ROMO1 is a constituent of the human presequence translocase required for YME1L protease import
| Autor: | Thomas Langer, Andreas Linden, Henning Urlaub, Abhishek Aich, Sven Dennerlein, Frank Richter, Miroslav Nikolov, Stefan Jakobs, Nataliia Naumenko, Peter Rehling, Daniel C. Jans, Thomas MacVicar |
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| Rok vydání: | 2018 |
| Předmět: |
Saccharomyces cerevisiae
Respiratory chain GTPase Mitochondrion Article ROMO1 YME1L Mitochondrial Proteins 03 medical and health sciences 0302 clinical medicine Mitochondrial Precursor Protein Import Complex Proteins Humans Translocase Inner membrane Research Articles 030304 developmental biology 0303 health sciences biology Membrane Proteins Membrane Transport Proteins Metalloendopeptidases Cell Biology biology.organism_classification Cell biology Protein Transport HEK293 Cells Membrane protein Gene Knockdown Techniques Mitochondrial Membranes biology.protein ATPases Associated with Diverse Cellular Activities 030217 neurology & neurosurgery Biogenesis |
| Zdroj: | J Cell Biol The Journal of Cell Biology |
| Popis: | Mitochondria are the powerhouses of eukaryotic cells and rely on protein import from the cytosol. Richter et al. found ROMO1 as a new constituent of the human mitochondrial import machinery linking protein import to quality control and mitochondrial morphology. The mitochondrial presequence translocation machinery (TIM23 complex) is conserved between the yeast Saccharomyces cerevisiae and humans; however, functional characterization has been mainly performed in yeast. Here, we define the constituents of the human TIM23 complex using mass spectrometry and identified ROMO1 as a new translocase constituent with an exceptionally short half-life. Analyses of a ROMO1 knockout cell line revealed aberrant inner membrane structure and altered processing of the GTPase OPA1. We show that in the absence of ROMO1, mitochondria lose the inner membrane YME1L protease, which participates in OPA1 processing and ROMO1 turnover. While ROMO1 is dispensable for general protein import along the presequence pathway, we show that it participates in the dynamics of TIM21 during respiratory chain biogenesis and is specifically required for import of YME1L. This selective import defect can be linked to charge distribution in the unusually long targeting sequence of YME1L. Our analyses establish an unexpected link between mitochondrial protein import and inner membrane protein quality control. |
| Databáze: | OpenAIRE |
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