Skip to main content
SpringerLink
Log in

Catalytic properties of β subunit isolated from chloroplast coupling factor 1

  • Regular Paper
  • Published:
Photosynthesis Research Aims and scope Submit manuscript

Abstract

The chloroplast coupling factor (CF1) was dissociated into subunits by the freezing-thawing procedure in the presence of 0.5 M NaBr and the β subunit was purified by ion-exchange chromatography on a DEAE-cellulose column. The β subunit did not catalyze ATP hydrolysis either in the presence or in the absence of reagents known to activate Mg2+-dependent ATPase activity of CF1. However, it manifested appreciable adenylate kinase-like and ATP-ADP γ-phosphate exchange activities. The adenylate kinase-like activity only slightly depended on Mg2+ ions. Ethanol, and especially diadenosine pentaphosphate, inhibited the reaction effectively. In contrast, the ATP-ADP exchange activity was Mg2+-dependent. Ethanol and diadenosine pentaphosphate were poor inhibitors. Sulfite, the CF1-ATPase activator, and quercetin, its inhibitor, had a minor effect on catalytic activity of the β subunit.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

CF:

chloroplast coupling factor 1

RBP:

carboxylase-ribulose-1,5-bisphosphate carboxylase

TLC:

thin layer chromatography

MES:

morpholinoethane sulfonic acid

PMSF:

phenylmethylsulfonyl fluoride

AP5A:

diadenosine pentaphosphate, P1, P5-bis(5′-adenosyl)pentaphosphate

DCCD:

N1N′-dicyclohexylcarbodiimide

SDS:

sodium dodecylsulfate

PAAG:

polyacrylamide gel

References

  • Al-Shavi MK, Parsonage D and Senior AE (1990) Adenosine triphosphatase and nucleotide binding activity of isolated β subunit preparations from Escherichia coli F1F0 synthase. J Biol Chem 265: 5595–5601

    Google Scholar 

  • Andralojc PJ and Harris DA (1990) Promotion and inhibition of catalytic cooperativity of the Ca2+-dependent ATPase activity of spinach chloroplast coupling factor 1 (CF1). Biochim Biophys Acta 1016: 55–62

    Google Scholar 

  • Berger G, Girault G, Andre F and Galmiche GM (1987) Application of HPLC to the purification of coupling factor CF1 from spinach chloroplasts and of some of its subunits. J Liquid Chrom 10: 1507–1517

    Google Scholar 

  • Bickel-Sandkotter S and Schull H (1987) ATP/ADP γ-phosphate exchange catalyzed by chloroplast ATPase. Biochim Biophys Acta 893: 342–348

    Google Scholar 

  • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254

    Google Scholar 

  • Bronnikov GE and Zakharov SD (1983) Microquantitative determination of P-ATP and ADP-ATP exchange kinetics using thin-layer chromatography on silica gel. Anal Biochem 131: 69–74

    Google Scholar 

  • Deters DW, Racker E, Nelson N and Nelson N (1975) Partial resolution of the enzymes catalyzing photophosphorylation. Approaches to the active site of coupling factor 1. J Biol Chem 250: 1041–1047

    Google Scholar 

  • Du Z and Boyer PD (1990) On the mechanism of sulfite activation of chloroplast thylakoid ATPase and the relation of ADP tightly bound at a catalytic site to the binding change mechanism. Biochemistry 29: 402–407

    Google Scholar 

  • Dunn SD and Futai M (1980) Reconstitution of a functional coupling factor from the isolated subunits of Escherichia coli F1 ATPase. J Biol Chem 255: 113–118

    Google Scholar 

  • Frash WD, Green J, Caguiat J and Mejia A (1989) ATP hydrolysis catalyzed by β subunit preparation purified from the chloroplast energy transducing complex CF1 CF0. J Biol Chem 264: 5064–5069

    Google Scholar 

  • Fromme P and Graber P (1989) Heterogeneity of ATP-binding sites on reconstituted CF0F1. FEBS Lett 259: 26–33

    Google Scholar 

  • Futai M (1977) Reconstitution of ATPase activity from the isolated α, β and γ subunits of the coupling factor F1 of Escherichia coli. Biochem Biophys Res Commun 79: 1231–1237

    Google Scholar 

  • Futai M, Shimomura S and Maeda M (1987) Binding of Mg2+ to the β subunit of H+-ATPase from Escherichia coli. Arch Biochem Biophys 254: 313–318

    Google Scholar 

  • Girault G, Berger G, Galmiche G-M and Andre F (1988) Characterization of six nucleotide binding sites of chloroplast coupling factor 1 and one site on its purified β subunit. J Biol Chem 263: 14690–14695

    Google Scholar 

  • Isern X, Amzel LM and Pedersen PL (1988) ATP synthases-structure of the F1-moiety and its relationship to function and mechanism. J Bioenerg Biomembr 20: 423–450

    Google Scholar 

  • Issartel JP and Vignais PV (1984) Evidence for a nucleotide binding site on the isolated β subunit from Escherichia coli F1ATPase. Interaction between nucleotide and aurovertin D binding sites. Biochemistry 23: 6591–6595

    Google Scholar 

  • Jagendorf AT (1982) Isolation of chloroplast coupling factor (CF1) and of its subunit. In: Edelman M, et al. (eds) Methods of Chloroplast Molecular Biology, pp 881–898. Elsevier Biomedical Press, Amsterdam

    Google Scholar 

  • Kasamo K, Kagita F and Arai Y (1989) Isolation of subunits of coupling factor 1 from maise and spinach chloroplasts and properties of combinations of subunits with ATPase activity. Plant Cell Physiol 30: 729–738

    Google Scholar 

  • Khananshvili D and Gromet-Elhaman Z (1985) Characterization of an inorganic phosphate binding site on the isolated reconstitutively active β subunit of F0F1 ATP synthase. Biochemistry 24: 2482–2487

    Google Scholar 

  • Laemli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–684

    Google Scholar 

  • Malyan AN (1980) Allosteric properties of CF1-ATPase from chloroplasts. Biochemistry (USSR) 45: 1303–1310

    Google Scholar 

  • Malyan AN (1981) Chloroplast ATPase (CF1): Allosteric regulation by ADP and Mg2+ ions. Photosynthetica 15: 474–483

    Google Scholar 

  • Malyan AN and Akulova EA (1978) Mechanism of stimulation of soluble ATPase of chloroplasts (CF1). Biochemistry (USSR) 43: 952–956

    Google Scholar 

  • Malyan AN and Makarov AD (1976) Study of kinetics and mechanism of hydrolysis of ATP by soluble ATPase of chloroplasts (CF1) in presence of Mg2+. Biochemistry (USSR) 41: 888–893

    Google Scholar 

  • Malyan AN and Vitseva OI (1987) Kinetics of sulfite activtion of CF1-ATPase Mg2+-dependent activity. Physiol Biochem Cult Plants 19: 456–461

    Google Scholar 

  • Malyan AN and Vitseva OI (1990) pH-dependent changes in ADP and ATP affinity for the tight nucleotide-binding site of chloroplast coupling factor 1. Photosynth Res 25: 11–16

    Google Scholar 

  • Malyan AN, Zakharov SD, Proskuryakov II (1981) The role of carboxyl groups in the catalytic and regulatory properties of CF1-ATPase. Biochem Physiol Pflanzen 176: 828–834

    Google Scholar 

  • Moudrianakis EN and Tiefert MA (1976) Synthesis of bound adenosine triphosphate from bound adenosine diphosphate by the purified coupling factor 1 of chloroplasts. Biol Chem 251: 7796–7801

    Google Scholar 

  • Nelson N, Nelson H and Racker E (1972) Partial resolution of the enzymes catalyzing photophosphorylation. Magnesium-adenosine triphosphatase properties of heat-activated coupling factor 1 from chloroplasts. J Biol Chem 247: 6506–6510

    Google Scholar 

  • Philosoph S, Binder A and Gromet-Elhanan Z (1977) Coupling factor ATPase complex of Rhodospirillum rubrum. Purification and properties of reconstitutively active single subunit. J Biol Chem 252: 8747–8752

    Google Scholar 

  • Richter ML, Gromet-Elhanan Z and McCarty RE (1986) Reconstitution of the H+-ATPase complex of Rhodospirillum rubrum by the β subunit of the chloroplast coupling factor 1. J Biol Chem 261: 12109–12113

    Google Scholar 

  • Roux-Fromy M, Neumann J-M, Andre F, Berger G, Girault G, Galmiche J-M and Remy R (1987) Biochemical and proton NMR characterization of the isolated functional beta-subunit of coupling factor one from spinach chloroplasts. Biochem and Biophys Res Commun 144: 718–725

    Google Scholar 

  • Sacurai H, Shinohara R, Hisabory T and Shinohara K (1981) Enhancement of adenosine triphosphatase activity of purified chloroplast coupling factor 1 in an aqueous organic solvent. J Biochem 90: 95–102

    Google Scholar 

  • Sato MH, Hisabory T and Yoshida M (1990) The 55-kDa polypeptide released from spinach thylakoid membranes with 1 M LiCl is not the β subunit of chloroplast F1. J Biol Chem 265: 13419–13422

    Google Scholar 

  • Schafer H-J, Rathgeber G, Dose K and Kagawa Y (1989) Photoaffinity crosslinking of F1-ATPase from thermophilic bacterium PS3 by 3′-arylazido-β-alanyl-2-azido ATP. FEBS Lett 253: 264–268

    Google Scholar 

  • Shavit N, Skye GE and Boyer PD (1967) Occurance and possible mechanism of 32P and 18O exchange reactions of photophosphorylation. J Biol Chem 242: 5125–5130

    Google Scholar 

  • Shoshan V and Selman BR (1980) The interaction of N1N′-dicyclohexylcarbodiimide with chloroplast coupling factor 1. J Biol Chem 255: 384–389

    Google Scholar 

  • Vambutas VK and Racker E (1965) Partial resolution of the enzymes catalyzing photophosphorylation. I. Stimulation of photophosphorylation by a preparation of a latent Ca2+-dependent adenosine triphosphatase from chloroplasts. J Biol Chem 240: 2660–2667

    Google Scholar 

  • Xue Z, Miller CG, Zhou J-M and Boyer PD (1987) Catalytic and non-catalytic nucleotide binding sites of chloroplast F1 ATPase. FEBS Lett 223: 391–394

    Google Scholar 

  • Yoshida M, Okamoto H, Sone N, Hirata H and Kagawa Y (1977) Reconstitution of thermostable ATPase capable of energy coupling from its purified subunits. Proc Natl Acad Sci USA 74: 936–940

    Google Scholar 

  • Younis HH, Winget GD and Racker E (1977) Requirement of the δ subunit of chloroplast coupling factor 1 for photophosphorylation. J Biol Chem 252: 1814–1818

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Soil Science and Photosynthesis, Academy of Sciences of the USSR, Pushchino, Moscow Region, USSR

    A. N. Malyan & O. I. Vitseva

Authors
  1. A. N. Malyan
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. O. I. Vitseva
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Malyan, A.N., Vitseva, O.I. Catalytic properties of β subunit isolated from chloroplast coupling factor 1. Photosynth Res 30, 107–113 (1991). https://doi.org/10.1007/BF00042008

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00042008

Key words

Search

Navigation