The compatible solutes ectoine and 5-hydroxyectoine: Catabolism and regulatory mechanisms

To cope with osmotic stress many microorganisms make use of short, osmotically active, organic compounds, the so-called compatible solutes. Examples for especially effective members of this type of molecules are the tetrahydropyrimidines ectoine and 5-hydroxyectoine. Both molecules are produced by a...

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Bibliographic Details
Main Author: Hermann, Lucas
Contributors: Bremer, Erhard (Prof. Dr.) (Thesis advisor)
Format: Doctoral Thesis
Language:English
Published: Philipps-Universität Marburg 2022
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Summary:To cope with osmotic stress many microorganisms make use of short, osmotically active, organic compounds, the so-called compatible solutes. Examples for especially effective members of this type of molecules are the tetrahydropyrimidines ectoine and 5-hydroxyectoine. Both molecules are produced by a large number of microorganisms, not only to fend-off osmotic stress, but also for example low and high temperature challenges. The biosynthetic pathway used by these organisms to synthesize ectoines has already been studied intensively and the enzymes used therein are characterized quite well, both biochemically as well as structurally. However, synthesis of ectoines is only half the story. Inevitably, ectoines are frequently released from the producer cells in different environmental settings. Especially in highly competitive habitats like the upper ocean layers some bacteria specialized on a niche like this. The model organism used in this work is such a species. It is the marine bacterium Ruegeria pomeroyi DSS-3 which belongs to the Roseobacter-clade. Roseobacter species are heterotrophic Proteobacteria which can live in symbiosis with phytoplankton as well as turning against them in a bacterial warfare fashion to scavenge valuable nutrients. Ectoines can be imported by R. pomeroyi DSS-3 in a high-affinity fashion and be used as energy as well as carbon- and nitrogen-sources. To achieve this, both ectoines rings are degraded by the hydrolase EutD and deacetylated by the deacetylase EutE. The first hydrolysis products α-ADABA (from ectoine) and hydroxy-α-ADABA (from hydroxyectoine) are deacetylated to DABA and hydroxy-DABA which are in additional biochemical reactions transformed to aspartate to fuel the cell’s central metabolism. The role and functioning of the EutDE enzymes which work in a concerted fashion are a central aspect of this work. Both enzymes could be biochemically and structurally characterized, and the architecture of the metabolic pathway could be illuminated. α-ADABA and hydroxy-α-ADABA are not only central to ectoine catabolism, but also to the regulatory mechanisms associated with it. Both molecules serve as inducers of the central regulatory protein of this pathway, the MocR-/GabR-type regulator protein EnuR. In the framework of this dissertation molecular details could be clarified which enable the EnuR repressor molecule to sense both molecules with high affinity to subsequently derepress the genes for the import and catabolism of ectoines.
Physical Description:302 Pages
DOI:10.17192/z2022.0217