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Mol Microbiol ; 115(4): 672-683, 2021 04.
Artigo em Inglês | MEDLINE | ID: mdl-33098326

RESUMO

Halomonas titanicae KHS3, isolated from a hydrocarbon-contaminated sea harbor in Argentina, is able to grow on aromatic hydrocarbons and displays chemotaxis toward those compounds. This behavior might contribute to the efficiency of its degradation capacity. Using high throughput screening, we identified two chemoreceptors (Htc1 and Htc2) that bind benzoate derivatives and other organic acids. Whereas Htc1 has a high affinity for benzoate (Kd 112 µM) and 2-hydroxybenzoate (Kd 83 µM), Htc2 binds 2-hydroxybenzoate with low affinity (Kd 3.25 mM), and also C3/C4 dicarboxylates. Both chemoreceptors are able to trigger a chemotactic response of E. coli cells to the specific ligands. A H. titanicae htc1 mutant has reduced chemotaxis toward benzoate, and is complemented upon expression of the corresponding receptor. Both chemoreceptors have a Cache-type sensor domain, double (Htc1) or single (Htc2), and their ability to bind aromatic compounds is reported here for the first time.


Assuntos
Proteínas de Bactérias/metabolismo , Benzoatos/metabolismo , Ácidos Carboxílicos/metabolismo , Células Quimiorreceptoras/metabolismo , Quimiotaxia , Halomonas/metabolismo , Hidroxibenzoatos/metabolismo , Proteínas de Bactérias/química , Proteínas de Bactérias/genética , Fatores Quimiotáticos/metabolismo , DNA Bacteriano , Transportadores de Ácidos Dicarboxílicos/química , Transportadores de Ácidos Dicarboxílicos/metabolismo , Escherichia coli/metabolismo , Halomonas/química , Halomonas/genética , Ensaios de Triagem em Larga Escala , Ligantes , Ligação Proteica , Domínios Proteicos , Água do Mar/microbiologia
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