Prof. Dr. rer. nat. Thomas Eitinger

Profil

Zusammenfassung

Thomas Eitinger erforscht Membrantransporter in Mikroorganismen, insbesondere wie Bakterien Metallionen wie Nickel und Cobalt aufnehmen. Seine Expertise umfasst die molekulare Charakterisierung von Transportsystemen, ihre Struktur-Funktions-Beziehungen und praktische Anwendungen wie die Reduktion von Ammoniakemissionen aus Gülle durch Inhibition von Nickelaufnahme.

Skills

Name

Prof. Dr. rer. nat. Thomas Eitinger

Titel

Prof. Dr. rer. nat.

Fakultät

Lebenswissenschaftliche Fakultät

Institut

Institut für Biologie

Arbeitsgruppe

Mikrobiologie

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HU-FIS-Profil

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28.6.2026, 01:04:54

• Dynamik der Untereinheiteninteraktionen in ECF-Transportern

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 01/2014 - 12/2016 Projektleitung: Prof. Dr. rer. nat. Thomas Eitinger

• ECF-Transporter – eine neue Klasse von Membrantransportern mit ATP-Bindekassette

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 10/2009 - 05/2014 Projektleitung: Prof. Dr. rer. nat. Thomas Eitinger

• Eine mechanistisch neuartige Gruppe von Membrantransportern

  Quelle ↗

  Förderer: DFG Sachbeihilfe Zeitraum: 10/2006 - 08/2010 Projektleitung: Prof. Dr. rer. nat. Thomas Eitinger

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• Genome sequence of the bioplastic-producing “Knallgas” bacterium Ralstonia eutropha H16

  2006

  Nature Biotechnology · 662 Zitationen · DOI

• Comparative and Functional Genomic Analysis of Prokaryotic Nickel and Cobalt Uptake Transporters: Evidence for a Novel Group of ATP-Binding Cassette Transporters

  2005

  Journal of Bacteriology · 295 Zitationen · 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.

• A Novel Class of Modular Transporters for Vitamins in Prokaryotes

  2008

  Journal of Bacteriology · 284 Zitationen · 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.

• Syddansk Universitet

  Inhibition of ammonia emissions from manure through inhibition of nickel uptake into microbial cells

  university