Short CV/Education and training

  • Since 2006
    Independent Research Group Leader and Principal Investigator, Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany

  • 1997 – 2005
    Research Group Leader, Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany

  • 1991 – 1996
    Research Associate, Department of Cellular Biochemistry and Biophysics, Sloan-Kettering Institute, New York, USA

  • 1989 – 1990
    Post-doc, Jules Stein Eye Institute, Los Angeles, USA

  • 1987 – 1989
    Post-doc, Institute für Physikalische Biochemie, Munich, Germany

  • 1986 – 1987
    Post-doc, Louis Pasteur Institute, Strasbourg, France

  • 1984 – 1986
    Post-doc, Department of Biochemistry, Oxford University, UK

  • 1984
    PhD in Chemistry – University of Stirling, Scotland, UK

  • 1981
    BSc. Joint Honors in Biology & Chemistry – University of Stirling, Scotland, UK

  • 1977
    General Teacher Certificate – Ministry of Education, Singapore

Selected publications

  • Dual function of protein confinement in chaperone-assisted protein folding. A. Brinker, G. Pfeifer, M.J. Kerner, D.J. Naylor, F.U. Hartl and M. Hayer-Hartl (2001). Cell 107, 223-233. (doi: 10.1016/s0092-8674(01)00517-7).

  • Structure and Function of RbcX, a specific assembly chaperone for hexadecameric Rubisco. Saschenbrecker, S., Bracher, A., Rao, K.V., Rao, B.V, Hartl, F.U. and Hayer-Hartl, M. (2007). Cell 129, 1189-1200. (doi: 10.1016/j.cell.2007.04.025).

  • Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Liu, C., Young, A.L., Starling-Windhof, A., Bracher, A., Saschenbrecker, S., Rao, B.V., Rao, K.V., Berninghausen, O., Mielke, T., Hartl, F.U., Beckmann, R. and Hayer-Hartl, M. (2010). Nature 463, 197-202. (doi: 10.1038/nature08651).

  • Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F.U., Bracher, A., and Hayer-Hartl, M. (2011). Nature 479, 194-199. (doi: 10.1038/nature10568).

  • Structure of green-type Rubisco activase from tobacco. Stotz, M., Mueller-Cajar, O., Ciniawsky, S., Wendler, P., Hartl, F.U., Bracher, A. and Hayer-Hartl, M. (2011). Nat. Struct. Mol. Biol. 18, 875-880. (doi: 10.1038/nsmb.2171).

  • Structure and mechanism of the Rubisco assembly chaperone Raf1. Hauser, T., Bhat, J., Miličić, G., Wendler, P., Hartl, F.U., Bracher, B. and Hayer-Hartl, M. (2015). Nat. Struct. Mol. Biol. 22, 720-728. (doi: 10.1038/nsmb.3062).

  • Mechanism of enzyme repair by the AAA+ chaperone Rubisco activase. Bhat, J.Y., Miličić, G., Thieulin-Pardo, G., Bracher, A., Maxwell, A., Ciniawsky, S., Mueller-Cajar, O., Engen, J.R., Hartl, F.U., Wendler, P. and Hayer-Hartl, M. (2017). Mol. Cell 67, 744-756. (doi: 10.1016/j.molcel.2017.07.004).

  • Plant Rubisco assembly in E. coli with five chloroplast chaperones including BSD2. Aigner, H., Wilson, H.R., Bracher, A., Calisse, L., Bhat, J.Y., Hartl, F.U. and Hayer-Hartl, M. (2017). Science 358, 1272-1278. (doi: 10.1126/science.aap9221).

  • Rubisco condensate formation by CcmM in -carboxysome biogenesis. Wang, H., Yan, X, Aigner, H., Bracher, A., Nguyen, N.D., Hee, W.Y., Long, B.M., Price, G.D., Hartl, F.U. and Hayer-Hartl, M. (2019). Nature 566, 131-135. (doi: 10.1038/s41586-019-0880-5).

  • Dual role of a Rubisco activase in metabolic repair and carboxysome organization. Flecken, M., Wang, H., Popilka, L., Hartl, F.U., Bracher, A. and Hayer-Hartl, M. (2020). Cell 183(2), 457-473. (doi: 10.1016/j.cell.2020.09.010).



Complete list of publications

Membership in scientific bodies/juries

  • Elected member, German Academy of Sciences Leopoldina, 2018

  • International Society of Photosynthesis Research (ISPR), since 2016

  • Elected member, European Molecular Biology Organization (EMBO), 2016

  • The American Society for Biochemistry & Molecular Biology (ASBMB), since 2012

  • Gesellschaft für Biochemie und Molekularbiologie (GBM), since 1999

Media coverage

  • https://www.isaaa.org/kc/cropbiotechupdate/newsletter/default.asp?Date=12/13/2017

  • https://www.x-mol.com/paper/617077

  • https://idw-online.de/de/news709388

  • https://idw-online.news/2019/01/23/a-boost-for-photosynthesis/

  • https://www.laborjournal.de/rubric/methoden/methoden/v193.php

  • http://www.laborjournal-archiv.de/epaper/LJ_18_04/76/

  • https://www.pressebox.de/inaktiv/max-planck-gesellschaft-zur-foerderung-der-wissenschaften-ev/Anstandsdamen-fuer-den-Klimaschutz/boxid/314561

  • https://www.techbriefs.com/component/content/article/tb/supplements/gdm/stories/news/12023

  • https://www.internetchemie.info/news/2011/nov11/rubisco-aktivase.php

  • https://www.innovations-report.de/fachgebiete/biowissenschaften-chemie/highspeed-origami-in-der-zelle-forscher-klaeren-wichtigen-mechanismus-der-proteinfaltung/

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