Abstract
Since the early studies on the resolution and reconstitution of the oxidative phosphorylation system from animal mitochondria, coupling factor B was recognized as an essential component of the machinery responsible for energy-driven ATP synthesis. At the phenomenological level, factor B was agreed to lie at the interface of energy transfer between the respiratory chain and the ATP synthase complex. However, biochemical characterization of the factor B polypeptide has proved difficult. It was not until 1990 that the N-terminal amino acid sequence of bovine mitochondrial factor B was reported, which followed, a decade later, by the report describing the amino acid sequence of full-length human factor B and its functional characterization. The present review summarizes the recent advances in structure-functional studies of factor B, including its recently determined crystal structure at 0.96 Å resolution. Ectopic expression of human factor B in cultured animal cells has unexpectedly revealed its role in shaping mitochondrial morphology. The supramolecular assembly of ATP synthase as dimer ribbons at highly curved apices of the mitochondrial cristae was recently suggested to optimize ATP synthesis under proton-limited conditions. We propose that the binding of the ATP synthase dimers with factor B tetramers could be a means to enhance the efficiency of the terminal step of oxidative phosphorylation in animal mitochondria.
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Angevine CM, Herold KA, Vincent OD, Fillingame RH (2007) J Biol Chem 282:9001–9007
Arnold I, Pfeiffer K, Neupert W, Stuart RA, Schägger H (1998) EMBO J 17:7170–7178
Arselin G, Vaillier J, Salin B, Schaeffer J, Giraud MF, Dautant A, Brethes D, Velours J (2004) J Biol Chem 279:40392–40399
Belogrudov GI (2002) Arch Biochem Biophys 406:271–274
Belogrudov GI (2006) Arch Biochem Biophys 451:68–78
Belogrudov GI (2007) Arch Biochem Biophys 461:95–103
Belogrudov GI (2008) Arch Biochem Biophys 473:76–87
Belogrudov GI, Hatefi Y (2002) J Biol Chem 277:6097–6103
Belogrudov GI, Tomich JM, Hatefi Y (1996) J Biol Chem 271:20340–20345
Belogrudov GI, Schirf V, Demeler B (2006) Biochim Biophys Acta 1764:1741–1749
Bindoli A, Fukuto JM, Forman HJ (2008) Antioxid Redox Signal 10:1549–1564
Bisetto E, Picotti P, Giorgio V, Alverdi V, Mavelli I, Lippe G (2008) J Bioenerg Biomembr 40:257–267
Branden M, Sanden T, Brzezinski P, Widengren J (2006) Proc Natl Acad Sci USA 103:19766–19770
Chan DC (2006) Annu Rev Cell Dev Biol 22:79–99
Collinson IR, Runswick MJ, Buchanan SK, Fearnley IM, Skehel JM, van Raaij MJ, Griffiths DE, Walker JE (1994) Biochemistry 33:7971–7978
Collinson IR, Skehel JM, Fearnley IM, Runswick MJ, Walker JE (1996) Biochemistry 35:12640–12646
Ernster L, Hundal T, Sandri G (1986) Methods Enzymol 126:428–433
Fernandez-Moran H, Oda T, Blair PV, Green DE (1964) J Cell Biol 22:63–100
Fillingame RH, Angevine CM, Dmitriev OY (2003) FEBS Lett 555:29–34
Frey TG, Mannella CA (2000) Trends Biochem Sci 25:319–324
Frey TG, Perkins GA, Ellisman MH (2006) Annu Rev Biophys Biomol Struct 35:199–224
Fuller N, Rand RP (2001) Biophys J 81:243–254
Hatefi Y (1993) Eur J Biochem 218:759–767
Hatefi Y, Lester RL (1958) Biochim Biophys Acta 27:83–88
Hong S, Pedersen PL (2004) J Bioenerg Biomembr 36:515–523
Hughes J, Joshi S, Murfitt RR, Sanadi DR (1979) In: Lee CP, Schatz G, Ernster L (eds) Membrane bioenergetics. Addison-Wesley, Boston, pp 81–95
Hughes J, Joshi S, Torok K, Sanadi DR (1982) J Bioenerg Biomembr 14:287–295
Jacobs EE, Jacob M, Sanadi DR, Bradley L (1956) J Biol Chem 223:147–156
Kantham L, Raychowdhury R, Ogata KK, Javed A, Rice J, Sanadi DR (1990) FEBS Lett. 277:105–108
Kobe B, Kajava AV (2001) Curr Opin Struct Biol 11:725–732
Lam KW, Warshaw JB, Sanadi DR (1967) Arch Biochem Biophys 119:477–484
Lee CP (1979) Methods Enzymol 55:105–112
Lee CP, Ernster L (1965) Biochem Biophys Res Commun 18:523–529
Lee JK, Belogrudov GI, Stroud RM (2008) Proc Natl Acad Sci USA 105:13379–13384
Lutter R, Saraste M, van Walraven HS, Runswick MJ, Finel M, Deatherage JF, Walker JE (1993) Biochem J 295:799–806
Mannella CA (2006) Biochim Biophys Acta 1763:542–548
McMahon HT, Gallop JL (2005) Nature 438:590–596
Meyer B, Wittig I, Trifilieff E, Karas M, Schägger H (2007) Mol Cell Proteomics 6:1690–1699
Minauro-Sanmiguel F, Wilkens S, García JJ (2005) Proc Natl Acad Sci USA 102:12356–12358
Mulkidjanian AY, Heberle J, Cherepanov DA (2006) Biochim Biophys Acta 1757:913–930
Pagliarini DJ, Calvo SE, Chang B, Sheth SA, Vafai SB, Ong SE, Walford GA, Sugiana C, Boneh A, Chen WK, Hill DE, Vidal M, Evans JG, Thorburn DR, Carr SA, Mootha VK (2008) Cell 134:112–123
Sanadi DR (1982) Biochim Biophys Acta 683:39–56
Sanadi DR, Joshi S (1979) Methods Enzymol 55:380–383
Shankaran R, Sani BP, Sanadi DR (1975) Arch Biochem Biophys 168:394–402
Stiggall DL, Galante YM, Kiehl R, Hatefi Y (1979) Arch Biochem Biophys 196:638–644
Strauss M, Hofhaus G, Schroder RR, Kuhlbrandt W (2008) EMBO J 27:1154–1160
Stuart RA (2008) J Bioenerg Biomembr 40:411–417
Vik SB, Long JC, Wada T, Zhang D (2000) Biochim Biophys Acta 1458:457–466
Walker JE, Lutter R, Dupuis A, Runswick MJ (1991) Biochemistry 30:5369–5378
You KS, Hatefi Y (1976) Biochim Biophys Acta 423:398–412
Youle RJ, Karbowski M (2005) Nat Rev Mol Cell Biol 6:657–663
Zhang J, Li X, Mueller M, Wang Y, Zong C, Deng N, Vondriska TM, Liem DA, Yang JI, Korge P, Honda H, Weiss JN, Apweiler R, Ping P (2008) Proteomics 8:1564–1575
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Belogrudov, G.I. Recent advances in stucture-functional studies of mitochondrial factor B. J Bioenerg Biomembr 41, 137–143 (2009). https://doi.org/10.1007/s10863-009-9210-1
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DOI: https://doi.org/10.1007/s10863-009-9210-1