S
Steffen Augustin
Researcher at University of Cologne
Publications - 5
Citations - 463
Steffen Augustin is an academic researcher from University of Cologne. The author has contributed to research in topics: Proteases & Protease. The author has an hindex of 5, co-authored 5 publications receiving 443 citations.
Papers
More filters
Journal ArticleDOI
m‐AAA protease‐driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria
TL;DR: Findings reveal for the first time a non‐proteolytic function of the m‐AAA protease during mitochondrial biogenesis and rationalise the requirement of a preceding step for intramembrane cleavage by rhomboid.
Journal ArticleDOI
Characterization of Peptides Released from Mitochondria EVIDENCE FOR CONSTANT PROTEOLYSIS AND PEPTIDE EFFLUX
TL;DR: A constant efflux of peptides from mitochondria is demonstrated and new insight is provided into the stability of the mitochondrial proteome and the efficiency of mitochondrial biogenesis.
Journal ArticleDOI
An Intersubunit Signaling Network Coordinates ATP Hydrolysis by m-AAA Proteases
Steffen Augustin,Florian Gerdes,Sukyeong Lee,Francis T.F. Tsai,Thomas Langer,Thomas Langer,Takashi Tatsuta +6 more
TL;DR: Coordinated ATP hydrolysis within m-AAA protease ring complexes, conserved AAA+ machines in the inner membrane of mitochondria, provides insight into how AAA+ proteins convert energy derived from ATP Hydrolysis into mechanical work.
Journal ArticleDOI
Role of the Novel Metallopeptidase MoP112 and Saccharolysin for the Complete Degradation of Proteins Residing in Different Subcompartments of Mitochondria
TL;DR: The identification of Mop112, a novel metallopeptidase of the pitrilysin family M16 localized in the intermembrane space of yeast mitochondria, and the discovery of peptides released from peptidase-deficient mitochondria by mass spectrometry indicates a dual function of MOP112 and saccharolysin.
Journal ArticleDOI
Electron Cryomicroscopy Structure of a Membrane-anchored Mitochondrial AAA Protease
Sukyeong Lee,Steffen Augustin,Takashi Tatsuta,Florian Gerdes,Thomas Langer,Thomas Langer,Francis T.F. Tsai +6 more
TL;DR: It is demonstrated that replacement of only two amino acid residues within the metallopeptidase domain of Yta12 allows its assembly into homo-oligomeric complexes, suggesting a mechanism regarding how proteins are recognized and degraded by m-AAA proteases.