Eukaryotic LYR Proteins Interact with Mitochondrial Protein Complexes

Biology

Heike Angerer¹ 

[1] Goethe University Frankfurt, Medical School, Institute of Biochemistry II, Structural Bioenergetics Group, Max-von-Laue Street 9, Frankfurt am Main 60438, Germany; E-Mail

关键词: LYR proteins;    LYRM;    LYR motif;    mitochondria;    OXPHOS complexes;    respiratory complex I;    mitochondrial acyl-carrier protein;    ACPM;    mitochondrial fatty acid synthesis type II;    lipoic acid (6;    8-dithio-octanoic acid);    reactive oxygen species;    insulin resistance;   

DOI  :  10.3390/biology4010133

来源: mdpi

【 摘 要 】

In eukaryotic cells, mitochondria host ancient essential bioenergetic and biosynthetic pathways. LYR (leucine/tyrosine/arginine) motif proteins (LYRMs) of the Complex1_LYR-like superfamily interact with protein complexes of bacterial origin. Many LYR proteins function as extra subunits (LYRM3 and LYRM6) or novel assembly factors (LYRM7, LYRM8, ACN9 and FMC1) of the oxidative phosphorylation (OXPHOS) core complexes. Structural insights into complex I accessory subunits LYRM6 and LYRM3 have been provided by analyses of EM and X-ray structures of complex I from bovine and the yeast Yarrowia lipolytica, respectively. Combined structural and biochemical studies revealed that LYRM6 resides at the matrix arm close to the ubiquinone reduction site. For LYRM3, a position at the distal proton-pumping membrane arm facing the matrix space is suggested. Both LYRMs are supposed to anchor an acyl-carrier protein (ACPM) independently to complex I. The function of this duplicated protein interaction of ACPM with respiratory complex I is still unknown. Analysis of protein-protein interaction screens, genetic analyses and predicted multi-domain LYRMs offer further clues on an interaction network and adaptor-like function of LYR proteins in mitochondria.

【 授权许可】

CC BY   
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