Hfq proximity and orientation controls RNA annealing [PDF]
Regulation of bacterial gene networks by small non-coding RNAs (sRNAs) requires base pairing with messenger RNA (mRNA) targets, which is facilitated by Hfq protein. Hfq is recruited to sRNAs and mRNAs through U-rich- and A-rich-binding sites, respectively, but their distance from the sRNA-mRNA complementary region varies widely among different genes ...
Panja, Subrata, Woodson, Sarah A.
openaire +2 more sources
E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain [PDF]
The RNA-binding protein Hfq has been studied extensively for its function as a modulator of gene expression at the post-transcriptional level. While most Hfq studies have focused on the protein's interaction with sRNAs and mRNAs, Hfq binding to DNA has been observed but is less explored.
Taylor B, Updegrove +4 more
openaire +2 more sources
The Pseudomonas aeruginosa CrcZ RNA interferes with Hfq-mediated riboregulation.
The RNA chaperone Hfq regulates virulence and metabolism in the opportunistic pathogen Pseudomonas aeruginosa. During carbon catabolite repression (CCR) Hfq together with the catabolite repression control protein Crc can act as a translational repressor ...
Elisabeth Sonnleitner +2 more
doaj +1 more source
The Pleiotropic Phenotypes Caused by an hfq Null Mutation in Vibrio harveyi
Hfq is a global regulator and can be involved in multiple cellular processes by assisting small regulatory RNAs (sRNAs) to target mRNAs. To gain insight into the virulence regulation of Hfq in Vibrio harveyi, the hfq null mutant, ∆hfq, was constructed in
Yiqin Deng +5 more
doaj +1 more source
Identification of small RNAs abundant in Burkholderia cenocepacia biofilms reveal putative regulators with a potential role in carbon and iron metabolism [PDF]
Small RNAs play a regulatory role in many central metabolic processes of bacteria, as well as in developmental processes such as biofilm formation. Small RNAs of Burkholderia cenocepacia, an opportunistic pathogenic beta-proteobacterium, are to date not ...
Coenye, Tom +2 more
core +3 more sources
The hyperfine structure of highly charged $^{238}_{92}$U ions with rotationally excited nuclei [PDF]
The hyperfine structure (hfs) of electron levels of $^{238}_{92}$U ions with the nucleus excited in the low-lying rotational $2^+$ state with an energy $E_{2^+} = 44.91$ keV is investigated.
Labzowsky, L. N. +4 more
core +2 more sources
Hfq affects mRNA levels independently of degradation [PDF]
Abstract Background The bacterial Lsm protein, Hfq, is an RNA chaperone involved in many reactions related to RNA metabolism, such as replication and stability, control of small RNA activity and polyadenylation. Despite this wide spectrum of known functions, the global role of Hfq is almost certainly undervalued; its ...
Le Derout, Jacques +3 more
openaire +3 more sources
Unnatural Amino Acid and Emerging Chemistry Approaches to Map RNA–Protein Interactions
This review highlights emerging chemistries for mapping RNA–protein interactions, including genetically encoded unnatural amino acids, novel photocrosslinkers, and non‐photoactivatable crosslinking systems. We compare their mechanisms, reactivity and applications, outlining how these next‐generation tools enable higher‐resolution, site‐specific ...
Eryn Lundrigan +3 more
wiley +2 more sources
Hfq mutation confers increased cephalosporin resistance in Klebsiella pneumoniae [PDF]
Klebsiella pneumoniae (K. pneumoniae), is an opportunistic pathogen raising significant public health concerns owing to its multi-drug resistance. Hfq, one of the main RNA-binding proteins, is a key post-transcriptional regulator.
Li Xinran +7 more
doaj +1 more source
The Irr and RirA proteins participate in a complex regulatory circuit and act in concert to modulate bacterioferritin expression in Ensifer meliloti 1021 [PDF]
In this work we found that the bfr gene of the rhizobial species Ensifer meliloti, encoding a bacterioferritin iron storage protein, is involved in iron homeostasis and the oxidative stress response. This gene is located downstream of and overlapping the
Amarelle, Vanesa +4 more
core +1 more source

