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In vivo cross-linking and transmembrane helix dynamics support a bidirectional non-piston model of signaling within E. coli EnvZ

https://doi.org/10.1101/206888

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/1873-3468.12658openalex-snapshot

Crystal structure of the EnvZ periplasmic domain with CHAPS

inferredcites →https://doi.org/10.1002/9781119004813.ch103openalex-snapshot

Modulators of The Bacterial Two‐component Systems Involved in Envelope Stress, Transport, and Virulence

inferredcites →https://doi.org/10.1002/jcc.20291openalex-snapshot

GROMACS: Fast, flexible, and free

inferredcites →https://doi.org/10.1006/bbrc.1996.6007openalex-snapshot

Purification and Characterization of the Periplasmic Domain of EnvZ Osmosensor inEscherichia coli

inferredcites →https://doi.org/10.1006/jmbi.2000.4315openalex-snapshot

Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen

inferredcites →https://doi.org/10.1016/0022-2836(80)90283-1openalex-snapshot

Analysis of gene control signals by DNA fusion and cloning in Escherichia coli

inferredcites →https://doi.org/10.1016/0022-2836(91)90497-topenalex-snapshot

EnvZ controls the concentration of phosphorylated OmpR to mediate osmoregulation of the porin genes

inferredcites →https://doi.org/10.1016/0923-2508(94)90083-3openalex-snapshot

Signal transduction by the EnvZ-OmpR phosphotransfer system in bacteria

inferredcites →https://doi.org/10.1016/j.bbamem.2011.06.018openalex-snapshot

Structural characterization of AS1–membrane interactions from a subset of HAMP domains

inferredcites →https://doi.org/10.1016/j.bbamem.2014.11.017openalex-snapshot

Differential repositioning of the second transmembrane helices from E. coli Tar and EnvZ upon moving the flanking aromatic residues

inferredcites →https://doi.org/10.1016/j.bbamem.2016.05.002openalex-snapshot

Identification of transmembrane helix 1 (TM1) surfaces important for EnvZ dimerisation and signal output

inferredcites →https://doi.org/10.1016/j.bpj.2016.12.027openalex-snapshot

Lipid-Mediated Regulation of Embedded Receptor Kinases via Parallel Allosteric Relays

inferredcites →https://doi.org/10.1016/j.cell.2006.06.058openalex-snapshot

The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling

inferredcites →https://doi.org/10.1016/j.cell.2006.08.024openalex-snapshot

Signaling by Transmembrane Proteins Shifts Gears

inferredcites →https://doi.org/10.1016/j.mib.2010.01.009openalex-snapshot

Two-component signaling circuit structure and properties

inferredcites →https://doi.org/10.1016/j.mib.2011.11.009openalex-snapshot

Histidine kinases and response regulators in networks

inferredcites →https://doi.org/10.1016/j.str.2014.04.019openalex-snapshot

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

inferredcites →https://doi.org/10.1016/j.str.2014.08.011openalex-snapshot

Piston versus Scissors: Chemotaxis Receptors versus Sensor His-Kinase Receptors in Two-Component Signaling Pathways

inferredcites →https://doi.org/10.1016/j.tibs.2007.09.014openalex-snapshot

Bacterial chemoreceptors: high-performance signaling in networked arrays

inferredcites →https://doi.org/10.1016/j.tim.2015.03.003openalex-snapshot

Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update

inferredcites →https://doi.org/10.1016/s0076-6879(07)23002-2openalex-snapshot

Use of Site‐Directed Cysteine and Disulfide Chemistry to Probe Protein Structure and Dynamics: Applications to Soluble and Transmembrane Receptors of Bacterial Chemotaxis

inferredcites →https://doi.org/10.1016/s0968-0004(00)01770-9openalex-snapshot

Transmembrane signaling in bacterial chemoreceptors

inferredcites →https://doi.org/10.1021/acs.biochem.6b00160openalex-snapshot

Structural Analysis of the Ligand-Binding Domain of the Aspartate Receptor Tar from Escherichia coli

inferredcites →https://doi.org/10.1021/bi061259iopenalex-snapshot

Tuning a Bacterial Chemoreceptor with Protein−Membrane Interactions

inferredcites →https://doi.org/10.1021/bi201555xopenalex-snapshot

The Residue Composition of the Aromatic Anchor of the Second Transmembrane Helix Determines the Signaling Properties of the Aspartate/Maltose Chemoreceptor Tar of Escherichia coli

inferredcites →https://doi.org/10.1021/bi4002002openalex-snapshot

Residues at the Cytoplasmic End of Transmembrane Helix 2 Determine the Signal Output of the TarEc Chemoreceptor

inferredcites →https://doi.org/10.1021/bi8013399openalex-snapshot

The Region Preceding the C-Terminal NWETF Pentapeptide Modulates Baseline Activity and Aspartate Inhibition of Escherichia coli Tar

inferredcites →https://doi.org/10.1021/sb500261topenalex-snapshot

Forcing the Issue: Aromatic Tuning Facilitates Stimulus-Independent Modulation of a Two-Component Signaling Circuit

inferredcites →https://doi.org/10.1038/emboj.2012.99openalex-snapshot

The inner membrane histidine kinase EnvZ senses osmolality via helix‐coil transitions in the cytoplasm

inferredcites →https://doi.org/10.1038/nature06387openalex-snapshot

Molecular code for transmembrane-helix recognition by the Sec61 translocon

inferredcites →https://doi.org/10.1038/nmeth.2089openalex-snapshot

NIH Image to ImageJ: 25 years of image analysis

inferredcites →https://doi.org/10.1073/pnas.0234782100openalex-snapshot

Robustness and the cycle of phosphorylation and dephosphorylation in a two-component regulatory system

inferredcites →https://doi.org/10.1073/pnas.0807278105openalex-snapshot

High stimulus unmasks positive feedback in an autoregulated bacterial signaling circuit

inferredcites →https://doi.org/10.1073/pnas.93.6.2545openalex-snapshot

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

inferredcites →https://doi.org/10.1074/jbc.m710592200openalex-snapshot

Crystal Structure of a Functional Dimer of the PhoQ Sensor Domain

inferredcites →https://doi.org/10.1086/503264openalex-snapshot

In Vivo Development of Ertapenem Resistance in a Patient with Pneumonia Caused by Klebsiella pneumoniae with an Extended-Spectrum -Lactamase

inferredcites →https://doi.org/10.1093/jac/46.2.273openalex-snapshot

Relationship between outer membrane alterations and susceptibility to antimicrobial agents in isogenic strains of Klebsiella pneumoniae

inferredcites →https://doi.org/10.1093/jac/dkl302openalex-snapshot

Sources of diversity of carbapenem resistance levels in Klebsiella pneumoniae carrying blaVIM-1

inferredcites →https://doi.org/10.1093/jac/dkv475openalex-snapshot

Combinations of mutations in envZ , ftsI , mrdA , acrB and acrR can cause high-level carbapenem resistance in Escherichia coli

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a021972openalex-snapshot

His-Asp Phosphotransfer Signal Transduction

inferredcites →https://doi.org/10.1099/0022-1317-72-7-1551openalex-snapshot

Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics

inferredcites →https://doi.org/10.1101/sqb.1981.045.01.022openalex-snapshot

Identification of a Sex-factor-affinity Site in E. coli as

inferredcites →https://doi.org/10.1111/j.1365-2958.2008.06426.xopenalex-snapshot

Cross‐talk suppression between the CpxA–CpxR and EnvZ–OmpR two‐component systems in E. coli

inferredcites →https://doi.org/10.1111/j.1365-2958.2009.06728.xopenalex-snapshot

MzrA: a novel modulator of the EnvZ/OmpR two‐component regulon

inferredcites →https://doi.org/10.1111/j.1365-2958.2009.06819.xopenalex-snapshot

Mutational analyses of HAMP helices suggest a dynamic bundle model of input–output signalling in chemoreceptors

inferredcites →https://doi.org/10.1126/science.aah6345openalex-snapshot

Mechanism of transmembrane signaling by sensor histidine kinases

inferredcites →https://doi.org/10.1128/9781555818319openalex-snapshot

Two-Component Signal Transduction

inferredcites →https://doi.org/10.1128/aac.00285-06openalex-snapshot

High-Level Carbapenem Resistance in a Klebsiella pneumoniae Clinical Isolate Is Due to the Combination of bla ACT-1 β-Lactamase Production, Porin OmpK35/36 Insertional Inactivation, and Down-Regulation of the Phosphate Transport Porin PhoE

inferredcites →https://doi.org/10.1128/aac.44.9.2534-2536.2000openalex-snapshot

Activities of Imipenem and Cephalosporins against Clonally Related Strains of Escherichia coli Hyperproducing Chromosomal β-Lactamase and Showing Altered Porin Profiles

inferredcites →https://doi.org/10.1128/aac.48.8.3203-3206.2004openalex-snapshot

Role of β-Lactamases and Porins in Resistance to Ertapenem and Other β-Lactams in Klebsiella pneumoniae

inferredcites →https://doi.org/10.1128/jb.00855-10openalex-snapshot

MzrA-EnvZ Interactions in the Periplasm Influence the EnvZ/OmpR Two-Component Regulon

inferredcites →https://doi.org/10.1128/jb.00953-10openalex-snapshot

Mutational Analysis of the Transmembrane Helix 2-HAMP Domain Connection in the Escherichia coli Aspartate Chemoreceptor Tar

inferredcites →https://doi.org/10.1128/jb.171.6.2949-2955.1989openalex-snapshot

DNA-binding properties of the transcription activator (OmpR) for the upstream sequences of ompF in Escherichia coli are altered by envZ mutations and medium osmolarity

inferredcites →https://doi.org/10.1128/jb.179.11.3729-3735.1997openalex-snapshot

Function of conserved histidine-243 in phosphatase activity of EnvZ, the sensor for porin osmoregulation in Escherichia coli

inferredcites →https://doi.org/10.1128/jb.180.1.171-174.1998openalex-snapshot

Differential Expression of the OmpF and OmpC Porin Proteins in Escherichia coli K-12 Depends upon the Level of Active OmpR

inferredcites →https://doi.org/10.1128/jb.185.7.2354-2361.2003openalex-snapshot

CheZ Phosphatase Localizes to Chemoreceptor Patches via CheA-Short

inferredcites →https://doi.org/10.1128/jb.186.22.7618-7625.2004openalex-snapshot

Continuous Control in Bacterial Regulatory Circuits

inferredcites →https://doi.org/10.1128/jcm.00418-06openalex-snapshot

Characterization of a Large Outbreak by CTX-M-1-Producing Klebsiella pneumoniae and Mechanisms Leading to In Vivo Carbapenem Resistance Development

inferredcites →https://doi.org/10.1128/mmbr.67.4.593-656.2003openalex-snapshot

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

inferredcites →https://doi.org/10.1186/s13036-015-0003-2openalex-snapshot

Employing aromatic tuning to modulate output from two-component signaling circuits

inferredcites →https://doi.org/10.1371/journal.pcbi.1002204openalex-snapshot

Transmembrane Helix Dynamics of Bacterial Chemoreceptors Supports a Piston Model of Signalling

inferredcites →https://doi.org/10.1371/journal.pcbi.1004862openalex-snapshot

Cache Domains That are Homologous to, but Different from PAS Domains Comprise the Largest Superfamily of Extracellular Sensors in Prokaryotes

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1007/978-1-4939-9884-5_1openalex-snapshot

Protein Dynamics in Phosphoryl-Transfer Signaling Mediated by Two-Component Systems

inferred← citeshttps://doi.org/10.1101/2020.08.25.266015openalex-snapshot

Employing scan-SCAM to identify residues that compose transmembrane helix 1 (TM1) of EnvZ

inferred← citeshttps://doi.org/10.3389/fcell.2018.00076openalex-snapshot

Membrane Thickness as a Key Factor Contributing to the Activation of Osmosensors and Essential Ras Signaling Pathways

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