Acyl modification and binding of mitochondrial ACP to multiprotein complexes
| Autor: | Heike Angerer, Michael Karas, Nina Morgner, Ute Bahr, Jan Hoffmann, Juliana Heidler, Stefan Schönborn, Volker Zickermann, Ilka Wittig, Jan Gorka |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Iron-Sulfur Proteins Enzyme complex Protein subunit Yarrowia Saccharomyces cerevisiae Fungal Proteins 03 medical and health sciences chemistry.chemical_compound NDUFA6 Acyl Carrier Protein Amino Acid Sequence Molecular Biology Central element Electron Transport Complex I biology Fatty Acids Cell Biology biology.organism_classification NDUFB9 Mitochondria Acyl carrier protein 030104 developmental biology chemistry Biochemistry Multiprotein Complexes biology.protein Phosphopantetheine |
| Zdroj: | Biochimica et biophysica acta. Molecular cell research. 1864(10) |
| ISSN: | 0167-4889 |
| Popis: | The mitochondrial acyl carrier protein (ACPM/NDUFAB1) is a central element of the mitochondrial fatty acid synthesis type II machinery. Originally ACPM was detected as a subunit of respiratory complex I but the reason for the association with the large enzyme complex remained elusive. Complex I from the aerobic yeast Yarrowia lipolytica comprises two different ACPMs, ACPM1 and ACPM2. They are anchored to the protein complex by LYR (leucine-tyrosine-arginine) motif containing protein (LYRM) subunits LYRM3 (NDUFB9) and LYRM6 (NDUFA6). The ACPM1-LYRM6 and ACPM2-LYRM3 modules are essential for complex I activity and assembly/stability, respectively. We show that in addition to the complex I bound fraction, ACPM1 is present as a free matrix protein and in complex with the soluble LYRM4(ISD11)/NFS1 complex implicated in Fe-S cluster biogenesis. We show that the presence of a long acyl chain bound to the phosphopantetheine cofactor is important for docking ACPMs to protein complexes and we propose that association of ACPMs and LYRMs is universally based on a new protein-protein interaction motif. |
| Databáze: | OpenAIRE |
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