K
Klaus Leonhard
Researcher at Ludwig Maximilian University of Munich
Publications - 5
Citations - 993
Klaus Leonhard is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Membrane protein & Translocase of the inner membrane. The author has an hindex of 5, co-authored 5 publications receiving 945 citations.
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Journal ArticleDOI
AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria.
Klaus Leonhard,Johannes M. Herrmann,Rosemary A. Stuart,Gertrud Mannhaupt,Walter Neupert,Thomas Langer +5 more
TL;DR: Two AAA proteases with their catalytic sites on opposite membrane surfaces constitute a novel proteolytic system for the degradation of membrane proteins in mitochondria.
Journal ArticleDOI
Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
TL;DR: It is shown that Yme1 senses the folding state of solvent-exposed domains and specifically degrades unfolded membrane proteins and suggests that the AAA domains of other AAA proteins may have a similar function.
Journal ArticleDOI
Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface.
Klaus Leonhard,Bernard Guiard,Giovanna Pellecchia,Alexander Tzagoloff,Walter Neupert,Thomas Langer +5 more
TL;DR: It is demonstrated that a model substrate polypeptide containing hydrophilic domains at both sides of the membrane can be completely degraded by either of the AAA proteases, if solvent-exposed domains are in an unfolded state.
Journal ArticleDOI
Role of the ABC transporter Mdl1 in peptide export from mitochondria.
TL;DR: Two pathways of peptide efflux from mitochondria exist that may allow communication between mitochondria and their cellular environment, and Mdl1 was identified as an intracellular peptide transporter localized in the inner membrane of yeast mitochondria.
Journal ArticleDOI
Mba1, a novel component of the mitochondrial protein export machinery of the yeast Saccharomyces cerevisiae.
TL;DR: It is concluded that Mba1 is part of the mitochondrial protein export machinery and represents the first component of a novel Oxa1-independent insertion pathway into the mitochondrial inner membrane.