ArticleProceedings of the National Academy of Sciences of the United States of America2018
Structure and function of the archaeal response regulator CheY.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 57 citations in OpenAlex.
- Archaeal Cytoskeletal Protein CetZ1 Influences Assembly of the Motility Machinery.Molecular microbiology · 2026Article
- Comparative Molecular Dynamics Study of the Thermal Stability of CheY Proteins from Hyperthermophilic and Mesophilic Organisms.Journal of chemical information and modeling · 2026Article
- Decoding the Chemical Language of Ribosomally Synthesized and Post-Translationally Modified Peptides from the Untapped Archaea Domain.Angewandte Chemie (International ed. in English) · 2025Article
- An atlas of metabolites driving chemotaxis in prokaryotes.Nature communications · 2025Article
- Article
- Spatial Layouts of Low-Entropy Hydration Shells Guide Protein Binding.Global challenges (Hoboken, NJ) · 2023Article
- Genetic determinants of Biofilm formation of Helicobacter pylori using whole-genome sequencing.BMC microbiology · 2023Article
- Comparative Genomic Insights into Chemoreceptor Diversity and Habitat Adaptation of Archaea.Applied and environmental microbiology · 2022Article
- Coarse-grained modeling of the calcium, sodium, magnesium and potassium cations interacting with proteins.Journal of molecular modeling · 2022Article
- The Viral Susceptibility of theViruses · 2022Article
- Structural insights into the mechanism of archaellar rotational switching.Nature communications · 2022Article
- Methods to Analyze Motility in Eury- and Crenarchaea.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Open Issues for Protein Function Assignment inGenes · 2021Article
- The Divergent Key Residues of TwoMicroorganisms · 2021Article
- Growth Phase Dependent Cell Shape ofMicroorganisms · 2021Article
- Cellular and Genomic Properties ofFrontiers in microbiology · 2021Article
- 3D Domain Swapping Dimerization of the Receiver Domain of Cytokinin Receptor CRE1 FromFrontiers in plant science · 2021Article
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Article
- The phosphorylated regulator of chemotaxis is crucial throughout biofilm biogenesis in Shewanella oneidensis.NPJ biofilms and microbiomes · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Motility is a central feature of many microorganisms and provides an efficient strategy to respond to environmental changes. Bacteria and archaea have developed fundamentally different rotary motors enabling their motility, termed flagellum and archaellum, respectively. Bacterial motility along chemical gradients, called chemotaxis, critically relies on the response regulator CheY, which, when phosphorylated, inverses the rotational direction of the flagellum via a switch complex at the base of the motor. The structural difference between archaellum and flagellum and the presence of functional CheY in archaea raises the question of how the CheY protein changed to allow communication with the archaeal motility machinery. Here we show that archaeal CheY shares the overall structure and mechanism of magnesium-dependent phosphorylation with its bacterial counterpart. However, bacterial and archaeal CheY differ in the electrostatic potential of the helix α4. The helix α4 is important in bacteria for interaction with the flagellar switch complex, a structure that is absent in archaea. We demonstrated that phosphorylation-dependent activation, and conserved residues in the archaeal CheY helix α4, are important for interaction with the archaeal-specific adaptor protein CheF. This forms a bridge between the chemotaxis system and the archaeal motility machinery. Conclusively, archaeal CheY proteins conserved the central mechanistic features between bacteria and archaea, but differ in the helix α4 to allow binding to an archaellum-specific interaction partner.
Indexed as
Identifiers
What OpenQuestion holds
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.