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 …

Hfq is a ubiquitous, Sm‐like RNA binding protein found in most bacteria and some archaea.
Hfq binds small regulatory RNAs (sRNAs), facilitates base pairing between sRNAs and their …

In many bacteria, iron homeostasis is controlled primarily by the ferric uptake regulator (Fur),
a transcriptional repressor. However, some genes, including those involved in iron storage …

The conserved RNA‐binding protein Hfq, originally discovered in Escherichia coli as a host
factor for Qβ replicase, has emerged as a pleiotropic regulator that modulates the stability or …

The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for
the Qβ phage RNA replication. During the last decade, it was shown to be involved in many …

The Sm-like protein Hfq has been implicated in the regulation of σS-dependent and σS-
independent genes in E. coli and in the regulation of virulence factors in both, Yersinia …

Hfq, a bacterial RNA‐binding protein, was recently shown to contain the Sm1 motif, a
characteristic of Sm and LSm proteins that function in RNA processing events in archaea …

Most of the sequenced bacterial genomes contain a gene encoding a protein known as Hfq
that resembles the eukaryotic RNA-binding proteins of the LSm family. It was originally …

The bacterial Sm protein and RNA chaperone Hfq stabilizes small noncoding RNAs
(sRNAs) and facilitates their annealing to mRNA targets involved in stress tolerance and …

Previous work has demonstrated that iron-dependent variations in the steady-state
concentration and translatability of sodB mRNA are modulated by the small regulatory RNA …