ArticlePLoS biology2010
Using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex.
Article in PLoS biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 62 citations in OpenAlex.
- Multiple input-multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis.FEMS microbiology reviews · 2026Review
- Structural and functional insights underlying recognition of histidine phosphotransfer protein in fungal phosphorelay systems.Communications biology · 2024Article
- Azorhizobium caulinodans Chemotaxis Is Controlled by an Unusual Phosphorelay Network.Journal of bacteriology · 2022Article
- Chemical Neural Networks Inside Synthetic Cells? A Proposal for Their Realization and Modeling.Frontiers in bioengineering and biotechnology · 2022Article
- The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins.The Biochemical journal · 2021Review
- Article
- Evolutionary diversification of the RomR protein of the invasive deltaproteobacterium, Bdellovibrio bacteriovorus.Scientific reports · 2019Article
- Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.Scientific reports · 2017Article
- Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action.eLife · 2016Article
- A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Biochemistry · 2016Article
- Phosphoryl Group Flow within the Pseudomonas aeruginosa Pil-Chp Chemosensory System: DIFFERENTIAL FUNCTION OF THE EIGHT PHOSPHOTRANSFERASE AND THREE RECEIVER DOMAINS.The Journal of biological chemistry · 2016Article
- A Social Medium: ASM's 5th Cell-Cell Communication in Bacteria Meeting in Review.Journal of bacteriology · 2015Article
- Article
- Comparative analysis of wolbachia genomes reveals streamlining and divergence of minimalist two-component systems.G3 (Bethesda, Md.) · 2015Article
- Article
- Influence of the AgrC-AgrA complex on the response time of Staphylococcus aureus quorum sensing.Journal of bacteriology · 2014Article
- The functional importance of co-evolving residues in proteins.Cellular and molecular life sciences : CMLS · 2014Review
- Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis.Journal of bacteriology · 2014Article
- Branched signal wiring of an essential bacterial cell-cycle phosphotransfer protein.Structure (London, England : 1993) · 2013Article
- Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling.Structure (London, England : 1993) · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Two-component signal transduction pathways comprising histidine protein kinases (HPKs) and their response regulators (RRs) are widely used to control bacterial responses to environmental challenges. Some bacteria have over 150 different two-component pathways, and the specificity of the phosphotransfer reactions within these systems is tightly controlled to prevent unwanted crosstalk. One of the best understood two-component signalling pathways is the chemotaxis pathway. Here, we present the 1.40 A crystal structure of the histidine-containing phosphotransfer domain of the chemotaxis HPK, CheA(3), in complex with its cognate RR, CheY(6). A methionine finger on CheY(6) that nestles in a hydrophobic pocket in CheA(3) was shown to be important for the interaction and was found to only occur in the cognate RRs of CheA(3), CheY(6), and CheB(2). Site-directed mutagenesis of this methionine in combination with two adjacent residues abolished binding, as shown by surface plasmon resonance studies, and phosphotransfer from CheA(3)-P to CheY(6). Introduction of this methionine and an adjacent alanine residue into a range of noncognate CheYs, dramatically changed their specificity, allowing protein interaction and rapid phosphotransfer from CheA(3)-P. The structure presented here has allowed us to identify specificity determinants for the CheA-CheY interaction and subsequently to successfully reengineer phosphotransfer signalling. In summary, our results provide valuable insight into how cells mediate specificity in one of the most abundant signalling pathways in biology, two-component signal transduction.
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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.