2023
Water potential governs the effector specificity of the transcriptional regulator XylR of Pseudomonas putida
DVOŘÁK, Pavel; Teca Calcagno GALVÃO; Katharina PFLÜGER-GRAU; Alice M. BANKS; Víctor DE LORENZO et. al.Základní údaje
Originální název
Water potential governs the effector specificity of the transcriptional regulator XylR of Pseudomonas putida
Autoři
DVOŘÁK, Pavel (203 Česká republika, domácí); Teca Calcagno GALVÃO; Katharina PFLÜGER-GRAU; Alice M. BANKS; Víctor DE LORENZO (garant) a Jose I. JIMÉNEZ
Vydání
Environmental Microbiology, Wiley, 2023, 1462-2912
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10606 Microbiology
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 4.300
Kód RIV
RIV/00216224:14310/23:00134057
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000924226000001
EID Scopus
2-s2.0-85147337278
Klíčová slova anglicky
Pseudomonas putida; bacteria; genetic engineering; protein-structure; range; activation; sequence
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 21. 6. 2023 15:53, Mgr. Marie Novosadová Šípková, DiS.
Anotace
V originále
The biodegradative capacity of bacteria in their natural habitats is affected by water availability. In this work, we have examined the activity and effector specificity of the transcriptional regulator XylR of the TOL plasmid pWW0 of Pseudomonas putida mt-2 for biodegradation of m-xylene when external water potential was manipulated with polyethylene glycol PEG8000. By using non-disruptive luxCDEAB reporter technology, we noticed that the promoter activated by XylR (Pu) restricted its activity and the regulator became more effector-specific towards head TOL substrates when cells were grown under water subsaturation. Such a tight specificity brought about by water limitation was relaxed when intracellular osmotic stress was counteracted by the external addition of the compatible solute glycine betaine. With these facts in hand, XylR variants isolated earlier as effector-specificity responders to the non-substrate 1,2,4-trichlorobenzene under high matric stress were re-examined and found to be unaffected by water potential in vivo. All these phenomena could be ultimately explained as the result of water potential-dependent conformational changes in the A domain of XylR and its effector-binding pocket, as suggested by AlphaFold prediction of protein structures. The consequences of this scenario for the evolution of specificities in regulators and the emergence of catabolic pathways are discussed.
Návaznosti
GA22-10845S, projekt VaV |
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