English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
 Local TagsRelease HistoryDetailsSummary
  The pH robustness of bacterial sensing

Monteagudo-Cascales, E., Martin-Mora, D., Xu, W., Sourjik, V., Matilla, M. A., Ortega, A., et al. (2022). The pH robustness of bacterial sensing. mBio, 13(5): e0165022. doi:10.1128/mbio.01650-22.

Item is

 

show all hide all

Basic

show hide
Item Permalink: https://hdl.handle.net/21.11116/0000-000B-3108-5 Version Permalink: https://hdl.handle.net/21.11116/0000-000E-7D4E-0
Genre: Journal Article

Files

show Files
hide Files
:
monteagudo-cascales-et-al-2022-the-ph-robustness-of-bacterial-sensing.pdf (Publisher version), 3MB
View   Save
File Permalink:
https://hdl.handle.net/21.11116/0000-000E-7D4F-F
Name:
monteagudo-cascales-et-al-2022-the-ph-robustness-of-bacterial-sensing.pdf
Description:
-
OA-Status:
Gold
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
View
Copyright Date:
-
Copyright Info:
-
License:
https://creativecommons.org/licenses/by/4.0/

Locators

show

Creators

show
hide
 Creators:
Monteagudo-Cascales, E., Author
Martin-Mora, D., Author
Xu, W.1, 2, Author           
Sourjik, V.1, 2, Author                 
Matilla, M. A., Author
Ortega, A., Author
Krell, T., Author
Affiliations:
1Microbial Networks, Department of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266309              
2Center for Synthetic Microbiology (SYNMIKRO), Philipps-Universität Marburg, ou_persistent22              

Content

show
hide
Free keywords: bacterial adaptation pH pH robustness receptors sensing sensor domains signal transduction
 Abstract: Bacteria have evolved many different signal transduction systems to sense and respond to changing environmental conditions. Signal integration is mainly achieved by signal recognition at extracytosolic ligand-binding domains (LBDs) of receptors. Hundreds of different LBDs have been reported, and our understanding of their sensing properties is growing. Receptors must function over a range of environmental pH values, but there is little information available on the robustness of sensing as a function of pH. Here, we have used isothermal titration calorimetry to determine the pH dependence of ligand recognition by nine LBDs that cover all major LBD superfamilies, of periplasmic solute-binding proteins, and cytosolic LBDs. We show that periplasmic LBDs recognize ligands over a very broad pH range, frequently stretching over eight pH units. This wide pH range contrasts with a much narrower pH response range of the cytosolic LBDs analyzed. Many LBDs must be dimeric to bind ligands, and analytical ultracentrifugation studies showed that the LBD of the Tar chemoreceptor forms dimers over the entire pH range tested. The pH dependences of Pseudomonas aeruginosa motility and chemotaxis were bell-shaped and centered at pH 7.0. Evidence for pH robustness of signaling in vivo was obtained by Forster Resonance Energy Transfer (FRET) measurements of the chemotaxis pathway responses in Escherichia coli. Bacteria have evolved several strategies to cope with extreme pH, such as periplasmic chaperones for protein refolding. The intrinsic pH resistance of periplasmic LBDs appears to be another strategy that permits bacteria to survive under adverse conditions. IMPORTANCE Demonstration of the pH robustness of extracytoplasmic sensing reveals a previously undescribed evolutionary mechanism that enables bacteria to monitor environmental changes under changing conditions. This mechanism includes the maintenance of the dimeric state of four-helixbundle ligand-binding domains (LBDs). The construction of biosensors is a rapidly growing field of research, and their use to monitor the progression of the COVID-19 pandemic has impressively demonstrated their usefulness. LBDs represent an enormous reservoir of binding modules that can be used to create novel biosensors. Among ligands recognized by LBDs are neurotransmitters, hormones, and quorum-sensing signals. The demonstration that extracytosolic LBDs bind their signals over a wide range of pH values will facilitate the design of biosensors that function under highly variable conditions of acidity and alkalinity.

Details

show
hide
Language(s): eng - English
 Dates: 2022-06-082022-09-072022-09-26
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: Other: 36154178
DOI: 10.1128/mbio.01650-22
ISSN: 2150-7511 (Electronic)
 Degree: -

Event

show

Legal Case

show

Project information

show hide
Project name : -
Grant ID : PID2020- 112612GB-I00
Funding program : -
Funding organization : Spanish Ministry for Science and Innovation/Agencia Estatal de Investigación, 10.13039/501100011033
Project name : -
Grant ID : PID2019-103972GA-I00
Funding program : -
Funding organization : Spanish Ministry for Science and Innovation/Agencia Estatal de Investigación, 10.13039/501100011033
Project name : -
Grant ID : P18-FR-1621
Funding program : -
Funding organization : Junta de Andalucía
Project name : -
Grant ID : AEI/10.13039/501100011033
Funding program : -
Funding organization : Ministry of Science and Innovation, the State Research Agency
Project name : -
Grant ID : RTI2018–094393-BC21-MCIU/AEI/FEDER, UE
Funding program : -
Funding organization : European Regional Development Fund
Project name : -
Grant ID : 20786/PI/18
Funding program : -
Funding organization : Seneca Foundation CARM
Project name : -
Grant ID : -
Funding program : LOEWE research cluster “Diffusible Signals” (subproject A1)
Funding organization : Hessian Ministry of Higher Education, Research, and the Arts (HMWK)
Project name : -
Grant ID : -
Funding program : Elites scholarship to W. Xu
Funding organization : Peterson Group “Serving Hometown”

Source 1

show
hide
Title: mBio
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, DC : American Society for Microbiology
Pages: - Volume / Issue: 13 (5) Sequence Number: e0165022 Start / End Page: - Identifier: ISSN: 2150-7511
CoNE: https://pure.mpg.de/cone/journals/resource/2150-7511