Mitochondrial fatty acid synthesis, fatty acids and mitochondrial physiology

Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

Volumn 1862, Issue 1, 2017, Pages 39-48

  Kastaniotis, Alexander J ^a   Autio, Kaija J ^a   Kerätär, Juha M ^a   Monteuuis, Geoffray ^a   Mäkelä, Anne M ^a   Nair, Remya R ^a   Pietikäinen, Laura P ^a   Shvetsova, Antonina ^a   Chen, Zhijun ^b   Hiltunen, J Kalervo ^a,b  

^a UNIVERSITY OF OULU   (Finland)

^b Jilin University   (China)

Author keywords

Fatty acid synthesis; Lipids; Lipoic acid; Metabolic compartmentalization; Metabolic interaction; Pathways; Respiration; Thioesters

Indexed keywords

2 ENOYL ACYL CARRIER PROTEIN REDUCTASE; 3 HYDROXYACYL ACYL CARRIER PROTEIN DEHYDRATASE; 3 KETOACYL ACYL CARRIER PROTEIN SYNTHASE; 3 OXOACYL ACYL CARRIER PROTEIN REDUCTASE; ACETYL COENZYME A CARBOXYLASE; ACYL CARRIER PROTEIN; COENZYME A; FATTY ACID; GLYCINE CLEAVAGE SYSTEM PROTEIN H; LIPOIC ACID SYNTHETASE; LIPOYLTRANSFERASE 1; LIPOYLTRANSFERASE 2; MALONYL COA ACYL CARRIER PROTEIN TRANSFERASE; MALONYL COENZYME A SYNTHETASE; NFU1 IRON SULFUR CLUSTER SCAFFOLD; PHOSPHOPANTETHENYL ACYL CARRIER PROTEIN TRANSFERASE; THIOCTIC ACID; THIOESTER; UNCLASSIFIED DRUG;

CELL RESPIRATION; CYTOPLASM; EUKARYOTE; EUKARYOTIC CELL; FATTY ACID OXIDATION; FATTY ACID SYNTHESIS; HUMAN; INTRACELLULAR SPACE; LIPID METABOLISM; LIPOYLATION; METABOLIC DISORDER; MITOCHONDRIAL BIOGENESIS; MITOCHONDRIAL RESPIRATION; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; REVIEW; ANIMAL; LIPOGENESIS; METABOLISM; OXIDATION REDUCTION REACTION; PHYSIOLOGY;

ACYL CARRIER PROTEIN; ANIMALS; CELL RESPIRATION; FATTY ACIDS; HUMANS; LIPID METABOLISM; LIPOGENESIS; MITOCHONDRIA; OXIDATION-REDUCTION;

EID: 84997079783     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2016.08.011     Document Type: Review

References (124)

1. [1] Bhaumik, P., Koski, M.K., Glumoff, T., Hiltunen, J.K., Wierenga, R.K., Structural biology of the thioester-dependent degradation and synthesis of fatty acids. Curr. Opin. Struct. Biol. 15 (2005), 621–628.
2. [2] Mikolajczyk, S., Brody, S., De novo fatty acid synthesis mediated by acyl-carrier protein in Neurospora crassa mitochondria. Eur. J. Biochem. 187 (1990), 431–437.
3. [3] Brody, S., Oh, C., Hoja, U., Schweizer, E., Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae. FEBS Lett. 408 (1997), 217–220.
4. [4] Torkko, J.M., Koivuranta, K.T., Miinalainen, I.J., Yagi, A.I., Schmitz, W., Kastaniotis, A.J., Airenne, T.T., Gurvitz, A., Hiltunen, K.J., Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1′p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence. Mol. Cell. Biol. 21 (2001), 6243–6253.
5. [5] Hiltunen, J.K., Schonauer, M.S., Autio, K.J., Mittelmeier, T.M., Kastaniotis, A.J., Dieckmann, C.L., Mitochondrial fatty acid synthesis type II: more than just fatty acids. J. Biol. Chem. 284 (2009), 9011–9015.
6. [6] Smith, S., Witkowski, A., Moghul, A., Yoshinaga, Y., Nefedov, M., de Jong, P., Feng, D., Fong, L., Tu, Y., Hu, Y., Young, S.G., Pham, T., Cheung, C., Katzman, S.M., Brand, M.D., Quinlan, C.L., Fens, M., Kuypers, F., Misquitta, S., Griffey, S.M., Tran, S., Gharib, A., Knudsen, J., Hannibal-Bach, H.K., Wang, G., Larkin, S., Thweatt, J., Pasta, S., Compromised mitochondrial fatty acid synthesis in transgenic mice results in defective protein lipoylation and energy disequilibrium. PLoS One, 7, 2012, e47196.
7. [7] Brody, S., Mikolajczyk, S., Neurospora mitochondria contain an acyl-carrier protein. Eur. J. Biochem. 173 (1988), 353–359.
8. [8] White, S.W., Zheng, J., Zhang, Y.M., Rock, The structural biology of type II fatty acid biosynthesis. Annu. Rev. Biochem. 74 (2005), 791–831.
9. [9] Harington, A., Herbert, C.J., Tung, B., Getz, G.S., Slonimski, P.P., Identification of a new nuclear gene (CEM1) encoding a protein homologous to a beta-keto-acyl synthase which is essential for mitochondrial respiration in Saccharomyces cerevisiae. Mol. Microbiol. 9 (1993), 545–555.
10. [10] Schneider, R., Brors, B., Burger, F., Camrath, S., Weiss, H., Two genes of the putative mitochondrial fatty acid synthase in the genome of Saccharomyces cerevisiae. Curr. Genet. 32 (1997), 384–388.
11. [11] Christensen, C.E., Kragelund, B.B., von Wettstein-Knowles, P., Henriksen, A., Structure of the human beta-ketoacyl [ACP] synthase from the mitochondrial type II fatty acid synthase. Protein Sci. 16 (2007), 261–272.
12. [12] Hiltunen, J.K., Chen, Z., Haapalainen, A.M., Wierenga, R.K., Kastaniotis, A.J., Mitochondrial fatty acid synthesis—an adopted set of enzymes making a pathway of major importance for the cellular metabolism. Prog. Lipid Res. 49 (2010), 27–45.
13. [13] Funabashi, H., Kawaguchi, A., Tomoda, H., Omura, S., Okuda, S., Iwasaki, S., Binding site of cerulenin in fatty acid synthetase. J. Biochem. 105 (1989), 751–755.
14. [14] Zhang, L., Joshi, A.K., Hofmann, J., Schweizer, E., Smith, S., Cloning, expression, and characterization of the human mitochondrial beta-ketoacyl synthase. Complementation of the yeast CEM1 knock-out strain. J. Biol. Chem. 280 (2005), 12422–12429.
15. [15] Chen, C., Han, X., Zou, X., Li, Y., Yang, L., Cao, K., Xu, J., Long, J., Liu, J., Feng, Z., 4-Methylene-2-octyl-5-oxotetrahydrofuran-3-carboxylic acid (C75), an inhibitor of fatty-acid synthase, suppresses the mitochondrial fatty acid synthesis pathway and impairs mitochondrial function. J. Biol. Chem. 289 (2014), 17184–17194.
16. [16] Wang, J., Soisson, S.M., Young, K., Shoop, W., Kodali, S., Galgoci, A., Painter, R., Parthasarathy, G., Tang, Y.S., Cummings, R., Ha, S., Dorso, K., Motyl, M., Jayasuriya, H., Ondeyka, J., Herath, K., Zhang, C., Hernandez, L., Allocco, J., Basilio, A., Tormo, J.R., Genilloud, O., Vicente, F., Pelaez, F., Colwell, L., Lee, S.H., Michael, B., Felcetto, T., Gill, C., Silver, L.L., Hermes, J.D., Bartizal, K., Barrett, J., Schmatz, D., Becker, J.W., Cully, D., Singh, S.B., Platensimycin is a selective FabF inhibitor with potent antibiotic properties. Nature 441 (2006), 358–361.
17. [17] Jackowski, S., Murphy, C.M., Cronan, J.E. Jr., Rock, C.O., Acetoacetyl-acyl carrier protein synthase. A target for the antibiotic thiolactomycin. J. Biol. Chem. 264 (1989), 7624–7629.
18. [18] Runswick, M.J., Fearnley, I.M., Skehel, J.M., Walker, J.E., Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett. 286 (1991), 121–124.
19. [19] Sackmann, U., Zensen, R., Rohlen, D., Jahnke, U., Weiss, H., The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH:ubiquinone reductase (complex I). Eur. J. Biochem. 200 (1991), 463–469.
20. [20] Zensen, R., Husmann, H., Schneider, R., Peine, T., Weiss, H., De novo synthesis and desaturation of fatty acids at the mitochondrial acyl-carrier protein, a subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa. FEBS Lett. 310 (1992), 179–181.
21. [21] Dobrynin, K., Abdrakhmanova, A., Richers, S., Hunte, C., Kerscher, S., Brandt, U., Characterization of two different acyl carrier proteins in complex I from Yarrowia lipolytica. Biochim. Biophys. Acta 1797 (2010), 152–159.
22. [22] Meyer, E.H., Heazlewood, J.L., Millar, A.H., Mitochondrial acyl carrier proteins in Arabidopsis thaliana are predominantly soluble matrix proteins and none can be confirmed as subunits of respiratory complex I. Plant Mol. Biol. 64 (2007), 319–327.
23. [23] Stuible, H.P., Meier, S., Wagner, C., Hannappel, E., Schweizer, E., A novel phosphopantetheine:protein transferase activating yeast mitochondrial acyl carrier protein. J. Biol. Chem. 273 (1998), 22334–22339.
24. [24] Joshi, A.K., Zhang, L., Rangan, V.S., Smith, S., Cloning, expression, and characterization of a human 4′-phosphopantetheinyl transferase with broad substrate specificity. J. Biol. Chem. 278 (2003), 33142–33149.
25. [25] Hoja, U., Marthol, S., Hofmann, J., Stegner, S., Schulz, R., Meier, S., Greiner, E., Schweizer, E., HFA1 encoding an organelle-specific acetyl-CoA carboxylase controls mitochondrial fatty acid synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004), 21779–21786.
26. [26] Wolfe, K.H., Shields, D.C., Molecular evidence for an ancient duplication of the entire yeast genome. Nature 387 (1997), 708–713.
27. [27] Kellis, M., Birren, B.W., Lander, E.S., Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae. Nature 428 (2004), 617–624.
28. [28] Suomi, F., Menger, K.E., Monteuuis, G., Naumann, U., Kursu, V.A., Shvetsova, A., Kastaniotis, A.J., Expression and evolution of the non-canonically translated yeast mitochondrial acetyl-CoA carboxylase Hfa1p. PLoS One, 9, 2014, e114738.
29. [29] Zitomer, R.S., Walthall, D.A., Rymond, B.C., Hollenberg, C.P., Saccharomyces cerevisiae ribosomes recognize non-AUG initiation codons. Mol. Cell. Biol. 4 (1984), 1191–1197.
30. [30] Natsoulis, G., Hilger, F., Fink, G.R., The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine tRNA synthetases of S. cerevisiae. Cell 46 (1986), 235–243.
31. [31] Chatton, B., Walter, P., Ebel, J.P., Lacroute, F., Fasiolo, F., The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases. J. Biol. Chem. 263 (1988), 52–57.
32. [32] Tang, H.L., Yeh, L.S., Chen, N.K., Ripmaster, T., Schimmel, P., Wang, C.C., Translation of a yeast mitochondrial tRNA synthetase initiated at redundant non-AUG codons. J. Biol. Chem. 279 (2004), 49656–49663.
33. [33] Chang, K.J., Wang, C.C., Translation initiation from a naturally occurring non-AUG codon in Saccharomyces cerevisiae. J. Biol. Chem. 279 (2004), 13778–13785.
34. [34] Turunen, O., Seelke, R., Macosko, J., In silico evidence for functional specialization after genome duplication in yeast. FEMS Yeast Res. 9 (2009), 16–31.
35. [35] Scholte, H.R., Luyt-Houwen, I.E., Dubelaar, M.L., Hulsmann, W.C., The source of malonyl-CoA in rat heart. The calcium paradox releases acetyl-CoA carboxylase and not propionyl-CoA carboxylase. FEBS Lett. 198 (1986), 47–50.
36. [36] Witkowski, A., Thweatt, J., Smith, S., Mammalian ACSF3 protein is a malonyl-CoA synthetase that supplies the chain extender units for mitochondrial fatty acid synthesis. J. Biol. Chem. 286 (2011), 33729–33736.
37. [37] Bieber, L.L., Carnitine. Annu. Rev. Biochem. 57 (1988), 261–283.
38. [38] Guan, X., Nikolau, B.J., AAE13 encodes a dual-localized malonyl-CoA synthetase that is crucial for mitochondrial fatty acid biosynthesis. Plant J. 85 (2016), 581–593.
39. [39] Feng, D., Witkowski, A., Smith, S., Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death. J. Biol. Chem. 284 (2009), 11436–11445.
40. [40] Heazlewood, J.L., Howell, K.A., Whelan, J., Millar, A.H., Towards an analysis of the rice mitochondrial proteome. Plant Physiol. 132 (2003), 230–242.
41. [41] Focke, M., Gieringer, E., Schwan, S., Jansch, L., Binder, S., Braun, H.P., Fatty acid biosynthesis in mitochondria of grasses: malonyl-coenzyme A is generated by a mitochondrial-localized acetyl-coenzyme A carboxylase. Plant Physiol. 133 (2003), 875–884.
42. [42] Chen, Z., Kastaniotis, A.J., Miinalainen, I.J., Rajaram, V., Wierenga, R.K., Hiltunen, J.K., 17beta-hydroxysteroid dehydrogenase type 8 and carbonyl reductase type 4 assemble as a ketoacyl reductase of human mitochondrial FAS. FASEB J. 23 (2009), 3682–3691.
43. [43] Venkatesan, R., Sah-Teli, S.K., Awoniyi, L.O., Jiang, G., Prus, P., Kastaniotis, A.J., Hiltunen, J.K., Wierenga, R.K., Chen, Z., Insights into mitochondrial fatty acid synthesis from the structure of heterotetrameric 3-ketoacyl-ACP reductase/3R-hydroxyacyl-CoA dehydrogenase. Nat. Commun., 5, 2014, 4805.
44. [44] Kastaniotis, A.J., Autio, K.J., Sormunen, R.T., Hiltunen, J.K., Htd2p/Yhr067p is a yeast 3-hydroxyacyl-ACP dehydratase essential for mitochondrial function and morphology. Mol. Microbiol. 53 (2004), 1407–1421.
45. [45] Autio, K.J., Kastaniotis, A.J., Pospiech, H., Miinalainen, I.J., Schonauer, M.S., Dieckmann, C.L., Hiltunen, J.K., An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing. FASEB J. 22 (2008), 569–578.
46. [46] Andreev, D.E., O'Connor, P.B., Zhdanov, A.V., Dmitriev, R.I., Shatsky, I.N., Papkovsky, D.B., Baranov, P.V., Oxygen and glucose deprivation induces widespread alterations in mRNA translation within 20 minutes. Genome Biol., 16, 2015 (90–015-0651-z).
47. [47] Autio, K.J., Guler, J.L., Kastaniotis, A.J., Englund, P.T., Hiltunen, J.K., The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei. FEBS Lett. 582 (2008), 729–733.
48. [48] Stephens, J.L., Lee, S.H., Paul, K.S., Englund, P.T., Mitochondrial fatty acid synthesis in Trypanosoma brucei. J. Biol. Chem. 282 (2007), 4427–4436.
49. [49] Mouilleron, H., Delcourt, V., Roucou, X., Death of a dogma: eukaryotic mRNAs can code for more than one protein. Nucleic Acids Res. 44 (2016), 14–23.
50. [50] Airenne, T.T., Torkko, J.M., Van den plas, S., Sormunen, R.T., Kastaniotis, A.J., Wierenga, R.K., Hiltunen, J.K., Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance. J. Mol. Biol. 327 (2003), 47–59.
51. [51] Miinalainen, I.J., Chen, Z.J., Torkko, J.M., Pirila, P.L., Sormunen, R.T., Bergmann, U., Qin, Y.M., Hiltunen, J.K., Characterization of 2-enoyl thioester reductase from mammals. An ortholog of YBR026p/MRF1'p of the yeast mitochondrial fatty acid synthesis type II. J. Biol. Chem. 278 (2003), 20154–20161.
52. [52] Torkko, J.M., Koivuranta, K.T., Kastaniotis, A.J., Airenne, T.T., Glumoff, T., Ilves, M., Hartig, A., Gurvitz, A., Hiltunen, J.K., Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers. J. Biol. Chem. 278 (2003), 41213–41220.
53. [53] Jornvall, H., Hedlund, J., Bergman, T., Oppermann, U., Persson, B., Superfamilies SDR and MDR: from early ancestry to present forms. Emergence of three lines, a Zn-metalloenzyme, and distinct variabilities. Biochem. Biophys. Res. Commun. 396 (2010), 125–130.
54. [54] Persson, B., Hedlund, J., Jornvall, H., Medium- and short-chain dehydrogenase/reductase gene and protein families : the MDR superfamily. Cell. Mol. Life Sci. 65 (2008), 3879–3894.
55. [55] Clay, H.B., Parl, A.K., Mitchell, S.L., Singh, L., Bell, L.N., Murdock, D.G., Altering the mitochondrial fatty acid synthesis (mtFASII) pathway modulates cellular metabolic states and bioactive lipid profiles as revealed by metabolomic profiling. PLoS One, 11, 2016, e0151171.
56. [56] Wada, H., Shintani, D., Ohlrogge, J., Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production. Proc. Natl. Acad. Sci. U. S. A. 94 (1997), 1591–1596.
57. [57] Perham, R.N., Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000), 961–1004.
58. [58] Cronan, J.E., Assembly of lipoic acid on its cognate enzymes: an extraordinary and essential biosynthetic pathway. Microbiol. Mol. Biol. Rev. 80 (2016), 429–450.
59. [59] Sulo, P., Martin, N.C., Isolation and characterization of LIP5. A lipoate biosynthetic locus of Saccharomyces cerevisiae. J. Biol. Chem. 268 (1993), 17634–17639.
60. [60] Biewenga, G.P., Haenen, G.R., Bast, A., The pharmacology of the antioxidant lipoic acid. Gen. Pharmacol. 29 (1997), 315–331.
61. [61] Bustamante, J., Lodge, J.K., Marcocci, L., Tritschler, H.J., Packer, L., Rihn, B.H., Alpha-lipoic acid in liver metabolism and disease. Free Radic. Biol. Med. 24 (1998), 1023–1039.
62. [62] Shay, K.P., Moreau, R.F., Smith, E.J., Smith, A.R., Hagen, T.M., Alpha-lipoic acid as a dietary supplement: molecular mechanisms and therapeutic potential. Biochim. Biophys. Acta 1790 (2009), 1149–1160.
63. [63] Goraca, A., Huk-Kolega, H., Piechota, A., Kleniewska, P., Ciejka, E., Skibska, B., Lipoic acid - biological activity and therapeutic potential. Pharmacol. Rep. 63 (2011), 849–858.
64. [64] Park, S., Karunakaran, U., Jeoung, N.H., Jeon, J.H., Lee, I.K., Physiological effect and therapeutic application of alpha lipoic acid. Curr. Med. Chem. 21 (2014), 3636–3645.
65. [65] Gomes, M.B., Negrato, C.A., Alpha-lipoic acid as a pleiotropic compound with potential therapeutic use in diabetes and other chronic diseases. Diabetol. Metab. Syndr., 6, 2014 (80–5996–6-80. eCollection 2014).
66. [66] Jiang, D.Q., Li, M.X., Ma, Y.J., Wang, Y., Wang, Y., Efficacy and safety of prostaglandin E1 plus lipoic acid combination therapy versus monotherapy for patients with diabetic peripheral neuropathy. J. Clin. Neurosci. 27 (2016), 8–16.
67. [67] Huerta, A.E., Prieto-Hontoria, P.L., Sainz, N., Martinez, J.A., Moreno-Aliaga, M.J., Supplementation with alpha-lipoic acid alone or in combination with eicosapentaenoic acid modulates the inflammatory status of healthy overweight or obese women consuming an energy-restricted diet. J. Nutr., 2016.
68. [68] Morikawa, T., Yasuno, R., Wada, H., Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria. FEBS Lett. 498 (2001), 16–21.
69. [69] Yi, X., Maeda, N., Endogenous production of lipoic acid is essential for mouse development. Mol. Cell. Biol. 25 (2005), 8387–8392.
70. [70] Padmalayam, I., Hasham, S., Saxena, U., Pillarisetti, S., Lipoic acid synthase (LASY): a novel role in inflammation, mitochondrial function, and insulin resistance. Diabetes 58 (2009), 600–608.
71. [71] Marvin, M.E., Williams, P.H., Cashmore, A.M., The isolation and characterisation of a Saccharomyces cerevisiae gene (LIP2) involved in the attachment of lipoic acid groups to mitochondrial enzymes. FEMS Microbiol. Lett. 199 (2001), 131–136.
72. [72] Schonauer, M.S., Kastaniotis, A.J., Kursu, V.A., Hiltunen, J.K., Dieckmann, C.L., Lipoic acid synthesis and attachment in yeast mitochondria. J. Biol. Chem. 284 (2009), 23234–23242.
73. [73] Fujiwara, K., Okamura-Ikeda, K., Motokawa, Y., Cloning and expression of a cDNA encoding bovine lipoyltransferase. J. Biol. Chem. 272 (1997), 31974–31978.
74. [74] Fujiwara, K., Suzuki, M., Okumachi, Y., Okamura-Ikeda, K., Fujiwara, T., Takahashi, E., Motokawa, Y., Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene. Eur. J. Biochem. 260 (1999), 761–767.
75. [75] Fujiwara, K., Hosaka, H., Matsuda, M., Okamura-Ikeda, K., Motokawa, Y., Suzuki, M., Nakagawa, A., Taniguchi, H., Crystal structure of bovine lipoyltransferase in complex with lipoyl-AMP. J. Mol. Biol. 371 (2007), 222–234.
76. [76] Hendrickson, S.L., Lautenberger, J.A., Chinn, L.W., Malasky, M., Sezgin, E., Kingsley, L.A., Goedert, J.J., Kirk, G.D., Gomperts, E.D., Buchbinder, S.P., Troyer, J.L., O'Brien, S.J., Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression. PLoS One, 5, 2010, e12862.
77. [77] Green, D.E., Morris, T.W., Green, J., Cronan, J.E. Jr., Guest, J.R., Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem. J. 309:Pt 3 (1995), 853–862.
78. [78] Fujiwara, K., Takeuchi, S., Okamura-Ikeda, K., Motokawa, Y., Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver. J. Biol. Chem. 276 (2001), 28819–28823.
79. [79] Hermes, F.A., Cronan, J.E., The role of the Saccharomyces cerevisiae lipoate protein ligase homologue, Lip3, in lipoic acid synthesis. Yeast 30 (2013), 415–427.
80. [80] Christensen, Q.H., Martin, N., Mansilla, M.C., de Mendoza, D., Cronan, J.E., A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis. Mol. Microbiol. 80 (2011), 350–363.
81. [81] Kursu, V.A., Pietikainen, L.P., Fontanesi, F., Aaltonen, M.J., Suomi, F., Raghavan Nair, R., Schonauer, M.S., Dieckmann, C.L., Barrientos, A., Hiltunen, J.K., Kastaniotis, A.J., Defects in mitochondrial fatty acid synthesis result in failure of multiple aspects of mitochondrial biogenesis in Saccharomyces cerevisiae. Mol. Microbiol. 90 (2013), 824–840.
82. [82] Harington, A., Schwarz, E., Slonimski, P.P., Herbert, C.J., Subcellular relocalization of a long-chain fatty acid CoA ligase by a suppressor mutation alleviates a respiration deficiency in Saccharomyces cerevisiae. EMBO J. 13 (1994), 5531–5538.
83. [83] Fontanesi, F., Soto, I.C., Horn, D., Barrientos, A., Mss51 and Ssc1 facilitate translational regulation of cytochrome c oxidase biogenesis. Mol. Cell. Biol. 30 (2010), 245–259.
84. [84] Herzig, S., Raemy, E., Montessuit, S., Veuthey, J.L., Zamboni, N., Westermann, B., Kunji, E.R., Martinou, J.C., Identification and functional expression of the mitochondrial pyruvate carrier. Science 337 (2012), 93–96.
85. [85] Carroll, J., Fearnley, I.M., Shannon, R.J., Hirst, J., Walker, J.E., Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell. Proteomics 2 (2003), 117–126.
86. [86] Hirst, J., Carroll, J., Fearnley, I.M., Shannon, R.J., Walker, J.E., The nuclear encoded subunits of complex I from bovine heart mitochondria. Biochim. Biophys. Acta 1604 (2003), 135–150.
87. [87] Vinothkumar, K.R., Zhu, J., Hirst, J., Architecture of mammalian respiratory complex I. Nature 515 (2014), 80–84.
88. [88] Mayr, J.A., Zimmermann, F.A., Fauth, C., Bergheim, C., Meierhofer, D., Radmayr, D., Zschocke, J., Koch, J., Sperl, W., Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation. Am. J. Hum. Genet. 89 (2011), 792–797.
89. [89] Ajit Bolar, N., Vanlander, A.V., Wilbrecht, C., Van der Aa, N., Smet, J., De Paepe, B., Vandeweyer, G., Kooy, F., Eyskens, F., De Latter, E., Delanghe, G., Govaert, P., Leroy, J.G., Loeys, B., Lill, R., Van Laer, L., Van Coster, R., Mutation of the iron-sulfur cluster assembly gene IBA57 causes severe myopathy and encephalopathy. Hum. Mol. Genet. 22 (2013), 2590–2602.
90. [90] Mayr, J.A., Feichtinger, R.G., Tort, F., Ribes, A., Sperl, W., Lipoic acid biosynthesis defects. J. Inherit. Metab. Dis. 37 (2014), 553–563.
91. [91] Tsurusaki, Y., Tanaka, R., Shimada, S., Shimojima, K., Shiina, M., Nakashima, M., Saitsu, H., Miyake, N., Ogata, K., Yamamoto, T., Matsumoto, N., Novel compound heterozygous LIAS mutations cause glycine encephalopathy. J. Hum. Genet. 60 (2015), 631–635.
92. [92] Soreze, Y., Boutron, A., Habarou, F., Barnerias, C., Nonnenmacher, L., Delpech, H., Mamoune, A., Chretien, D., Hubert, L., Bole-Feysot, C., Nitschke, P., Correia, I., Sardet, C., Boddaert, N., Hamel, Y., Delahodde, A., Ottolenghi, C., de Lonlay, P., Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase. Orphanet J. Rare Dis., 8, 2013 (192–1172–8-192).
93. [93] Tort, F., Ferrer-Cortes, X., Thio, M., Navarro-Sastre, A., Matalonga, L., Quintana, E., Bujan, N., Arias, A., Garcia-Villoria, J., Acquaviva, C., Vianey-Saban, C., Artuch, R., Garcia-Cazorla, A., Briones, P., Ribes, A., Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes. Hum. Mol. Genet. 23 (2014), 1907–1915.
94. [94] Tache, V., Bivina, L., White, S., Gregg, J., Deignan, J., Boyadjievd, S.A., Poulain, F.R., Lipoyltransferase 1 gene defect resulting in fatal lactic acidosis in two siblings. Case Rep. Obstet. Gynecol., 2016, 2016, 6520148.
95. [95] Cameron, J.M., Janer, A., Levandovskiy, V., Mackay, N., Rouault, T.A., Tong, W.H., Ogilvie, I., Shoubridge, E.A., Robinson, B.H., Mutations in iron-sulfur cluster scaffold genes NFU1 and BOLA3 cause a fatal deficiency of multiple respiratory chain and 2-oxoacid dehydrogenase enzymes. Am. J. Hum. Genet. 89 (2011), 486–495.
96. [96] Baker, P.R. II, Friederich, M.W., Swanson, M.A., Shaikh, T., Bhattacharya, K., Scharer, G.H., Aicher, J., Creadon-Swindell, G., Geiger, E., MacLean, K.N., Lee, W.T., Deshpande, C., Freckmann, M.L., Shih, L.Y., Wasserstein, M., Rasmussen, M.B., Lund, A.M., Procopis, P., Cameron, J.M., Robinson, B.H., Brown, G.K., Brown, R.M., Compton, A.G., Dieckmann, C.L., Collard, R., Coughlin, C.R. II, Spector, E., Wempe, M.F., Van Hove, J.L., Variant non ketotic hyperglycinemia is caused by mutations in LIAS, BOLA3 and the novel gene GLRX5. Brain 137 (2014), 366–379.
97. [97] Navarro-Sastre, A., Tort, F., Stehling, O., Uzarska, M.A., Arranz, J.A., Del Toro, M., Labayru, M.T., Landa, J., Font, A., Garcia-Villoria, J., Merinero, B., Ugarte, M., Gutierrez-Solana, L.G., Campistol, J., Garcia-Cazorla, A., Vaquerizo, J., Riudor, E., Briones, P., Elpeleg, O., Ribes, A., Lill, R., A fatal mitochondrial disease is associated with defective NFU1 function in the maturation of a subset of mitochondrial Fe-S proteins. Am. J. Hum. Genet. 89 (2011), 656–667.
98. [98] Shen, Y.Q., Burger, G., Plasticity of a key metabolic pathway in fungi. Funct. Integr. Genomics 9 (2009), 145–151.
99. [99] Patkar, R.N., Ramos-Pamplona, M., Gupta, A.P., Fan, Y., Naqvi, N.I., Mitochondrial beta-oxidation regulates organellar integrity and is necessary for conidial germination and invasive growth in Magnaporthe oryzae. Mol. Microbiol. 86 (2012), 1345–1363.
100. [100] Jackson, J.B., Proton translocation by transhydrogenase. FEBS Lett. 545 (2003), 18–24.
101. [101] Yang, H., Yang, T., Baur, J.A., Perez, E., Matsui, T., Carmona, J.J., Lamming, D.W., Souza-Pinto, N.C., Bohr, V.A., Rosenzweig, A., de Cabo, R., Sauve, A.A., Sinclair, D.A., Nutrient-sensitive mitochondrial NAD + levels dictate cell survival. Cell 130 (2007), 1095–1107.
102. [102] Mailloux, R.J., Harper, M.E., Glucose regulates enzymatic sources of mitochondrial NADPH in skeletal muscle cells; a novel role for glucose-6-phosphate dehydrogenase. FASEB J. 24 (2010), 2495–2506.
103. [103] Hiltunen, J.K., Qin, Y., Beta-oxidation - strategies for the metabolism of a wide variety of acyl-CoA esters. Biochim. Biophys. Acta 1484 (2000), 117–128.
104. [104] STERN, J.R., DEL CAMPILLO, A., Enzymes of fatty acid metabolism. II. Properties of crystalline crotonase. J. Biol. Chem. 218 (1956), 985–1002.
105. [105] Chen, Z., Leskinen, H., Liimatta, E., Sormunen, R.T., Miinalainen, I.J., Hassinen, I.E., Hiltunen, J.K., Myocardial overexpression of Mecr, a gene of mitochondrial FAS II leads to cardiac dysfunction in mouse. PLoS One, 4, 2009, e5589.
106. [106] Schonauer, M.S., Kastaniotis, A.J., Hiltunen, J.K., Dieckmann, C.L., Intersection of RNA processing and the type II fatty acid synthesis pathway in yeast mitochondria. Mol. Cell. Biol. 28 (2008), 6646–6657.
107. [107] Schneider, R., Massow, M., Lisowsky, T., Weiss, H., Different respiratory-defective phenotypes of Neurospora crassa and Saccharomyces cerevisiae after inactivation of the gene encoding the mitochondrial acyl carrier protein. Curr. Genet. 29 (1995), 10–17.
108. [108] Parl, A., Mitchell, S.L., Clay, H.B., Reiss, S., Li, Z., Murdock, D.G., The mitochondrial fatty acid synthesis (mtFASII) pathway is capable of mediating nuclear-mitochondrial cross talk through the PPAR system of transcriptional activation. Biochem. Biophys. Res. Commun. 441 (2013), 418–424.
109. [109] Kim, D.G., Yoo, J.C., Kim, E., Lee, Y.S., Yarishkin, O.V., da Lee, Y., Lee, K.H., Hong, S.G., Hwang, E.M., Park, J.Y., A novel cytosolic isoform of mitochondrial trans-2-enoyl-CoA reductase enhances peroxisome proliferator-activated receptor alpha activity. Endocrinol. Metab. (Seoul) 29 (2014), 185–194.
110. [110] Masuda, N., Yasumo, H., Furusawa, T., Tsukamoto, T., Sadano, H., Osumi, T., Nuclear receptor binding factor-1 (NRBF-1), a protein interacting with a wide spectrum of nuclear hormone receptors. Gene 221 (1998), 225–233.
111. [111] Yamazoe, M., Shirahige, K., Rashid, M.B., Kaneko, Y., Nakayama, T., Ogasawara, N., Yoshikawa, H., A protein which binds preferentially to single-stranded core sequence of autonomously replicating sequence is essential for respiratory function in mitochondrial of Saccharomyces cerevisiae. J. Biol. Chem. 269 (1994), 15244–15252.
112. [112] Doulias, P.T., Tenopoulou, M., Greene, J.L., Raju, K., Ischiropoulos, H., Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation. Sci. Signal., 6, 2013 (rs1).
113. [113] Gurvitz, A., Triclosan inhibition of mycobacterial InhA in Saccharomyces cerevisiae: yeast mitochondria as a novel platform for in vivo antimycolate assays. Lett. Appl. Microbiol. 50 (2010), 399–405.
114. [114] Cicchillo, R.M., Booker, S.J., Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J. Am. Chem. Soc. 127 (2005), 2860–2861.
115. [115] Praphanphoj, V., Sacksteder, K.A., Gould, S.J., Thomas, G.H., Geraghty, M.T., Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene. Mol. Genet. Metab. 72 (2001), 336–342.
116. [116] Zhang, L., Joshi, A.K., Smith, S., Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein. J. Biol. Chem. 278 (2003), 40067–40074.
117. [117] Chen, Z.J., Pudas, R., Sharma, S., Smart, O.S., Juffer, A.H., Hiltunen, J.K., Wierenga, R.K., Haapalainen, A.M., Structural enzymological studies of 2-enoyl thioester reductase of the human mitochondrial FAS II pathway: new insights into its substrate recognition properties. J. Mol. Biol. 379 (2008), 830–844.
118. [118] Nagarajan, L., Storms, R.K., Molecular characterization of GCV3, the Saccharomyces cerevisiae gene coding for the glycine cleavage system hydrogen carrier protein. J. Biol. Chem. 272 (1997), 4444–4450.
119. [119] Zay, A., Choy, F.Y., Patrick, C., Sinclair, G., Glycine cleavage enzyme complex: molecular cloning and expression of the H-protein cDNA from cultured human skin fibroblasts. Biochem. Cell Biol. 89 (2011), 299–307.
120. [120] Schilke, B., Voisine, C., Beinert, H., Craig, E., Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 10206–10211.
121. [121] Liu, Y., Qi, W., Cowan, J.A., Iron-sulfur cluster biosynthesis: functional characterization of the N- and C-terminal domains of human NFU. Biochemistry 48 (2009), 973–980.
122. [122] Liu, Y., Cowan, J.A., Iron-sulfur cluster biosynthesis: characterization of a molten globule domain in human NFU. Biochemistry 48 (2009), 7512–7518.
123. [123] Wang, Y., Mohsen, A.W., Mihalik, S.J., Goetzman, E.S., Vockley, J., Evidence for physical association of mitochondrial fatty acid oxidation and oxidative phosphorylation complexes. J. Biol. Chem. 285 (2010), 29834–29841.
124. [124] Goetzman, E.S., Modeling disorders of fatty acid metabolism in the mouse. Prog. Mol. Biol. Transl. Sci. 100 (2011), 389–417.