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Hanjo A. Hellmann

Hanjo Hellmann

Field of Study: Plant Physiology, Molecular Plant Biology
Title: Professor
Degrees: Ph.D., Eberhardt-Karls-University Tübingen, Germany
Homepage: Homepage/Lab Web Site Link
Google Scholar:  Google Scholar
Office: Abelson 435A
Email: hellmann@wsu.edu
Phone: 509-335-2762
Fax: 509-335-3184
Mailing Address: School of Biological Sciences
Washington State University
PO Box 644236
Pullman,WA 99164-4236

RESEARCH INTERESTS

At its present growth rate, the human population will reach nine billion by the year 2050. Concurrently, periods of increased abiotic stress, due to variations in global climate, and the limited availability of arable land are expected to restrict agricultural output. The combination of these factors poses a severe and unprecedented challenge in food production that requires novel approaches to better understand how plants cope with stress. My research uses different molecular and physiological approaches to investigate mechanisms that control protein turnover, transcriptional processes and metabolism in plants. My lab focuses primarily on two areas:
1) Mechanisms that regulate protein dynamics in context with the ubiquitin proteasome pathway. We focus on a specific enzyme that attaches ubiquitin moieties to other proteins and thereby marks them for degradation by the 26S proteasome. Most of the proteins that are marked by the enzyme are transcription factors that control a wide range of physiological and developmental processes in plants.
2) Vitamin B6 homeostasis in plants. The vitamin is a critical cofactor that is needed for broad range of biochemical reactions in the cell, mostly in context with amino acid metabolism. In addition, the vitamin is also a potent antioxidant. We try to understand what regulatory steps exist in plants to regulate the cellular vitamin B6 content in order to sustain normal cellular metabolism and plant growth

Representative Publications:

  • Parra, M., Stahl, S., Hellmann, H. (2018) Vitamin B6 and Its Role in Cell Metabolism and Physiology Cells, 7, 84
    Novikova, I.V., Sharma, N., Moser, T., Sontag, R., Liu, Y., Collazo, M., Cascio, D., Shokuhfar, T., Hellmann, H., Knoblauch, M., Evans, J.E. (2018) Protein Structural Biology Using a Cell-Free Platform from Wheat Germ. Adv. Struct. Chem. Imag. (2018) 4:13
  • Navarre, D.A., Moehninsi, M., Lin, S., Hellmann, H. (2018) Nutritional properties and enhancement/ biofortification of potatoes. Book Chapter Wang-Pruski, G. (ed.), Achieving sustainable cultivation of potatoes Volume 1: Breeding improved varieties, Burleigh Dodds Science Publishing, Cambridge, UK, (ISBN: 978 1 78676 100 2)
  • Chen L., Bernhardt A., Lee J.H., Hellmann H. (2015) Identification of Arabidopsis MYB56 as a novel substrate for CRL3BPM E3 ligases. Mol. Plant 8, 242-250.
  • Leuendorf, E., Mooney, S., Chen, L., Hellmann, H. (2014) Arabidopsis thaliana PDX1.2 is critical for embryo development and heat shock tolerance. Planta 240, 137-146
  • Leuendorf, E., Mooney, S., Chen, L., Hellmann, H. (2014) Arabidopsis thaliana PDX1.2 is critical for embryo development and heat shock tolerance. Planta 240, 137-146
  • Mooney, S., Chen, L., Kühn, C., Navarre, D.A., Knowles, N.R., Hellmann, H. (2013) Genotype Specific Changes in Vitamin B6 Content and the PDX Family in Potato. BioMed Res Int Article ID 389723.
  • Chen, L., Lee, J.H., Weber, H., Tohge, T., Witt, S., Roje, S., Fernie, A.R., Hellmann, H. (2013) Arabidopsis BPM proteins function as substrate adapters to a CUL3-based E3 ligase to affect fatty acid metabolism in plants. Plant Cell 25, 2253-2264.
  • Chen, L., and Hellmann, H. (2013) Plant E3 Ligases: Flexible Enzymes In A Sessile World. Mol Plant 10.1093/mp/sst005
  • Biedermann S. and Hellmann H. (2010) The DDB1a interacting proteins ATCSA-1 and DDB2 are critical factors for UV-B tolerance and genomic integrity in Arabidopsis thaliana. Plant J. 62, 404-415.