Summary
A concise overview of the chloroplast ATP synthase is presented, with an emphasis on its functions, regulation, composition, and structure from fluorescence energy transfer mapping. The ATP synthase may be separated into two parts: coupling factor 1 (CF1) and CF0•CF1 is a large hydrophilic protein that contains the catalytic sites of the synthase. The functions of its five different polypeptides are briefly discussed. CF0 binds CF1 and functions to conduct protons across the thylakoid membrane. Because CF0 will not be considered in detail in subsequent chapters, the composition of CFα and some of its interactions with CF1 are discussed. Insights into the structure and function of CF1 as well as into subunit interactions, gleaned by structural mapping by fluorescence resonance energy transfer, are presented.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abrahams JP, Leslie AGW, Lotter R and Walker JE (1994) Structure at 2.8Å resolution of F1-ATPase from bovine heart mitochondria. Nature 230: 621–628
Avron M (1978) Energy transduction in photosynthesis. FEBS Lett 96: 225–232
Avron M and Jagendorf AT (1959) Evidence concerning the mechanism of adenosine triphosphate formation by spinach chloroplasts. J Biol Chem 234: 967–972
Binder A, Jagendorf AT and Ngo E (1978) Isolation and composition of the subunits of spinach coupling factor protein. J Biol Chem 253: 3094–3100
Boekema EJ, Xiao J and McCarty RE (1990) Structure of the ATP synthase from chloroplasts studied by electron microscopy: Location of the small subunits. Biochim Biophys Acta 1020: 49–56
Boyer PD (1989) A perspective of the binding change mechanism for ATP synthesis. FASEB J 3: 2164–2178
Cozens AL and Walker JE (1987) The organization and sequence of the genes for ATP synthase subunits in the cyanobacterium Synechococcus 6301. Support for an endosymbiotic origin of chloroplasts. J Mol Biol 194: 359–383
Curtis SE (1988) Structure, organization and expression of cyanobacterial ATP synthase genes. Photosynth Res 18: 223–244
Dann MS and McCarty RE (1992) Characterization of the activation of membrane-bound and soluble CF1 by thioredoxin. Plant Physiol 99: 153–160
Davenport JW and McCarty RE (1981) Quantitative aspects of adenosine triphosphate-driven proton translocation in spinach chloroplast thylakoids. J Biol Chem 256: 8947–8954
Davenport JW and McCarty RE (1984) An analysis of proton fluxes coupled to electron transport and ATP synthesis in chloroplast thylakoids. Biochim Biophys Acta 766: 363–374
Davenport JW and McCarty RE (1986) Relationships between rates of steady state ATP synthesis and the magnitude of the proton gradient across thylakoid membranes. Biochim Biophys Acta 851: 136–145
Deckers-Hebestreit G and Altendorf K (1992) Influence of subunit-speciflc antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. II. Effects of subunit c-specific polyclonal antibodies. J Biol Chem 267: 12364–12369
Feldman RI and Sigman NS (1982) The synthesis of enzyme-bound ATP by soluble chloroplast coupling factor 1. J Biol Chem 257: 1676–1683
Feng Y and McCarty RE (1990a) Purification and reconstitution of active chloroplast F0 J Biol Chem 265: 5104–5109
Feng Y and McCarty RE (1990b) Chromatographic purification of the chloroplast ATP synthase (CF0-CF1 and the role of CF0 subunit IV in proton conductance. J Biol Chem 265: 12474–12480
Fromme PP, Grüber P and Salnikow J (1987) Isolation and identification of a fourth subunit in the membrane part of the chloroplast ATP synthase. FEBS Lett 210: 27–30
Futai M, Noumi T and Maeda J (1989) ATP synthase (H+-ATPase): Results by combined biochemical and molecular biological approaches. Annu Rev Biochem 58: 111–136
Girvin ME and Fillingame RH (1993) Helical structure and folding of subunits of F1F0ATP Synthase: ATP synthase HNMR resonance assignments and NOE analysis. Biochemistry 32: 12167–1177
Grüber P (1990) Kinetics of proton-transport coupled ATP synthesis in chloroplasts. In: Milazzo G and Blank M (eds) Bioelectrochemistry III, pp 277–309. Plenum Press, New York
Gromet-Elhanan Z (1992) Identification of subunits required for catalytic activity of the F1-ATPase. J Bioengr Biomembr 24: 447–452
Hangarter RP and Good ND (1982) Energy thresholds for ATP synthesis in chloroplasts. Biochim Biophys Acta 681: 396–404
Herrmann RG, Steppuhn J, Herrmann GS and Nelson N (1993) The nuclear-encoded polypeptide CF0-H from spinach is a real, ninth subunit of chloroplast ATP synthase. FEBS Lett 326: 192–198
Hochman Y, Lanir A and Carmeli C (1976) Relations between divalent cation binding and ATPase activity in coupling factor from chloroplasts. FEBS Lett 61: 255–259
Hudson GS and Mason JG (1988) The chloroplast genes encoding subunits of the H+-ATP synthase. Photosynth Res 18: 205–222
Jagendorf AT, Robertson N and McCarty RE (1991) Molecular biology of the chloroplast coupling factor subunits. In: Vasil I and Bogorad L (eds) The Molecular Biology of Plastids and Mitochondria, Vol 7 in the series, Cell and Somatic Mutagenesis of Plants, pp 225–254. Academic Press, New York
Junge W (1989) Protons, the thylakoid membrane and chloroplast ATP synthase. Ann NY Acad Sci 574: 268–286
Ketcham SR, Davenport JW, Warncke K and McCarty RE (1984) Role of the subunit of chloroplast coupling factor 1 in the light-dependent activation of photophosphorylation and ATPase activity by dithiothreitol. J Biol Chem 259: 7286–7293
Komatsu-Takaki M (1993) Energy-dependent changes in the conformation of the ATP synthase and its catalytic activity. Eur J Biochem 214: 587–591
Lemaire C and Wollman F-A (1989) The chloroplast ATP synthase in Chlamydomonas reinhardtii. II. Biochemical studies on its biogenesis using mutants defective in photophos-phorylation. J Biol Chem 264: 10235–10242
McCarty RE and Fagan J (1973) Light stimulated incorporation of N-ethylmaleimide into coupling factor 1 in spinach chloroplasts. Biochemistry 12: 1503–1507
McCarty RE and Hammes GG (1987) Molecular architecture of chloroplast coupling factor 1. Trends in Biochem Sci 12: 234–237
McCarty RE and Racker E (1966) Effects of a coupling factor in its antiserum on photophosphorylation and hydrogen ion transport. Brookhaven Symposium in Biology 19: 202–214
McCarty RE and Racker E (1968) Partial resolution of the enzymes catalyzing photophosphorylation III. Activation of adenosine triphosphatase and 32-P-labeled orthophosphate-adenosine triphosphate exchange of chloroplasts. J Biol Chem 243: 129–137
Mills JD and Mitchell P (1984) Thiol modulation of the chloroplast proton motive ATPase and its effects on photophosphorylation. Biochim Biophys Acta 764: 63–67
Mitchell P (1968) Chemiosmotic coupling and energy transfer. Glynn Research Bodmin
Moroney JV and McCarty RE (1982) Effect of proteolytic digestion on the Ca2+-ATPase activity and subunits of latent and thiol-activated chloroplast coupling factor 1. J Biol Chem 257: 5910–5914
Murataliev MB, Milgrom YM and Boyer PD (1991) Charac-teristics of the combination of inhibitory Mg2+ and azide with the F1 ATPase of chloroplasts. Biochemistry 30: 8305–8310
Ort DR and Oxborough K (1992) In situ regulation of chloroplast coupling factor. Annu Rev Plant Physiol Plant Mol Biol 43: 269–291
Pederson PL and Amzel LM (1993) ATP synthases, structure, reaction center, mechanism and regulation of one of nature’s most unique machines. J Biol Chem 268: 9937–9940
Petrack B and Lipmann F (1961) Photophosphorylation and photohydrolysis in cell-free preparations of blue-green algae. In: McElroy WD and Glass HB (eds) Light and Life, pp 621–624. Johns Hopkins Press, Baltimore
Racker E (1976) A new look at mechanisms in bioenergetics. Academic Press, New York
Richter ML, Gromet-Elhanan Z and McCarty RE (1986) Reconstitution of the H+ATPase of Rhodospirillum rubrum by the β subunit of chloroplast coupling factor 1. J Biol Chem 261: 12109–12113
Ryrie IJ and Jagendorf AT (1972) Correlation between a conformational change in the coupling factor protein and the high energy state in chloroplasts. J Biol Chem 247: 4453–4459
Shapiro AB and McCarty RE (1990) Substrate binding-induced alteration of nucleotide binding site properties of chloroplast coupling factor 1. J Biol Chem 265: 4340–4347
Shapiro AB, Huber AH and McCarty RE (1991a) Four tight nucleotide binding sites ofchloroplast coupling factor 1. J Biol Chem 266: 4194–4200
Shapiro AB, Gibson KD, Scheraga HA and McCarty RE (1991 b) Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites ofchloroplast coupling factor 1. J Biol Chem 266: 17276–17285
Sigrist-Nelson K, Sigrist H and Azzi A (1978) Characterization of the dicyclohexylcarbodiimide-binding protein isolated from chloroplast membranes. Eur J Biochem 92: 9–14
Soteropoulos P, Süss K-H and McCarty RE (1992) Modifications of the γ subunit of chloroplast coupling factor 1 alter interactions with the inhibitory ∈ subunit. J Biol Chem 267: 10348–10354
Strotmann H and Bickel-Sandkötter S (1986) Structure, function and regulation ofchloroplast ATPase. Annu Rev Plant Physiol 35: 97–120
Süss KH (1986) Neighbouring subunits of CF0 and between CF1 and CF0 of the soluble chloroplast ATP synthase (CF1-CF0 as revealed by chemical cross-linking. FEBS Lett 201: 63–68
Süss KH and Schmidt O (1982) Evidence for an α3,β3γ,δ,I,II,∈,III3 subunit stoichiometry of chloroplast ATP synthase complex (CF1-CF0 FEBS Lett 144: 213–218
Vambutas VK and Racker E (1965) Stimulation of photophos-phorylation by a preparation of a latent Ca++ dependent adenosine triphosphatase from chloroplasts. J Biol Chem 240: 2660–2667
Wang Z-Y, Freire E, and McCarty RE (1993) Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase. J Biol Chem 268: 20785–20790
Wetzel CM and McCarty RE (1993a) Aspects of subunit interactions in the chloroplast ATP synthase. I. Isolation of a chloroplast-coupling factor 1-subunit III complex from spinach chloroplast thylakoids. Plant Physiol 102: 241–249
Wetzel CM and McCarty RE (1993b) Aspects of subunit interactions in the chloroplast ATP synthase. II. Characterization of a chloroplast coupling factor 1-subunit III complex from spinach thylakoids. Plant Physiol 102: 251–259
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1996 Kluwer Academic Publishers
About this chapter
Cite this chapter
McCarty, R.E. (1996). An Overview of the Function, Composition and Structure of the Chloroplast ATP Synthase. In: Ort, D.R., Yocum, C.F., Heichel, I.F. (eds) Oxygenic Photosynthesis: The Light Reactions. Advances in Photosynthesis and Respiration, vol 4. Springer, Dordrecht. https://doi.org/10.1007/0-306-48127-8_23
Download citation
DOI: https://doi.org/10.1007/0-306-48127-8_23
Publisher Name: Springer, Dordrecht
Print ISBN: 978-0-7923-3683-9
Online ISBN: 978-0-306-48127-7
eBook Packages: Springer Book Archive