A Nitrate-Sensing Domain-Containing Chemoreceptor Is Required for Successful Entry and Virulence of<i>Dickeya dadantii</i>3937 in Potato Plants

Gálvez-Roldán, Clara; Cerna-Vargas, Jean Paul; Herva, Jose Juan Rodriguez; Krell, Tino; Santamaría‐Hernando, Saray; López‐Solanilla, Emilia

doi:10.1094/phyto-10-22-0367-r

Cited by 8 publications

(16 citation statements)

References 71 publications

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“…Considering that the ligand preferences differ between Dd15070‐LBD (Gálvez‐Roldán et al, 2022) and PscN‐LBD, we studied the NIT domain of the chemoreceptor ECA_RS02210 from P. atrosepticum SCRI1043. To this end, we used a similar approach and produced the individual domain as purified protein for its microcalorimetric analysis.…”

Section: Resultsmentioning

confidence: 99%

“…For example, maximal response for nitrate were 15‐fold higher than PacA‐mediated responses and 7‐fold higher compared to a strain in which the PacA concentration was increased by overexpressing its gene in trans ( Matilla, Velando, Tajuelo, et al, 2022 ) . The magnitude of nitrate chemotaxis was also superior to that mediated by the other characterised NIT‐containing chemoreceptor, Dd15070 of D. dadantii (Gálvez‐Roldán et al, 2022). The magnitude of nitrate response may indicate a particular physiological relevance.…”

Section: Discussionmentioning

confidence: 97%

“…Among the ligands tested were compounds with a structure very similar to nitrate/nitrite like phosphate, thiophosphate, dithiophosphate, sulphate, thiosulfate or tetrathionate, among others. Furthermore, the analyses of PacN‐LBD and Dd15070 (Gálvez‐Roldán et al, 2022) underline the nitrate/nitrite specificity of NIT domains. However, the failure of both ligands to bind to the NIT domain of P. aeruginosa chemoreceptor PA4520 indicated that not all family members bind these ligands.…”

Section: Discussionmentioning

confidence: 99%

“…The NIT domain of the Dd15070 chemoreceptor from Dickeya dadantii had a preference for nitrate and bound nitrite with lower affinity (Gálvez-Roldán et al, 2022). To assess ligand specificity and affinity of NIT domains, we have produced the NIT domain of the chemoreceptor PSA3335_RS14925 from P. savastanoi pv.…”

Section: Nit Domains Differ In Their Ligand Preferences For Nitrate O...mentioning

confidence: 99%

“…We have shown previously that the NIT domain of Pseudomonas aeruginosa chemoreceptor PA4520 does not bind nitrate/nitrite nor is it involved in mediating nitrate chemotaxis (Martín‐Mora et al, 2019). In contrast, another study showed that the NIT domain of chemoreceptor Dd15070 from Dickeya dadantii bound nitrate with an affinity that was only slightly superior to that of nitrite (Gálvez‐Roldán et al, 2022). NIT domains are found in more than 1% of chemoreceptors (Sanchis‐López et al, 2021), and the 3D structure of an apo‐NIT domain from the transcription anti‐terminator NasR has been reported (Boudes et al, 2012) (Figure 1).…”

Section: Introductionmentioning

confidence: 98%

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Study of NIT domain‐containing chemoreceptors from two global phytopathogens and identification of NIT domains in eukaryotes

Monteagudo‐Cascales

Ortega

Velando

et al. 2023

Molecular Microbiology

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Bacterial 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.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Nit Domains Differ In Their Ligand Preferences For Nitrate O...mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Study of NIT domain‐containing chemoreceptors from two global phytopathogens and identification of NIT domains in eukaryotes

Monteagudo‐Cascales

Ortega

Velando

et al. 2023

Molecular Microbiology

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Bacterial sensor evolved by decreasing complexity

Monteagudo-Cascales,

Gavira,

Xing

et al. 2024

Preprint

Self Cite

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Bacterial receptors feed into multiple signal transduction pathways that regulate a variety of cellular processes including gene expression, second messenger levels and motility. Receptors are typically activated by signal binding to ligand binding domains (LBD). Cache domains are omnipresent LBDs found in bacteria, archaea, and eukaryotes, including humans. They form the predominant family of extracytosolic bacterial LBDs and were identified in all major receptor types. Cache domains are composed of either a single (sCache) or a double (dCache) structural module. The functional relevance of bimodular LBDs remains poorly understood. Here, we identify the PacF chemoreceptor in the phytopathogen Pectobacterium atrosepticum that recognizes formate at the membrane distal module of its dCache domain, triggering chemoattraction. We further demonstrate that a family of formate-specific sCache domains has evolved from a dCache domain, exemplified by PacF, by losing the membrane proximal module. By solving high-resolution structures of two family members in complex with formate, we show that the molecular basis for formate binding at sCache and dCache domains is highly similar, despite their low sequence identity. The apparent loss of the membrane proximal module may be related to the observation that dCache domains bind ligands typically at the membrane distal module, whereas the membrane proximal module is not involved in signal sensing. This work advances our understanding of signal sensing in bacterial receptors and suggests that evolution by reducing complexity may be a common trend shaping their diversity.

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Methanol chemoreceptor MtpA- and flagellin protein FliC-dependent methylotaxis determines the spaciotemporal colonization of PPFM in the phyllosphere

Katayama,

Shiraishi,

Kaji

et al. 2024

Preprint

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Pink-pigmented facultative methylotrophs (PPFMs) capable of growth on methanol are dominant and versatile phyllosphere bacteria that provide positive effects on plant growth through symbiosis. However, the spatiotemporal behavior of PPFMs on plant surfaces and its molecular basis are unknown. Here we show thatMethylobacteriumsp. strain OR01 inoculated onto red perilla seeds colonized across the entire plant surface in the phyllosphere concomitant with the plant growth. FliC flagellin proteins required for motility were necessary for distributed colonization on plant leaves, but not for colonization at the leaf periphery. Methanol-sensing chemoreceptor MtpA-dependent chemotaxis (methylotaxis; chemotaxis toward methanol) facilitated the bacterial movement from the peripheral to the inner part of leaves and further entry into the stomatal cavity, indicating that methanol functions as a volatile messenger attracting PPFMs to particular leaf locations possibly to support with photosynthesis and to afford protection from pathogenic invasion.

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A Nitrate-Sensing Domain-Containing Chemoreceptor Is Required for Successful Entry and Virulence ofDickeya dadantii3937 in Potato Plants

Cited by 8 publications

References 71 publications

Study of NIT domain‐containing chemoreceptors from two global phytopathogens and identification of NIT domains in eukaryotes

Study of NIT domain‐containing chemoreceptors from two global phytopathogens and identification of NIT domains in eukaryotes

Bacterial sensor evolved by decreasing complexity

Methanol chemoreceptor MtpA- and flagellin protein FliC-dependent methylotaxis determines the spaciotemporal colonization of PPFM in the phyllosphere

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