Kerstin Helbig

Die Person ist Expertin für Forschungsdatenmanagement (FDM) und Open Science, mit einem Schwerpunkt auf der Implementierung von FAIR-Prinzipien in der wissenschaftlichen Praxis. Sie engagiert sich stark in der Entwicklung von Forschungsinfrastrukturen, insbesondere im Rahmen der Nationalen Forschungsdateninfrastruktur (NFDI), und fördert die Datenkompetenz durch Hochschuldidaktik und Training. Ihre Arbeit umfasst die Konzeption von Datenmanagementplänen, die Evaluation von FDM-Services und die Förderung eines Kulturwandels in der Wissenschaft. Zusätzlich bringt sie naturwissenschaftliche Expertise aus den Bereichen Molekularbiologie und Analytische Chemie mit, was ihre Fähigkeit zur interdisziplinären Beratung unterstreicht.

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• Concept Development for Collaborative Research Data Management Services

  Quelle ↗

  Förderer: Berlin University Alliance (BUA) Zeitraum: 08/2020 - 11/2022 Projektleitung: Kerstin Helbig, Malte Dreyer

• FDLink Rahmenbedingungen für Kulturwandel und gemeinsame Servicelandschaft stärken

  Quelle ↗

  Förderer: DFG sonstige Programme Zeitraum: 12/2024 - 04/2028 Projektleitung: Malte Dreyer, Kerstin Helbig

• FDNext Weiterentwicklung der Forschungsdatenpraxis: Werkzeuge zur Qualitätsentwicklung für Serviceeinrichtungen in Kooperation mit Fachbereichen und Forschungsverbünden - Teilprojekt Konzepte und Kompetenzen für FD-Rechtsberatung

  Quelle ↗

  Förderer: DFG sonstige Programme Zeitraum: 09/2023 - 07/2025 Projektleitung: Kerstin Helbig, Malte Dreyer

• Glutathione and Transition-Metal Homeostasis in<i>Escherichia coli</i>

  2008

  Journal of Bacteriology · DOI

  Glutathione (GSH) and its derivative phytochelatin are important binding factors in transition-metal homeostasis in many eukaryotes. Here, we demonstrate that GSH is also involved in chromate, Zn(II), Cd(II), and Cu(II) homeostasis and resistance in Escherichia coli. While the loss of the ability to synthesize GSH influenced metal tolerance in wild-type cells only slightly, GSH was important for residual metal resistance in cells without metal efflux systems. In mutant cells without the P-type ATPase ZntA, the additional deletion of the GSH biosynthesis system led to a strong decrease in resistance to Cd(II) and Zn(II). Likewise, in mutant cells without the P-type ATPase CopA, the removal of GSH led to a strong decrease of Cu(II) resistance. The precursor of GSH, gamma-glutamylcysteine (gammaEC), was not able to compensate for a lack of GSH. On the contrary, gammaEC-containing cells were less copper and cadmium tolerant than cells that contained neither gammaEC nor GSH. Thus, GSH may play an important role in trace-element metabolism not only in higher organisms but also in bacteria.

• Cadmium Toxicity in Glutathione Mutants of<i>Escherichia coli</i>

  2008

  Journal of Bacteriology · DOI

  The higher affinity of Cd(2+) for sulfur compounds than for nitrogen and oxygen led to the theoretical consideration that cadmium toxicity should result mainly from the binding of Cd(2+) to sulfide, thiol groups, and sulfur-rich complex compounds rather than from Cd(2+) replacement of transition-metal cations from nitrogen- or oxygen-rich biological compounds. This hypothesis was tested by using Escherichia coli for a global transcriptome analysis of cells synthesizing glutathione (GSH; wild type), gamma-glutamylcysteine (DeltagshB mutant), or neither of the two cellular thiols (DeltagshA mutant). The resulting data, some of which were validated by quantitative reverse transcription-PCR, were sorted using the KEGG (Kyoto Encyclopedia of Genes and Genomes) orthology system, which groups genes hierarchically with respect to the cellular functions of their respective products. The main difference among the three strains concerned tryptophan biosynthesis, which was up-regulated in wild-type cells upon cadmium shock and strongly up-regulated in DeltagshA cells but repressed in DeltagshB cells containing gamma-glutamylcysteine instead of GSH. Overall, however, all three E. coli strains responded to cadmium shock similarly, with the up-regulation of genes involved in protein, disulfide bond, and oxidative damage repair; cysteine and iron-sulfur cluster biosynthesis; the production of proteins containing sensitive iron-sulfur clusters; the storage of iron; and the detoxification of Cd(2+) by efflux. General energy conservation pathways and iron uptake were down-regulated. These findings indicated that the toxic action of Cd(2+) indeed results from the binding of the metal cation to sulfur, lending support to the hypothesis tested.