apl. Prof. Dr. Sabine Hunke

apl. Prof. Dr. Sabine Hunke erforscht, wie Bakterien – insbesondere E. coli und Salmonella – auf Umweltstress reagieren, indem sie sogenannte Zwei-Komponenten-Systeme nutzen. Diese molekularen Signalwege ermöglichen es Bakterien, Veränderungen in ihrer Zellhülle zu erkennen und darauf zu reagieren. Ihre aktuelle Arbeit konzentriert sich darauf, die genauen Mechanismen dieser Sensorsysteme zu verstehen – etwa wie Proteine miteinander interagieren, um Signale weiterzuleiten, und wie Bakterien ihre Gene in Reaktion auf Stress regulieren. Diese Grundlagenforschung ist relevant für die Entwicklung neuer Antibiotika und für das Verständnis von Bakterienvirulenz, da diese Systeme auch bei der Pathogenese eine Rolle spielen. Darüber hinaus leitet sie Doktorandenprogramme, die internationale Nachwuchsforschende in diesem Bereich ausbilden.

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• Doctoral Scholarships from Jameel Education Foundation 17th Cohort

  Quelle ↗

  Förderer: Andere internationale Stiftungen Zeitraum: 03/2023 - 12/2027 Projektleitung: Dr. Andrea George, Jeannette Latino, apl. Prof. Dr. Sabine Hunke

• Doctoral Scholarships from Jameel Education Foundation 18th Cohort

  Quelle ↗

  Förderer: Andere internationale Stiftungen Zeitraum: 03/2024 - 05/2028 Projektleitung: Dr. Andrea George, apl. Prof. Dr. Sabine Hunke, Jeannette Latino

• Doctoral Scolarships from Jameel Education Foundation 19th Cohort

  Quelle ↗

  Förderer: Andere internationale Stiftungen Zeitraum: 06/2026 - 05/2030 Projektleitung: Dr. Andrea George, apl. Prof. Dr. Sabine Hunke, Jeannette Latino

• ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains

  1998

  FEMS Microbiology Reviews · DOI

  Members of the superfamily of adenosine triphosphate (ATP)-binding-cassette (ABC) transport systems couple the hydrolysis of ATP to the translocation of solutes across a biological membrane. Recognized by their common modular organization and two sequence motifs that constitute a nucleotide binding fold, ABC transporters are widespread among all living organisms. They accomplish not only the uptake of nutrients in bacteria but are involved in diverse processes, such as signal transduction, protein secretion, drug and antibiotic resistance, antigen presentation, bacterial pathogenesis and sporulation. Moreover, some human inheritable diseases, like cystic fibrosis, adrenoleukodystrophy and Stargardt's disease are caused by defective ABC transport systems. Thus, albeit of major significance, details of the molecular mechanism by which these systems exert their functions are still poorly understood. In this review, recent data concerning the properties and putative role of the ATP-hydrolyzing subunits/domains are summarized and compared between bacterial and eukaryotic systems.

• Purification, Reconstitution, and Characterization of the CpxRAP Envelope Stress System of Escherichia coli

  2007

  Journal of Biological Chemistry · DOI

  In Escherichia coli the Cpx sensor regulator system senses different kinds of envelope stress and responds by triggering the expression of periplasmic folding factors and proteases. It consists of the membrane-anchored sensor kinase CpxA, the response regulator CpxR, and the periplasmic protein CpxP. The Cpx pathway is induced in vivo by a variety of signals including pH variation, osmotic stress, and misfolded envelope proteins and is inhibited by overproduced CpxP. Because it is not clear how the Cpx pathway is able to recognize and correspond to so many different signals we overproduced, solubilized, purified, and incorporated the complete membrane-integral CpxA protein into proteoliposomes to analyze its biochemical properties in more detail. Autokinase and phosphotransfer activities of the reconstituted CpxA-His6 protein were stimulated by KCl. NaCl also stimulated the activities but to a lesser extent. Other osmotic active solutes as glycine betaine, sucrose, and proline had no effect. The system was further characterized by testing for susceptibility to sensor kinase inhibitors. Among these, Closantel inhibited the activities of solubilized but not of the reconstituted CpxA-His6 protein. We further analyzed the effect of CpxP on CpxA activities. Purified tagless CpxP protein reduced the phosphorylation status of CpxA to 50% but had no effect on CpxA phosphotransfer or phosphatase activities. As the in vitro system excludes the involvement of other factors our finding is the first biochemical evidence for direct protein-protein interaction between the sensor kinase CpxA and the periplasmic protein CpxP resulting in a down-regulation of the autokinase activity of CpxA.