialized RNA-binding protein called an RNA chaperone. Recent findings show that proteins containing a ProQ/FinO domain constitute a new class of RNA chaperones that could play key roles in post-transcriptional gene regulation throughout bacterial species.
Attaiech, Laetitia, Glover, J. N. Mark, Charpentier, Xavier   +2 more
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Ironing out Hfq regulation

Nature Reviews Microbiology, 2012
The stringent response regulator RelA promotes multimerization of Hfq and increases its affinity for target small RNAs.
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