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. 1984 Jul;75(3):539–541. doi: 10.1104/pp.75.3.539

Light-Induced Nuclear Synthesis of Spinach Chloroplast Fructose-1,6-bisphosphatase 1

Ana Chueca 1, Juan José Lázaro 1, Julio López Gorgé 1
PMCID: PMC1066951  PMID: 16663662

Abstract

Etiolated spinach (Spinacia oleracea L. var Winter Giant) seedlings show a residual photosynthetic fructose-1,6-bisphosphatase activity, which sharply rises under illumination. This increase in activity is due to a light-induced de novo synthesis, as it has been demonstrated by enzyme labeling experiments with 2H2O and [35S]methionine. The rise of bisphosphatase activity under illumination is strongly inhibited by cycloheximide, but not by the 70S ribosome inhibitor lincocin, which shows the nuclear origin of this chloroplastic enzyme.

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Selected References

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  1. Anderson L. E., Avron M. Light Modulation of Enzyme Activity in Chloroplasts: Generation of Membrane-bound Vicinal-Dithiol Groups by Photosynthetic Electron Transport. Plant Physiol. 1976 Feb;57(2):209–213. doi: 10.1104/pp.57.2.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anderson L. E., Chin H. M., Gupta V. K. Modulation of Chloroplast Fructose-1,6-bisphosphatase Activity by Light. Plant Physiol. 1979 Sep;64(3):491–494. doi: 10.1104/pp.64.3.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Arnon D. I. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949 Jan;24(1):1–15. doi: 10.1104/pp.24.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blair G. E., Ellis R. J. Protein synthesis in chloroplasts. I. Light-driven synthesis of the large subunit of fraction I protein by isolated pea chloroplasts. Biochim Biophys Acta. 1973 Aug 24;319(2):223–234. doi: 10.1016/0005-2787(73)90013-0. [DOI] [PubMed] [Google Scholar]
  5. Bloom M. V., Milos P., Roy H. Light-dependent assembly of ribulose-1,5-bisphosphate carboxylase. Proc Natl Acad Sci U S A. 1983 Feb;80(4):1013–1017. doi: 10.1073/pnas.80.4.1013. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Buchanan B. B., Schürmann P., Kalberer P. P. Ferredoxin-activated fructose diphosphatase of spinach chloroplasts. Resolution of the system, properties of the alkaline fructose diphosphatase component, and physiological significance of the ferredoxin-linked activation. J Biol Chem. 1971 Oct 10;246(19):5952–5959. [PubMed] [Google Scholar]
  7. Charles S. A., Halliwell B. Properties of freshly purified and thiol-treated spinach chloroplast fructose bisphosphatase. Biochem J. 1980 Mar 1;185(3):689–693. doi: 10.1042/bj1850689. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Chua N. H., Schmidt G. W. Post-translational transport into intact chloroplasts of a precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase. Proc Natl Acad Sci U S A. 1978 Dec;75(12):6110–6114. doi: 10.1073/pnas.75.12.6110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Criddle R. S., Dau B., Kleinkopf G. E., Huffaker R. C. Differential synthesis of ribulosediphosphate carboxylase subunits. Biochem Biophys Res Commun. 1970 Nov 9;41(3):621–627. doi: 10.1016/0006-291x(70)90058-6. [DOI] [PubMed] [Google Scholar]
  10. Domagk G. F., Chilla R. Glucose-6-phosphate dehydrogenase from Candida utilia. Methods Enzymol. 1975;41:205–208. doi: 10.1016/s0076-6879(75)41048-5. [DOI] [PubMed] [Google Scholar]
  11. Grossman A. R., Bartlett S. G., Schmidt G. W., Mullet J. E., Chua N. H. Optimal conditions for post-translational uptake of proteins by isolated chloroplasts. In vitro synthesis and transport of plastocyanin, ferredoxin-NADP+ oxidoreductase, and fructose-1,6-bisphosphatase. J Biol Chem. 1982 Feb 10;257(3):1558–1563. [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. Leto K. J., Keresztes A., Arntzen C. J. Nuclear Involvement in the Appearance of a Chloroplast-Encoded 32,000 Dalton Thylakoid Membrane Polypeptide Integral to the Photosystem II Complex. Plant Physiol. 1982 Jun;69(6):1450–1458. doi: 10.1104/pp.69.6.1450. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Portis A. R., Jr, Heldt H. W. Light-dependent changes of the Mg2+ concentration in the stroma in relation to the Mg2+ dependency of CO2 fixation in intact chloroplasts. Biochim Biophys Acta. 1976 Dec 6;449(3):434–436. doi: 10.1016/0005-2728(76)90154-7. [DOI] [PubMed] [Google Scholar]
  15. Pradel J., Soulié J. M., Buc J., Meunier J. C., Ricard J. On the activation of fructose-1,6-bisphosphatase of spinach chloroplasts and the regulation of the Calvin cycle. Eur J Biochem. 1981 Jan;113(3):507–511. doi: 10.1111/j.1432-1033.1981.tb05092.x. [DOI] [PubMed] [Google Scholar]
  16. Steinback K. E., McIntosh L., Bogorad L., Arntzen C. J. Identification of the triazine receptor protein as a chloroplast gene product. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7463–7467. doi: 10.1073/pnas.78.12.7463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wolosiuk R. A., Crawford N. A., Yee B. C., Buchanan B. B. Isolation of three thioredoxins from spinach leaves. J Biol Chem. 1979 Mar 10;254(5):1627–1632. [PubMed] [Google Scholar]
  18. Zimmermann G., Kelly G. J., Latzko E. Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase. Eur J Biochem. 1976 Nov 15;70(2):361–367. doi: 10.1111/j.1432-1033.1976.tb11025.x. [DOI] [PubMed] [Google Scholar]
  19. Zimmermann G., Kelly G. J., Latzko E. Purification and properties of spinach leaf cytoplasmic fructose-1,6-bisphosphatase. J Biol Chem. 1978 Sep 10;253(17):5952–5956. [PubMed] [Google Scholar]

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