Superoxide dismutase A (SodA) is a c-di-GMP effector protein governing oxidative stress tolerance in Stenotrophomonas maltophilia
Copyright © 2023 Elsevier GmbH. All rights reserved..
C-di-GMP is a bacterial second messenger implicated in the regulation of many key functions including antibiotic tolerance and biofilm formation. Our understanding of how c-di-GMP exerts its action via receptors to modulate different biological functions is still limited. Here we used a c-di-GMP affinity pull-down assay coupled to LC-MS/MS to identify c-di-GMP-binding proteins in the opportunistic pathogen Stenotrophomonas maltophilia. This analysis identified Smlt3238 (SodA), a protein of the superoxide dismutase family, as a c-di-GMP-binding protein. Microscale thermophoresis showed that purified SodA protein bound c-di-GMP with an estimated dissociation constant (Kd) value of 141.5 μM. Using various in vivo and in vitro experiments, we demonstrated that c-di-GMP modulates the enzyme activity of SodA directly. Circular dichroism experiments revealed that SodA protein gradually altered its basic structure with increasing levels of c-di-GMP. Phenotypic experiments conducted in the presence of a range of intracellular c-di-GMP levels showed that SodA function is modulated by c-di-GMP. The findings thus identify a novel c-di-GMP binding protein that governs oxidative stress tolerance in S. maltophilia.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 2023 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:278 |
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| Enthalten in: |
Microbiological research - 278(2023) vom: 01. Jan., Seite 127535 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sun, Xiao-Yu [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 28.11.2023 Date Revised 28.11.2023 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.micres.2023.127535 |
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| 520 | |a C-di-GMP is a bacterial second messenger implicated in the regulation of many key functions including antibiotic tolerance and biofilm formation. Our understanding of how c-di-GMP exerts its action via receptors to modulate different biological functions is still limited. Here we used a c-di-GMP affinity pull-down assay coupled to LC-MS/MS to identify c-di-GMP-binding proteins in the opportunistic pathogen Stenotrophomonas maltophilia. This analysis identified Smlt3238 (SodA), a protein of the superoxide dismutase family, as a c-di-GMP-binding protein. Microscale thermophoresis showed that purified SodA protein bound c-di-GMP with an estimated dissociation constant (Kd) value of 141.5 μM. Using various in vivo and in vitro experiments, we demonstrated that c-di-GMP modulates the enzyme activity of SodA directly. Circular dichroism experiments revealed that SodA protein gradually altered its basic structure with increasing levels of c-di-GMP. Phenotypic experiments conducted in the presence of a range of intracellular c-di-GMP levels showed that SodA function is modulated by c-di-GMP. The findings thus identify a novel c-di-GMP binding protein that governs oxidative stress tolerance in S. maltophilia | ||
| 650 | 4 | |a Journal Article | |
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| 700 | 1 | |a Siu, Kam-Leung |e verfasserin |4 aut | |
| 700 | 1 | |a Cheng, Ying-Ying |e verfasserin |4 aut | |
| 700 | 1 | |a Ye, Liumei |e verfasserin |4 aut | |
| 700 | 1 | |a Qin, Jiaoxia |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Ke |e verfasserin |4 aut | |
| 700 | 1 | |a Qu, Jiu-Xin |e verfasserin |4 aut | |
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| 700 | 1 | |a Wang, Fuxiang |e verfasserin |4 aut | |
| 700 | 1 | |a Jin, Dong-Yan |e verfasserin |4 aut | |
| 700 | 1 | |a Yang, Liang |e verfasserin |4 aut | |
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