Current position

04/2021 – present

Associate Professor and group leader, NNF-CPR, Faculty of Health and Medical Sciences, University of Copenhagen, Denmark

Previous positions

11/2014 – 02/2021

Postdoctoral researcher with Prof. Nenad Ban| ETH Zurich, Switzerland

• reconstitution of the first mammalian mitochondrial translation complexes and their high-resolution structure determination by cryo-electron microscopy

11/2013 – 10/2014

Postdoctoral researcher with Prof. Bernd Bukau| University of Heidelberg, Germany

• biochemical and structural characterization of the function of molecular chaperones

Education

10/2009 – 10/2013

Dr. rer. nat. (summa cum laude) | University of Heidelberg, Germany

Thesis title: ‘The protein disaggregation activity of the ClpB/Hsp104 chaperone is regulated by its M domain’, supervisor: Prof. Bernd Bukau

• function and regulation of molecular chaperones, protein biochemistry and fluorescence microscopy

10/2004 – 09/2009

Diplom in Human Biology (1.1, very good) | University of Greifswald, Germany

Thesis title: ‘Studies on MgsR and Spx paralogs in B. subtilis and S. aureus’about mechanisms of bacterial adaption to oxidative stress, supervisor: Prof. Michael Hecker

• specializations: Microbiology, Immunology, Biochemistry

 Prizes, awards, fellowships

01/2014 – 12/2015: 2-years EMBO Long-Term Fellowship

07/2013:                     Protein Society Symposium ‘Graduate Best Poster Award’, Boston USA

07/2013:                     GlaxoSmithKline travel grant to attend Protein Society Symposium

05/2012:                     HBIGS travel grant to attend Cold Spring Harbor Meeting

10/2009 – 12/2011: ZMBH PhD fellowship

09/2009:                    3-years PhD fellowship of the Hartmut Hoffmann-Berling International Graduate School (gratefully declined in favour of ZMBH PhD fellowship)

 Training in leadership and mentoring

• course ‘Lateral leadership’ (2 days, ETH Zurich, 09/2020)
• course ‘Project Management’ (3days, ETH Zurich, 03-05/2020)
• course ‘Leadership essentials’ (3 days, BWI Zurich, 02-03/2020)
• course ‘Learning to Teach’ (35 hours, ETH Zurich, 04/2019)
• course ‘Intra- and Interpersonal Competences in Academia’ (2 ½  days, ETH Zurich,
• 01-02/2019)
• course ‘Laboratory Leadership for Postdocs’ (3 days, EMBO course, 06/2018)

Institutional responsibilities

2016 – 2021:             AVETH (Academic Association of Scientific Staff at ETH Zurich)

2016 – 2021:             Female peer mentoring group (Department of Biology, ETH Zurich)

2012 − 2014:             IT team member and leader (2013-2014) at the life sciences job fair CONTACT, Heidelberg, Germany, (https://www.biocontact.info)

2005 − 2008:      member and president (2007-2008) of the student’s association Humanbiologie e.V. Greifswald

The Kummer group has a deep interest in understanding the biology of human mitochondria with a specific focus on how these important organelles maintain their DNA and how they produce functional RNA species. We combine structural approaches with functional biochemistry and cell biology in order to investigate essential mitochondrial processes in molecular and cellular detail. Our structural analysis is primarily based on single particle cryo-EM and cryo-electron tomography. By gaining fundamental mechanistic insights into mitochondrial DNA maintenance and RNA maturation, our lab hopes to shed light on the molecular triggers of mitochondrial disorders that are frequently caused by mutations in the involved protein factors.

Main findings

Protein synthesis in mammalian mitochondria

Kummer et al. Nature 2018, Kummer and Ban EMBO 2020, Kummer and Ban Nat Rev MCB 2021

Cryo-EM studies unraveling specific structural and functional adaptions in the process of protein production that mammalian mitochondria have acquired during evolution. Among these studies is the first reconstituted mitochondrial translation complex.

Reversion of protein aggregation by concerted action of molecular chaperones

Seyffer, Kummer et al. NSMB 2012, Oguchi, Kummer et al. 2012, Carroni et al. eLIFE 2014

Unraveled a novel principle of how two chaperone systems disentangle aggregating, misfolded proteins inside the cell. Showed that direct interaction of the chaperones tunes their activity in space and time in order to adequately respond to cellular needs and prevent detrimental off-target effects. Bacteria and fungi thereby manage to sustain a healthy proteome at a relatively low energetic expense.