Eva Kummer
ETH Zurich
15 Papers
51 Citations
Eva Kummer is an academic researcher from ETH Zurich. The author has contributed to research in topics: CLPB & Translation (biology). The author has an hindex of 10, co-authored 14 publications. Previous affiliations of Eva Kummer include German Cancer Research Center & École Polytechnique Fédérale de Lausanne.
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Papers
Mechanisms and regulation of protein synthesis in mitochondria
Eva Kummer,Nenad Ban +1 more
TL;DR: In this paper, the authors review fundamental insights that have been made into the biogenesis, architecture and mechanisms of the mitochondrial translation apparatus in the past years owing to the emergence of numerous near-atomic structures and a considerable amount of biochemical work.
234
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
Fabian Seyffer,Eva Kummer,Yuki Oguchi,Juliane Winkler,Mohit Kumar,Regina Zahn,Victor Sourjik,Bernd Bukau,Axel Mogk +8 more
TL;DR: The results uncover a new function for Hsp70: the coupling of substrate targeting to AAA+ chaperone activation at aggregate surfaces, and it is shown that ClpB has low intrinsic disaggregation activity that is normally repressed by theClpB middle (M) domain.
178
Cooperation of Hsp70 and Hsp100 chaperone machines in protein disaggregation
Axel Mogk,Eva Kummer,Bernd Bukau +2 more
TL;DR: This work has shown that a bi-chaperone system composed of ATP-dependent Hsp70 and hexameric Hsp100 (ClpB/Hsp104) chaperones, which rescue aggregated proteins and provide thermotolerance to cells, is crucial for cell viability as permanently activated Hsp 100 variants are toxic.
A tightly regulated molecular toggle controls AAA+ disaggregase.
Yuki Oguchi,Eva Kummer,Fabian Seyffer,Mykhaylo Berynskyy,Benjamin Anstett,Regina Zahn,Rebecca C. Wade,Axel Mogk,Bernd Bukau +8 more
TL;DR: It is shown that M domains nestle at the ClpB ring surface, with both M-domain motifs contacting the first ATPase domain (AAA-1) and a regulated M- domain toggle control mechanism is elucidated.
156
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation.
Marta Carroni,Eva Kummer,Yuki Oguchi,Petra Wendler,Daniel K. Clare,Irmgard Sinning,Jürgen Kopp,Axel Mogk,Bernd Bukau,Helen R. Saibil +9 more
TL;DR: EM structures of the BAP variant of ClpB that binds the protease ClpP show a wavelike activation of Cl pB subunits around the ring, and Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single Clp B hexamer.