Detailed Information on Publication Record
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.Basic information
Original name
Water potential governs the effector specificity of the transcriptional regulator XylR of Pseudomonas putida
Authors
DVOŘÁK, Pavel (203 Czech Republic, belonging to the institution), Teca Calcagno GALVÃO, Katharina PFLÜGER-GRAU, Alice M. BANKS, Víctor DE LORENZO (guarantor) and Jose I. JIMÉNEZ
Edition
Environmental Microbiology, Wiley, 2023, 1462-2912
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10606 Microbiology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 5.100 in 2022
RIV identification code
RIV/00216224:14310/23:00134057
Organization unit
Faculty of Science
UT WoS
000924226000001
Keywords in English
Pseudomonas putida; bacteria; genetic engineering; protein-structure; range; activation; sequence
Tags
Tags
International impact, Reviewed
Změněno: 21/6/2023 15:53, Mgr. Marie Šípková, DiS.
Abstract
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.
Links
GA22-10845S, research and development project |
|