ArticleJournal of bacteriology2009
The Acinetobacter baylyi Hfq gene encodes a large protein with an unusual C terminus.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Development of two compatible plasmids to assess sRNA-mediated post-transcriptional regulation inMicrobiology (Reading, England) · 2025Article
- Global analysis of the RNA-RNA interactome in Acinetobacter baumannii AB5075 uncovers a small regulatory RNA repressing the virulence-related outer membrane protein CarO.Nucleic acids research · 2024Article
- Identification of Hfq-binding RNAs in Caulobacter crescentus.RNA biology · 2019Article
- The Mechanisms of Disease Caused byFrontiers in microbiology · 2019Review
- The primary transcriptome, small RNAs and regulation of antimicrobial resistance in Acinetobacter baumannii ATCC 17978.Nucleic acids research · 2018Article
- The unusual glycine-rich C terminus of theThe Journal of biological chemistry · 2018Article
- Article
- A Negative Regulator of Cellulose Biosynthesis,Frontiers in microbiology · 2017Article
- Functional Characterization ofFrontiers in microbiology · 2017Article
- Review
- C-terminal domain of the RNA chaperone Hfq drives sRNA competition and release of target RNA.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Hfq plays important roles in virulence and stress adaptation in Cronobacter sakazakii ATCC 29544.Infection and immunity · 2015Article
- Association of RNAs with Bacillus subtilis Hfq.PloS one · 2013Article
- Hfq and its constellation of RNA.Nature reviews. Microbiology · 2011Review
- The RNA chaperone Hfq is important for growth and stress tolerance in Francisella novicida.PloS one · 2011Article
- The second RNA chaperone, Hfq2, is also required for survival under stress and full virulence of Burkholderia cenocepacia J2315.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In gammaproteobacteria the Hfq protein shows a great variation in size, especially in its C-terminal part. Extremely large Hfq proteins consisting of almost 200 amino acid residues and more are found within the gammaproteobacterial family Moraxellaceae. The difference in size compared to other Hfq proteins is due to a glycine-rich domain near the C-terminal end of the protein. Acinetobacter baylyi, a nonpathogenic soil bacterium and member of the Moraxellaceae encodes a large 174-amino-acid Hfq homologue containing the unique and repetitive amino acid pattern GGGFGGQ within the glycine-rich domain. Despite the presence of the C-terminal extension, A. baylyi Hfq complemented an Escherichia coli hfq mutant in vivo. By using polyclonal anti-Hfq antibodies, we detected the large A. baylyi Hfq that corresponds to its annotated size indicating the expression and stability of the full protein. Deletion of the complete A. baylyi hfq open reading frame resulted in severe reduction of growth. In addition, a deletion or overexpression of Hfq was accompanied by the loss of cell chain assembly. The glycine-rich domain was not responsible for growth and cell phenotypes. hfq gene localization in A. baylyi is strictly conserved within the mutL-miaA-hfq operon, and we show that hfq expression starts within the preceding miaA gene or further upstream.
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