Cited by 550Bacterial Genetics and BiotechnologyBiochemical and Structural CharacterizationGene Regulatory Network Analysis

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Molecular Mechanisms of Two-Component Signal Transduction

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Zschiedrich, Christopher P., Keidel, Victoria, Szurmant, Hendrik·2016·Journal of Molecular Biology

DOI 10.1016/j.jmb.2016.08.003PMC PMC5023499

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Abstract

Two-component systems (TCS) comprising sensor histidine kinases and response regulator proteins are among the most important players in bacterial and archaeal signal transduction and also occur in reduced numbers in some eukaryotic organisms. Given their importance to cellular survival, virulence, and cellular development, these systems are among the most scrutinized bacterial proteins. In the recent years, a flurry of bioinformatics, genetic, biochemical, and structural studies have provided detailed insights into many molecular mechanisms that underlie the detection of signals and the generation of the appropriate response by TCS. Importantly, it has become clear that there is significant diversity in the mechanisms employed by individual systems. This review discusses the current knowledge on common themes and divergences from the paradigm of TCS signaling. An emphasis is on the information gained by a flurry of recent structural and bioinformatics studies.

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YycH and YycI Interact To Regulate the Essential YycFG Two-Component System in Bacillus subtilis
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Convergence of Ser/Thr and Two-component Signaling to Coordinate Expression of the Dormancy Regulon in Mycobacterium tuberculosis*
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The NMR Structure of the Sensory Domain of the Membranous Two-component Fumarate Sensor (Histidine Protein Kinase) DcuS of Escherichia coli
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The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors
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Ligand Binding to the Receptor Domain Regulates the Ratio of Kinase to Phosphatase Activities of the Signaling Domain of the Hybrid Escherichia coli Transmembrane Receptor, Taz1
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Dissecting the Specificity of Protein-Protein Interaction in Bacterial Two-Component Signaling: Orphans and Crosstalks
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An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins
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Conformational coupling in the chemotaxis response regulator CheY
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Two Unique Phosphorylation-Driven Signaling Pathways Crosstalk in Staphylococcus aureus to Modulate the Cell-Wall Charge: Stk1/Stp1 Meets GraSR
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An Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAO
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Dual-Site Phosphorylation of the Control of Virulence Regulator Impacts Group A Streptococcal Global Gene Expression and Pathogenesis
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Structural and Enzymatic Insights into the ATP Binding and Autophosphorylation Mechanism of a Sensor Histidine Kinase
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CheC is related to the family of flagellar switch proteins and acts independently from CheD to control chemotaxis inBacillus subtilis
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Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD
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Phosphorylation of the RitR DNA‐binding domain by a Ser–Thr phosphokinase: implications for global gene regulation in the streptococci
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Structure of an Atypical Orphan Response Regulator Protein Supports a New Phosphorylation-independent Regulatory Mechanism
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Staphylococcal NreB: an O 2 ‐sensing histidine protein kinase with an O 2 ‐labile iron–sulphur cluster of the FNR type
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Interaction fidelity in two-component signaling
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The Mycobacterium tuberculosis serine/threonine kinase PknL phosphorylates Rv2175c: Mass spectrometric profiling of the activation loop phosphorylation sites and their role in the recruitment of Rv2175c
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Allosteric Activation of Bacterial Response Regulators: the Role of the Cognate Histidine Kinase Beyond Phosphorylation
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A PAS Domain Binds Asparagine in the Chemotaxis Receptor McpB in Bacillus subtilis
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A coiled coil switch mediates cold sensing by the thermosensory protein DesK
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Inter-Protein Sequence Co-Evolution Predicts Known Physical Interactions in Bacterial Ribosomes and the Trp Operon
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A PAS Domain with an Oxygen Labile [4Fe-4S] 2+ Cluster in the Oxygen Sensor Kinase NreB of Staphylococcus carnosus
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Assembly of the Transmembrane Domain of E. coli PhoQ Histidine Kinase: Implications for Signal Transduction from Molecular Simulations
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Sensing membrane thickness: Lessons learned from cold stress
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Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ
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A novel mode of regulation of the Staphylococcus aureus Vancomycin-resistance-associated response regulator VraR mediated by Stk1 protein phosphorylation
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Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate
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The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction
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Features of Protein–Protein Interactions in Two‐Component Signaling Deduced from Genomic Libraries
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The Piston Rises Again
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A Response Regulatory Protein with the Site of Phosphorylation Blocked by an Arginine Interaction: Crystal Structure of Spo0F from Bacillus subtilis,
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The Mycobacterium tuberculosis Ser/Thr Kinase Substrate Rv2175c Is a DNA-binding Protein Regulated by Phosphorylation
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Evolving a robust signal transduction pathway from weak cross‐talk
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Asymmetry in the Autophosphorylation of the Two-Component Regulatory System Transmitter Protein Nitrogen Regulator II of Escherichia coli
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Extracytoplasmic PAS-Like Domains Are Common in Signal Transduction Proteins
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Kinetic Characterization of Catalysis by the Chemotaxis Phosphatase CheZ
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Inference of Direct Residue Contacts in Two-Component Signaling
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Receiver Domains Control the Active-State Stoichiometry of Aquifex aeolicus σ54 Activator NtrC4, as Revealed by Electrospray Ionization Mass Spectrometry
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The cytoplasmic kinase domain of PhoR is sufficient for the low phosphate‐inducible expression of Pho regulon genes in Bacillus subtilis
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Structural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniae
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PhoR autokinase activity is controlled by an intermediate in wall teichoic acid metabolism that is sensed by the intracellular PAS domain during the PhoPR ‐mediated phosphate limitation response of B acillus subtilis
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Matching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator Proteins
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Prokaryotic 2-component systems and the OmpR/PhoB superfamily
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Evidence Against the “Y–T Coupling” Mechanism of Activation in the Response Regulator NtrC
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Functional Role for a Conserved Aspartate in the Spo0E Signature Motif Involved in the Dephosphorylation of the Bacillus subtilis Sporulation Regulator Spo0A
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Strain-Specific Regulatory Role of Eukaryote-Like Serine/Threonine Phosphatase in Pneumococcal Adherence
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Co-Evolving Motions at Protein−Protein Interfaces of Two-Component Signaling Systems Identified by Covariance Analysis
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Bacterial sensor kinases using Fe–S cluster binding PAS or GAF domains for O 2 sensing
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The S-Helix Determines the Signal in a Tsr Receptor/Adenylyl Cyclase Reporter
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The VieB auxiliary protein negatively regulates the VieSA signal transduction system in Vibrio cholerae
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Crystal Structures of Two Cyanobacterial Response Regulators in Apo- and Phosphorylated Form Reveal a Novel Dimerization Motif of Phytochrome-Associated Response Regulators
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STAC—A New Domain Associated with Transmembrane Solute Transport and Two-Component Signal Transduction Systems
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Ligand-induced Conformational Changes in the Bacillus subtilis Chemoreceptor McpB Determined by Disulfide Crosslinking in vivo
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Crystal structure of a cyanobacterial phytochrome response regulator
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Computational Modeling of Phosphotransfer Complexes in Two-Component Signaling
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Ligand-Induced Folding of a Two-Component Signaling Receiver Domain
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Snapshots of Conformational Changes Shed Light into the NtrX Receiver Domain Signal Transduction Mechanism
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Characterizing Cross-Talk In Vivo
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Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins
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Authors: Zschiedrich, C. P., Keidel, V., & Szurmant, H.
Affiliations: Scripps Research Institute (US)
Corresponding author: Szurmant, Hendrik
ORCID: Szurmant, Hendrik
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 2016-09
Volume: 428
Issue: 19
Pages: 3752-3775
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1016/j.jmb.2016.08.003
PMC: PMC5023499
OpenAlex: W2498485322
Cited by: 540
References: 189
Citations by year: 2026: 33 · 2025: 54 · 2024: 64 · 2023: 54 · 2022: 63 · 2021: 63 · 2020: 58 · 2019: 69 · 2018: 40 · 2017: 39 · 2016: 2
FWCI: 6.57
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: US National Institute of General Medical Sciences, National Institutes of Health (GM106085)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
Keywords: two-component systems, signal transduction, sensor histidine kinase, response regulator proteins, bacterial signaling, signal detection, protein structure, molecular mechanisms
MeSH terms: Histidine Kinase, Archaea, Bacteria, Gene Expression Regulation, Transcription Factors, Signal Transduction, Eukaryota

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Molecular Mechanisms of Two-Component Signal Transduction

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