Molecular Mechanisms of Two-Component Signal Transduction

Two-Component Signal Transduction

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PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light

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Structural identification of a bacterial quorum-sensing signal containing boron

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Identification of direct residue contacts in protein–protein interaction by message passing

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Biological Insights from Structures of Two-Component Proteins

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Specificity in Two-Component Signal Transduction Pathways

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Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

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Robust and accurate prediction of residue–residue interactions across protein interfaces using evolutionary information

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Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domainPreprint

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Two-State Allosteric Behavior in a Single-Domain Signaling Protein

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Cyclic Diguanylate Is a Ubiquitous Signaling Molecule in Bacteria: Insights into Biochemistry of the GGDEF Protein Domain

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The Ubiquitous Protein Domain EAL Is a Cyclic Diguanylate-Specific Phosphodiesterase: Enzymatically Active and Inactive EAL Domains

Schmidt, A. J., Ryjenkov, D. A., & Gomelsky, M. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.14.4774-4781.2005 · Cited by 569 · see citing works

A light-sensing knot revealed by the structure of the chromophore-binding domain of phytochrome

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Recognition of Antimicrobial Peptides by a Bacterial Sensor Kinase

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Structure and Signaling Mechanism of Per-ARNT-Sim Domains

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Cyclic diguanylate (c‐di‐GMP) regulates Vibrio cholerae biofilm formation

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Structural basis of activity and allosteric control of diguanylate cyclase

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Diversity in Chemotaxis Mechanisms among the Bacteria and Archaea

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Rewiring the Specificity of Two-Component Signal Transduction Systems

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Global regulation by the small RNA‐binding protein CsrA and the non‐coding RNA molecule CsrB

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Functional Characterization in Vitro of All Two-component Signal Transduction Systems from Escherichia coli

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The RNA Molecule CsrB Binds to the Global Regulatory Protein CsrA and Antagonizes Its Activity in Escherichia coli

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Two-Component Signal Transduction Pathways Regulating Growth and Cell Cycle Progression in a Bacterium: A System-Level Analysis

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The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling

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Molecular basis of thermosensing: a two‐component signal transduction thermometer in Bacillus subtilis

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The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins

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Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a Ligand

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Multiple histidine kinases regulate entry into stationary phase and sporulation in Bacillus subtilis

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Structural Insight into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction

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PAS: a multifunctional domain family comes to light

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Structure of a biological oxygen sensor: A new mechanism for heme-driven signal transduction

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Design and Signaling Mechanism of Light-Regulated Histidine Kinases

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Structure of the Escherichia coli Response Regulator NarL,

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Structure of the entire cytoplasmic portion of a sensor histidine‐kinase protein

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Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of development in B. subtilis

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Ligand-Induced Asymmetry in Histidine Sensor Kinase Complex Regulates Quorum Sensing

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The EAL Domain Protein VieA Is a Cyclic Diguanylate Phosphodiesterase

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Signal Transduction in Histidine Kinases: Insights from New Structures

Bhate, M., Molnar, K. S., Goulian, M., & DeGrado, W. F. (2015) · Structure · doi:10.1016/j.str.2015.04.002 · Cited by 284 · see citing works

Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor.Preprint

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Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus

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Structural relationships in the OmpR family of winged-helix transcription factors 1 1Edited by M. Gottesman

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The MiST2 database: a comprehensive genomics resource on microbial signal transduction

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Receiver domain structure and function in response regulator proteins

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Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.

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Genomics-aided structure prediction

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Large-scale determination of previously unsolved protein structures using evolutionary information

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Identification of a novel response regulator required for the swarmer-to-stalked-cell transition in Caulobacter crescentus

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Conformational changes induced by phosphorylation of the FixJ receiver domain

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A novel type of conserved DNA-binding domain in the transcriptional regulators of the AlgR/AgrA/LytR family

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Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA + ATPase domainsPreprint

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Phylogenetic analysis of the phytochrome superfamily reveals distinct microbial subfamilies of photoreceptors

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Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family.

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Protein kinases and protein phosphatases in prokaryotes: a genomic perspective

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Signaling Mechanisms of HAMP Domains in Chemoreceptors and Sensor Kinases

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Accurate prediction of protein–protein interactions from sequence alignments using a Bayesian method

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Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F

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Structural plasticity and catalysis regulation of a thermosensor histidine kinase

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Full-Length Structure of a Sensor Histidine Kinase Pinpoints Coaxial Coiled Coils as Signal Transducers and Modulators

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Intramembrane-sensing histidine kinases: a new family of cell envelope stress sensors in Firmicutes bacteria

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Molecular strategies for phosphorylation-mediated regulation of response regulator activity

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A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction

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Mechanistic Insights Revealed by the Crystal Structure of a Histidine Kinase with Signal Transducer and Sensor Domains

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Keeping Signals Straight in Phosphorelay Signal Transduction

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Crystal structure of an activated response regulator bound to its target.

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High-resolution protein complexes from integrating genomic information with molecular simulation

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Physiologically relevant small phosphodonors link metabolism to signal transduction

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Visualizing autophosphorylation in histidine kinases

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Structure of the Staphylococcus aureus AgrA LytTR Domain Bound to DNA Reveals a Beta Fold with an Unusual Mode of Binding

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Evolution of signalling in the sporulation phosphorelay

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Structure of Concatenated HAMP Domains Provides a Mechanism for Signal Transduction

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New Mechanistic Insights from Structural Studies of the Oxygen-Sensing Domain of Bradyrhizobium japonicum FixL,

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The Structure of the Periplasmic Ligand-binding Domain of the Sensor Kinase CitA Reveals the First Extracellular PAS Domain

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Structural Analysis of Ligand Stimulation of the Histidine Kinase NarX

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Autoregulation of antibiotic biosynthesis by binding of the end product to an atypical response regulator

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Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis

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Membrane Thickness Cue for Cold Sensing in a Bacterium

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A Ligand-Induced Switch in the Periplasmic Domain of Sensor Histidine Kinase CitA

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The Structure of a pH-Sensing Mycobacterial Adenylyl Cyclase Holoenzyme

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Structural Characterization of the Predominant Family of Histidine Kinase Sensor Domains

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Sensor complexes regulating two-component signal transduction

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Ser/Thr phosphorylation as a regulatory mechanism in bacteria

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Intermolecular complementation of the kinase activity of CheA

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Three-dimensional crystal structure of the transcription factor PhoB receiver domain 1 1Edited by R. Huber

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Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation

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Cys-Scanning Disulfide Crosslinking and Bayesian Modeling Probe the Transmembrane Signaling Mechanism of the Histidine Kinase, PhoQ

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P2CS: updates of the prokaryotic two-component systems database

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Formation of a Novel Four-Helix Bundle and Molecular Recognition Sites by Dimerization of a Response Regulator Phosphotransferase

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Bacillus subtilis CheC and FliY Are Members of a Novel Class of CheY-P-hydrolyzing Proteins in the Chemotactic Signal Transduction Cascade

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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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Targeting microbial quorum sensing: the next frontier to hinder bacterial driven gastrointestinal infections

Su, Y., & Ding, T. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2252780 · Cited by 42 · see citing works

A molecular overview of the polymyxin-LPS interaction in the context of its mode of action and resistance development

Padhy, I., Dwibedy, S. K., & Mohapatra, S. S. (2024) · Microbiological Research · doi:10.1016/j.micres.2024.127679 · Cited by 40 · see citing works

The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii

Kim, S. Y., Kim, M., Kim, S. I., Son, J. H., Kim, S., Lee, Y. C., Shin, M., Oh, M. H., & Lee, J. C. (2019) · BMC Microbiology · doi:10.1186/s12866-019-1679-0 · Cited by 41 · see citing works

Complete genome sequence of fish-pathogenic Aeromonas hydrophila HX-3 and a comparative analysis: insights into virulence factors and quorum sensing

Jin, L., Chen, Y., Yang, W., Qiao, Z., & Zhang, X. (2020) · Scientific Reports · doi:10.1038/s41598-020-72484-8 · Cited by 41 · see citing works

Essential Two-Component Systems Regulating Cell Envelope Functions: Opportunities for Novel Antibiotic Therapies

Cardona, S. T., Choy, M., & Hogan, A. M. (2017) · The Journal of Membrane Biology · doi:10.1007/s00232-017-9995-5 · Cited by 40 · see citing works

Protein Histidine Methylation

Kwiatkowski, S., & Drożak, J. (2020) · Current Protein and Peptide Science · doi:10.2174/1389203721666200318161330 · Cited by 41 · see citing works

The role of two-component regulatory systems in environmental sensing and virulence inSalmonella

de Pina, L. C., da Silva, F. S. H., Galvão, T. C., Pauer, H., Ferreira, R. B. R., & Antunes, L. C. M. (2021) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2021.1895067 · Cited by 39 · see citing works

Phosphatase activity of the control of virulence sensor kinase CovS is critical for the pathogenesis of group A streptococcus

Horstmann, N., Tran, C. N., Brumlow, C., DebRoy, S., Yao, H., González, G. N., Makthal, N., Kumaraswami, M., & Shelburne, S. A. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007354 · Cited by 39 · see citing works

Hybrid histidine kinase activation by cyclic di-GMP–mediated domain liberation

Dubey, B. N., Agustoni, E., Böhm, R., Kaczmarczyk, A., Mangia, F., von Arx, C., Jenal, U., Hiller, S., Plaza-Menacho, I., & Schirmer, T. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911427117 · Cited by 39 · see citing works

The Molecular Mechanism of Fludioxonil Action Is Different to Osmotic Stress Sensing

Bersching, K., & Jacob, S. (2021) · Journal of Fungi · doi:10.3390/jof7050393 · Cited by 39 · see citing works

Understanding Bacillus response to salt stress: Growth inhibition, enhanced EPS secretion, and molecular adaptation mechanisms

Yin, Z.-Y., Yuan, Y., Zhang, R., Gan, J.-T., Yu, L., Qiu, X.-H., Chen, R., & Wang, Q. (2024) · Process Biochemistry · doi:10.1016/j.procbio.2024.09.023 · Cited by 38 · see citing works

Group B streptococcal infections in pregnancy and early life

Manuel, G., Twentyman, J., Noble, K. N., Eastman, A. J., Aronoff, D. M., Seepersaud, R., Rajagopal, L., & Waldorf, K. M. A. (2024) · Clinical Microbiology Reviews · doi:10.1128/cmr.00154-22 · Cited by 44 · see citing works

Regulation of Virulence by Two-Component Systems in Pathogenic Burkholderia

Schaefers, M. M. (2020) · Infection and Immunity · doi:10.1128/iai.00927-19 · Cited by 38 · see citing works

Transcriptional Regulation of the Multiple Resistance Mechanisms in Salmonella—A Review

Wójcicki, M., Świder, O., Daniluk, K. J., Średnicka, P., Akimowicz, M., Roszko, M. Ł., Sokołowska, B., & Juszczuk‐Kubiak, E. (2021) · Pathogens · doi:10.3390/pathogens10070801 · Cited by 38 · see citing works

Two-Component Systems

Biondi, E. G. (2013) · Springer eBooks · doi:10.1007/978-1-4419-9863-7_744 · Cited by 1 · see citing works

Untangling the Complexity of Two-Component Signal Transduction in Bacteria

Wadach, P., Jakimowicz, D., & Gongerowska-Jac, M. (2025) · Microorganisms · doi:10.3390/microorganisms13092013 · Cited by 14 · see citing works

Bacterial Two-Component Systems: Structures and Signaling Mechanisms

Wang, S. (2012) · InTech eBooks · doi:10.5772/48277 · Cited by 45 · see citing works

Targeting New Functions and Applications of Bacterial Two‐Component Systems

Ji, S., Li, C., Liu, M., Liu, Y., & Jiang, L. (2024) · ChemBioChem · doi:10.1002/cbic.202400392 · Cited by 5 · see citing works

The role of sensory kinase proteins in two-component signal transduction

Álvarez, A. F., & Georgellis, D. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220848 · Cited by 19 · see citing works