Eva Kummer

Eva Kummer

Associate professor, group leader

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.

Selected publications

  1. Mechanisms and regulation of protein synthesis in mitochondria

    Kummer, Eva & Ban, N., 16 Feb 2021, (E-pub ahead of print) In: Nature Reviews. Molecular Cell Biology.

    Research output: Contribution to journalReviewResearchpeer-review

  2. Structural insights into mammalian mitochondrial translation elongation catalyzed by mtEFG1

    Kummer, Eva & Ban, N., 2020, In: The EMBO Journal. 39, 15, e104820.

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Unique features of mammalian mitochondrial translation initiation revealed by cryo-EM

    Kummer, Eva, Leibundgut, M., Rackham, O., Lee, R. G., Boehringer, D., Filipovska, A. & Ban, N., 2018, In: Nature. 560, 7717, p. 263-267 5 p.

    Research output: Contribution to journalJournal articleResearchpeer-review

  4. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

    Carroni, M., Kummer, Eva, Oguchi, Y., Wendler, P., Clare, D. K., Sinning, I., Kopp, J., Mogk, A., Bukau, B. & Saibil, H. R., 2014, In: eLife. 3, p. e02481

    Research output: Contribution to journalJournal articleResearchpeer-review

  5. Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces

    Seyffer, F., Kummer, Eva, Oguchi, Y., Winkler, J., Kumar, M., Zahn, R., Sourjik, V., Bukau, B. & Mogk, A., 2012, In: Nature Structural & Molecular Biology. 19, 12, p. 1347-55 9 p.

    Research output: Contribution to journalJournal articleResearchpeer-review

  6. A tightly regulated molecular toggle controls AAA+ disaggregase

    Oguchi, Y., Kummer, Eva, Seyffer, F., Berynskyy, M., Anstett, B., Zahn, R., Wade, R. C., Mogk, A. & Bukau, B., 2012, In: Nature Structural & Molecular Biology. 19, 12, p. 1338-46 9 p.

    Research output: Contribution to journalJournal articleResearchpeer-review

ID: 255981517