ArticleBMC microbiology2012
The protein interaction network of a taxis signal transduction system in a halophilic archaeon.
Article in BMC microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Archaeal Cytoskeletal Protein CetZ1 Influences Assembly of the Motility Machinery.Molecular microbiology · 2026Article
- Review
- Studying the long-term adaptation ofFrontiers in microbiology · 2025Article
- Comparative Genomic Insights into Chemoreceptor Diversity and Habitat Adaptation of Archaea.Applied and environmental microbiology · 2022Article
- Structural insights into the mechanism of archaellar rotational switching.Nature communications · 2022Article
- Cellular and Genomic Properties ofFrontiers in microbiology · 2021Article
- A comprehensive history of motility and Archaellation in Archaea.FEMS microbes · 2021Article
- Elucidation of the Translation Initiation Factor Interaction Network ofFrontiers in microbiology · 2021Article
- Article
- Insights into gene expression changes under conditions that facilitate horizontal gene transfer (mating) of a model archaeon.Scientific reports · 2020Article
- The switch complex ArlCDE connects the chemotaxis system and the archaellum.Molecular microbiology · 2020Article
- Evolution of the Stator Elements of Rotary Prokaryote Motors.Journal of bacteriology · 2020Review
- Accessory Gvp Proteins Form a Complex During Gas Vesicle Formation of Haloarchaea.Frontiers in microbiology · 2020Article
- Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Article
- Taxis in archaea.Emerging topics in life sciences · 2018Article
- Archaeal cell surface biogenesis.FEMS microbiology reviews · 2018Article
- Structure and function of the archaeal response regulator CheY.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Light-controlled motility in prokaryotes and the problem of directional light perception.FEMS microbiology reviews · 2017Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe taxis signaling system of the extreme halophilic archaeon Halobacterium (Hbt.) salinarum differs in several aspects from its model bacterial counterparts Escherichia coli and Bacillus subtilis. We studied the protein interactions in the Hbt. salinarum taxis signaling system to gain an understanding of its structure, to gain knowledge about its known components and to search for new members.
resultsThe interaction analysis revealed that the core signaling proteins are involved in different protein complexes and our data provide evidence for dynamic interchanges between them. Fifteen of the eighteen taxis receptors (halobacterial transducers, Htrs) can be assigned to four different groups depending on their interactions with the core signaling proteins. Only one of these groups, which contains six of the eight Htrs with known signals, shows the composition expected for signaling complexes (receptor, kinase CheA, adaptor CheW, response regulator CheY). From the two Hbt. salinarum CheW proteins, only CheW1 is engaged in signaling complexes with Htrs and CheA, whereas CheW2 interacts with Htrs but not with CheA. CheY connects the core signaling structure to a subnetwork consisting of the two CheF proteins (which build a link to the flagellar apparatus), CheD (the hub of the subnetwork), two CheC complexes and the receptor methylesterase CheB.
conclusionsBased on our findings, we propose two hypotheses. First, Hbt. salinarum might have the capability to dynamically adjust the impact of certain Htrs or Htr clusters depending on its current needs or environmental conditions. Secondly, we propose a hypothetical feedback loop from the response regulator to Htr methylation made from the CheC proteins, CheD and CheB, which might contribute to adaptation analogous to the CheC/CheD system of B. subtilis.
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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.