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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

These references are in PubMed. This may not be the complete list of references from this article.

  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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