Angerer 2017 Biochim Biophys Acta Mol Cell Res

From Bioblast
Publications in the MiPMap
Angerer H, SchΓΆnborn S, Gorka J, Bahr U, Karas M, Wittig I, Heidler J, Hoffmann J, Morgner N, Zickermann V (2017) Acyl modification and binding of mitochondrial ACP to multiprotein complexes.

Β» Biochim Biophys Acta Mol Cell Res 1864:1913-20. PMID: 28802701 Open Access

Angerer Heike, Schoenborn Stefan, Gorka Jan, Bahr Ute, Karas Michael, Wittig Ilka, Heidler Juliana, Hoffmann Jan, Morgner Nina, Zickermann Volker (2017) Biochim Biophys Acta Mol Cell Res

Abstract: 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.

β€’ Bioblast editor: Plangger M

Labels: MiParea: mt-Structure;fission;fusion 

Enzyme: Complex I 

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