Prof. Eitinger erforscht Membrantransporter in Mikroorganismen, insbesondere ECF-Transporter (Energy-Coupling-Factor-Transporter) und deren Mechanismen beim Transport von Metallionen wie Nickel und Kobalt sowie Vitaminen in prokaryotische Zellen. Ein aktueller Anwendungsfokus liegt auf der Hemmung von Ammoniakemissionen aus Gülle durch gezielte Blockade der Nickelaufnahme in Mikroben — ein Problem, das für die Landwirtschaft und Umweltschutz relevant ist. Seine Arbeiten kombinieren strukturbiologische Analysen mit funktionalen Studien, um die molekularen Mechanismen dieser Transporter zu verstehen und gezielt zu manipulieren. Die Erkenntnisse ermöglichen es, mikrobielle Prozesse wie Ureaseaktivität zu regulieren und damit Emissionen zu reduzieren.
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Prof. Dr. rer. nat. Thomas Eitinger
HU-FIS-Profil ↗Inhibition of ammonia emissions from manure through inhibition of nickel uptake into microbial cells
university
Förderer: DFG Sachbeihilfe Zeitraum: 10/2003 - 03/2007 Projektleitung: Prof. Dr. rer. nat. Thomas Eitinger
Förderer: DFG Sachbeihilfe Zeitraum: 10/2005 - 12/2006 Projektleitung: Prof. Dr. rer. nat. Thomas Eitinger
Förderer: DFG Sachbeihilfe Zeitraum: 10/2006 - 08/2010 Projektleitung: Prof. Dr. rer. nat. Thomas Eitinger
Nature Biotechnology · DOI
The H(2)-oxidizing lithoautotrophic bacterium Ralstonia eutropha H16 is a metabolically versatile organism capable of subsisting, in the absence of organic growth substrates, on H(2) and CO(2) as its sole sources of energy and carbon. R. eutropha H16 first attracted biotechnological interest nearly 50 years ago with the realization that the organism's ability to produce and store large amounts of poly[R-(-)-3-hydroxybutyrate] and other polyesters could be harnessed to make biodegradable plastics. Here we report the complete genome sequence of the two chromosomes of R. eutropha H16. Together, chromosome 1 (4,052,032 base pairs (bp)) and chromosome 2 (2,912,490 bp) encode 6,116 putative genes. Analysis of the genome sequence offers the genetic basis for exploiting the biotechnological potential of this organism and provides insights into its remarkable metabolic versatility.
Journal of Bacteriology · DOI
The transition metals nickel and cobalt, essential components of many enzymes, are taken up by specific transport systems of several different types. We integrated in silico and in vivo methods for the analysis of various protein families containing both nickel and cobalt transport systems in prokaryotes. For functional annotation of genes, we used two comparative genomic approaches: identification of regulatory signals and analysis of the genomic positions of genes encoding candidate nickel/cobalt transporters. The nickel-responsive repressor NikR regulates many nickel uptake systems, though the NikR-binding signal is divergent in various taxonomic groups of bacteria and archaea. B(12) riboswitches regulate most of the candidate cobalt transporters in bacteria. The nickel/cobalt transporter genes are often colocalized with genes for nickel-dependent or coenzyme B(12) biosynthesis enzymes. Nickel/cobalt transporters of different families, including the previously known NiCoT, UreH, and HupE/UreJ families of secondary systems and the NikABCDE ABC-type transporters, showed a mosaic distribution in prokaryotic genomes. In silico analyses identified CbiMNQO and NikMNQO as the most widespread groups of microbial transporters for cobalt and nickel ions. These unusual uptake systems contain an ABC protein (CbiO or NikO) but lack an extracytoplasmic solute-binding protein. Experimental analysis confirmed metal transport activity for three members of this family and demonstrated significant activity for a basic module (CbiMN) of the Salmonella enterica serovar Typhimurium transporter.
Journal of Bacteriology · DOI
The specific and tightly controlled transport of numerous nutrients and metabolites across cellular membranes is crucial to all forms of life. However, many of the transporter proteins involved have yet to be identified, including the vitamin transporters in various human pathogens, whose growth depends strictly on vitamin uptake. Comparative analysis of the ever-growing collection of microbial genomes coupled with experimental validation enables the discovery of such transporters. Here, we used this approach to discover an abundant class of vitamin transporters in prokaryotes with an unprecedented architecture. These transporters have energy-coupling modules comprised of a conserved transmembrane protein and two nucleotide binding proteins similar to those of ATP binding cassette (ABC) transporters, but unlike ABC transporters, they use small integral membrane proteins to capture specific substrates. We identified 21 families of these substrate capture proteins, each with a different specificity predicted by genome context analyses. Roughly half of the substrate capture proteins (335 cases) have a dedicated energizing module, but in 459 cases distributed among almost 100 gram-positive bacteria, including numerous human pathogens, different and unrelated substrate capture proteins share the same energy-coupling module. The shared use of energy-coupling modules was experimentally confirmed for folate, thiamine, and riboflavin transporters. We propose the name energy-coupling factor transporters for the new class of membrane transporters.