ArticleJournal of bacteriology2009
Properties of HflX, an enigmatic protein from Escherichia coli.
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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- An integrative multi-omics approach points to membrane composition as a key factor in E. coli persistence.PloS one · 2026Article
- The structure-function analysis of Obg-like GTPase proteins along the evolutionary tree from bacteria to humans.Genes to cells : devoted to molecular & cellular mechanisms · 2022Review
- DistinctiveFrontiers in plant science · 2022Article
- Mycobacterial HflX is a ribosome splitting factor that mediates antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Impact of the Stringent Response on TRAFAC GTPases and Prokaryotic Ribosome Assembly.Cells · 2019Review
- Structural modules of the stress-induced protein HflX: an outlook on its evolution and biological role.Current genetics · 2019Review
- HflXr, a homolog of a ribosome-splitting factor, mediates antibiotic resistance.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- HflX protein protectsJournal of biosciences · 2018Article
- The universally conserved GTPase HflX is an RNA helicase that restores heat-damagedThe Journal of cell biology · 2018Article
- Characterization of the autophosphorylation property of HflX, a ribosome-binding GTPase from Escherichia coli.FEBS open bio · 2016Article
- HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions.Nature structural & molecular biology · 2015Article
- Novel MntR-independent mechanism of manganese homeostasis in Escherichia coli by the ribosome-associated protein HflX.Journal of bacteriology · 2014Article
- Identification and characterization of a hitherto unknown nucleotide-binding domain and an intricate interdomain regulation in HflX-a ribosome binding GTPase.Nucleic acids research · 2013Article
- The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011Review
- An HflX-type GTPase from Sulfolobus solfataricus binds to the 50S ribosomal subunit in all nucleotide-bound states.Journal of bacteriology · 2011Article
- Studies on Escherichia coli HflKC suggest the presence of an unidentified λ factor that influences the lysis-lysogeny switch.BMC microbiology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli gene hflX was first identified as part of the hflA operon, mutations in which led to an increased frequency of lysogenization upon infection of the bacterium by the temperate coliphage lambda. Independent mutational studies have also indicated that the HflX protein has a role in transposition. Based on the sequence of its gene, HflX is predicted to be a GTP-binding protein, very likely a GTPase. We report here purification and characterization of the HflX protein. We also specifically examined its suggested functional roles mentioned above. Our results show that HflX is a monomeric protein with a high (30% to 40%) content of helices. It exhibits GTPase as well as ATPase activities, but it has no role in lambda lysogeny or in transposition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.