Dr Manajit Hayer-Hartl
- Section Biochemistry and Biophysics
- Location Martinsried, Germany
- Election year 2018
Research
Research Priorities: Molecular chaperones, protein folding, artificial proteins, photosynthesis, Rubisco biogenesis, crop plants
Manajit Hayer-Hartl is a Singaporean biophysicist and biochemist. She conducts research into molecular machines (chaperones) and their role in protein folding. Chaperones are also useful in creating artificial proteins in test tubes. With her team, Manajit Hayer-Hartl was able to create a model of the key protein in photosynthesis. Her research results may help to develop more efficient crops.
Proteins are involved in many essential processes within cells. Photosynthesis, one of the most important biological processes, entails plants converting carbon dioxide and water into oxygen and sugar. However, proteins can only fulfil their functions once they have folded themselves into the correct three-dimensional structure. To ensure that proteins are folded correctly, cells use “auxiliary proteins”, also known as molecular chaperones.
However, chaperones are also an important tool for scientific research, as they can be used to artificially create proteins in test tubes. “Rubisco” is the key protein in photosynthesis. It binds carbon dioxide and thus creates sugar molecules, which serve as building material for the organism. Manajit Hayer-Hartl was able to create this protein in the lab.
She now aims to modify the artificially generated protein in such a way that it makes more efficient use of carbon dioxide than the natural protein. This could lead to increased production of grains. Hayer-Hartl’s work could also be important for climate protection, as it might help to create plants and microorganisms which work more effectively and are able to bind more carbon dioxide from the atmosphere.
Manajit Hayer-Hartl is a Singaporean biophysicist and biochemist. She conducts research into molecular machines (chaperones) and their role in protein folding. Chaperones are also useful in creating artificial proteins in test tubes. With her team, Manajit Hayer-Hartl was able to create a model of the key protein in photosynthesis. Her research results may help to develop more efficient crops.
Proteins are involved in many essential processes within cells. Photosynthesis, one of the most important biological processes, entails plants converting carbon dioxide and water into oxygen and sugar. However, proteins can only fulfil their functions once they have folded themselves into the correct three-dimensional structure. To ensure that proteins are folded correctly, cells use “auxiliary proteins”, also known as molecular chaperones.
However, chaperones are also an important tool for scientific research, as they can be used to artificially create proteins in test tubes. “Rubisco” is the key protein in photosynthesis. It binds carbon dioxide and thus creates sugar molecules, which serve as building material for the organism. Manajit Hayer-Hartl was able to create this protein in the lab.
She now aims to modify the artificially generated protein in such a way that it makes more efficient use of carbon dioxide than the natural protein. This could lead to increased production of grains. Hayer-Hartl’s work could also be important for climate protection, as it might help to create plants and microorganisms which work more effectively and are able to bind more carbon dioxide from the atmosphere.
Career
- since 2014 Group Leader, Research Group “Chaperonin-assisted Protein Folding”, Max Planck Institute (MPI) of Biochemistry, Martinsried, Germany
- since 2006 Principal Investigator, Department of “Cellular Biochemistry”, MPI of Biochemistry, Martinsried, Germany
- 1997-2005 Research Group Leader, Department of “Cellular Biochemistry”, MPI of Biochemistry, Martinsried, Germany
- 1991-1996 Research Associate, Department of Cellular Biochemistry and Biophysics, Sloan-Kettering-Institute, New York City, USA
- 1989-1990 Postdoctoral Fellow, Jules Stein Eyes Institute, University of California (UCLA), Los Angeles, USA
- 1987-1989 Postdoctoral Fellow, Institute of Physical Biochemistry, Ludwig-Maximilians-Universität (LMU) München, Munich, Germany
- 1986-1987 Postdoctoral Fellow, Institut Pasteur, Strasbourg, France
- 1984-1986 Postdoctoral Fellow, Department of Biochemistry, Oxford University, Oxford, UK
- 1984 PhD in Chemistry, University of Stirling, Stirling, UK
- 1981 BSc in Biology and Chemistry, University of Stirling, Stirling, UK
Projects
- 2016-2024 Principal Investigator, Subproject “Mechanisms of chaperone-mediated protein folding and assembly”, Collaborative Research Centre (CRC) 1035, German Research Foundation (DFG), Germany
- 2001-2012 Principal Investigator, Subproject “Chaperone-mediated protein folding”, CRC 594, DFG, Germany
Honours and Memberships
- 2022 Lawrence Bogorad Award, American Society of Plant Biologists (ASPB), USA
- 2020 ASBMB Merck Award, American Society of Biochemistry and Molecular Biology (ASBMB), USA
- since 2018 Member, German National Academy of Sciences Leopoldina, Germany
- 2018 Charles F. Kettering Prize, ASPB, USA
- 2017 Dorothy Crowfoot Hodgkins Award, Protein Society, USA
- since 2016 Member, European Molecular Biology Organization (EMBO)