Publication:
Study of NIT domain-containing chemoreceptors from two global phytopathogens and identification of NIT domains in eukaryotes

Simple item page
dc.contributor.authorOrtega Retuerta, Álvaro
dc.contributor.authorMonteagudo-Cascales, Elizabet
dc.contributor.authorVelando, Félix
dc.contributor.authorMorel, Bertrand
dc.contributor.authorMatilla, Miguel A.
dc.contributor.authorKrel, Tino
dc.contributor.departmentBioquímica y Biología Molecular B e Inmunología
dc.contributor.otherFacultad de Química
dc.date.accessioned2026-02-20T10:58:03Z
dc.date.available2026-02-20T10:58:03Z
dc.date.copyright© 2023 The Authors
dc.date.issued2023-04-25
dc.description.abstractBacterial signal transduction systems are typically activated by the binding of signal molecules to receptor ligand binding domains (LBDs), such as the NIT LBD. We report here the identification of the NIT domain in more than 15,000 receptors that were present in 30 bacterial phyla, but also in 19 eukaryotic phyla, expanding its known phylogenetic distribution. The NIT domain formed part of seven receptor families that either control transcription, mediate chemotaxis or regulate second messenger levels. We have produced the NIT domains from chemoreceptors of the bacterial phytopathogens Pectobacterium atrosepticum (PacN) and Pseudomonas savastanoi (PscN) as individual purified proteins. High-throughput ligand screening using compound libraries revealed a specificity for nitrate and nitrite binding. Isothermal titration calorimetry experiments showed that PacN-LBD bound preferentially nitrate ( K D = 1.9 μM), whereas the affinity of PscN-LBD for nitrite ( K D = 2.1 μM) was 22 times higher than that for nitrate. Analytical ultracentrifugation experiments indicated that PscN-LBD is monomeric in the presence and absence of ligands. The R182A mutant of PscN did not bind nitrate or nitrite. This residue is not conserved in the NIT domain of the Pseudomonas aeruginosa chemoreceptor PA4520, which may be related to its failure to bind nitrate/nitrite. The magnitude of P. atrosepticum chemotaxis towards nitrate was significantly greater than that of nitrite and pacN deletion almost abolished responses to both compounds. This study highlights the important role of nitrate and nitrite as signal molecules in life and advances our knowledge on the NIT domain as universal nitrate/nitrite sensor module.
dc.formatapplication/pdf
dc.format.extent13
dc.identifier.citationMolecular Microbiology, 119, 739–751
dc.identifier.doihttps://doi.org/10.1111/mmi.15069
dc.identifier.eissn1365-2958
dc.identifier.issn0950-382X
dc.identifier.urihttp://hdl.handle.net/10201/209181
dc.languageeng
dc.publisherWiley
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/doi/10.1111/mmi.15069
dc.rightsAttribution-NonCommercial 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/*
dc.subject.odsObjetivo 12: Producción y consumo sostenibles
dc.titleStudy of NIT domain-containing chemoreceptors from two global phytopathogens and identification of NIT domains in eukaryotes
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublicationes
relation.isAuthorOfPublication12370e68-6859-4506-8ff9-cd5c6b488194
relation.isAuthorOfPublication.latestForDiscovery12370e68-6859-4506-8ff9-cd5c6b488194
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
Molecular Microbiology - 2023 - Monteagudo‐Cascales - Study of NIT domain‐containing chemoreceptors from two global.pdf
Size:
4.22 MB
Format:
Adobe Portable Document Format
Description:
Download
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
1.37 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Artículos