Functioning of the mercury resistance operon at extremely high Hg(II) loads in a chemostat: a proteome analysis.

2.50
Hdl Handle:
http://hdl.handle.net/10033/18632
Title:
Functioning of the mercury resistance operon at extremely high Hg(II) loads in a chemostat: a proteome analysis.
Authors:
Leonhäuser, Johannes; Wang, Wei; Deckwer, Wolf-Dieter; Wagner-Döbler, Irene
Abstract:
The transformation of extremely high concentrations of ionic mercury (up to 500 mg L(-1)) was investigated in a chemostat for two mercury-resistant Pseudomonas putida strains, the sediment isolate Spi3 carrying a regulated mercury resistance (mer) operon, and the genetically engineered strain KT2442Colon, two colonsmer73 expressing the mer operon constitutively. Both strains reduced Hg(II) with an efficiency of 99.9% even at the maximum load, but the concentration of particle bound mercury in the chemostat increased strongly. A proteome analysis using two-dimensional gel electrophoresis and mass spectrometry (2-DE/MS) showed constant expression of the MerA and MerB proteins in KT2442Colon, two colonsmer73 as expected, while in Spi3 expression of both proteins was strongly dependent on the Hg(II) concentration. The total cellular proteome of the two strains showed very little changes at high Hg(II) load. However, certain cellular responses of the two strains were identified, especially in membrane-related transport proteins. In Spi3, an up to 45-fold strong induction of a cation efflux transporter was observed, accompanied by a drastic downregulation (106-fold) of an outer membrane porin. In such a way, the cell complemented the highly specific mercury resistance mechanism with a general detoxification response. No indication of a higher demand on energy metabolism could be found for both strains.
Affiliation:
Technical University Braunschweig/HZI-Helmholtz Center for Infection Research, Biochemical Engineering, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.
Citation:
Functioning of the mercury resistance operon at extremely high Hg(II) loads in a chemostat: a proteome analysis. 2007, 132 (4):469-80 J. Biotechnol.
Journal:
Journal of biotechnology
Issue Date:
1-Dec-2007
URI:
http://hdl.handle.net/10033/18632
DOI:
10.1016/j.jbiotec.2007.08.018
PubMed ID:
17904239
Type:
Article
Language:
en
ISSN:
0168-1656
Appears in Collections:
collections of the research group microbial communication (KOM)

Full metadata record

DC FieldValue Language
dc.contributor.authorLeonhäuser, Johannes-
dc.contributor.authorWang, Wei-
dc.contributor.authorDeckwer, Wolf-Dieter-
dc.contributor.authorWagner-Döbler, Irene-
dc.date.accessioned2008-02-19T09:51:39Z-
dc.date.available2008-02-19T09:51:39Z-
dc.date.issued2007-12-01-
dc.identifier.citationFunctioning of the mercury resistance operon at extremely high Hg(II) loads in a chemostat: a proteome analysis. 2007, 132 (4):469-80 J. Biotechnol.en
dc.identifier.issn0168-1656-
dc.identifier.pmid17904239-
dc.identifier.doi10.1016/j.jbiotec.2007.08.018-
dc.identifier.urihttp://hdl.handle.net/10033/18632-
dc.description.abstractThe transformation of extremely high concentrations of ionic mercury (up to 500 mg L(-1)) was investigated in a chemostat for two mercury-resistant Pseudomonas putida strains, the sediment isolate Spi3 carrying a regulated mercury resistance (mer) operon, and the genetically engineered strain KT2442Colon, two colonsmer73 expressing the mer operon constitutively. Both strains reduced Hg(II) with an efficiency of 99.9% even at the maximum load, but the concentration of particle bound mercury in the chemostat increased strongly. A proteome analysis using two-dimensional gel electrophoresis and mass spectrometry (2-DE/MS) showed constant expression of the MerA and MerB proteins in KT2442Colon, two colonsmer73 as expected, while in Spi3 expression of both proteins was strongly dependent on the Hg(II) concentration. The total cellular proteome of the two strains showed very little changes at high Hg(II) load. However, certain cellular responses of the two strains were identified, especially in membrane-related transport proteins. In Spi3, an up to 45-fold strong induction of a cation efflux transporter was observed, accompanied by a drastic downregulation (106-fold) of an outer membrane porin. In such a way, the cell complemented the highly specific mercury resistance mechanism with a general detoxification response. No indication of a higher demand on energy metabolism could be found for both strains.en
dc.language.isoenen
dc.subject.meshBiotransformationen
dc.subject.meshGene Expression Regulation, Bacterialen
dc.subject.meshGenetic Engineeringen
dc.subject.meshMercuryen
dc.subject.meshOperonen
dc.subject.meshOxidoreductasesen
dc.subject.meshProteomeen
dc.subject.meshPseudomonas putidaen
dc.titleFunctioning of the mercury resistance operon at extremely high Hg(II) loads in a chemostat: a proteome analysis.en
dc.typeArticleen
dc.contributor.departmentTechnical University Braunschweig/HZI-Helmholtz Center for Infection Research, Biochemical Engineering, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.en
dc.identifier.journalJournal of biotechnologyen

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