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. 1994 Aug;105(4):1393–1398. doi: 10.1104/pp.105.4.1393

Two Distinct Aldolases of Class II Type in the Cyanoplasts and in the Cytosol of the Alga Cyanophora paradoxa.

W Gross 1, M G Bayer 1, C Schnarrenberger 1, U B Gebhart 1, T L Maier 1, HEA Schenk 1
PMCID: PMC159472  PMID: 12232294

Abstract

Two aldolases from the alga Cyanophora paradoxa (Glaucocystophyta) can be separated by chromatography on diethylaminoethyl-Fractogel. The two aldolases are inhibited by 1 mM ethylene-diaminetetraacetate (EDTA) and, therefore, are class II aldolases. When cells of C. paradoxa were fractionated, one aldolase was associated with the cytosol fraction and the other was associated with the cyanoplast fraction. The Km(fructose-1,6-bisphosphate) was 600 [mu]M for the cytosolic aldolase and 340 [mu]M for the cyanoplast aldolase. The activity of the cytosolic aldolase was increased up to 4-fold by 100 mM K+ and slightly inhibited by Li+ and Cs+, whereas the cyanoplast aldolase was not affected by these ions. Inactivation by 1 mM EDTA could be partly restored by the addition of Co2+ or Mn2+ and to a lesser extent by Zn2+ or Mg2+. The molecular masses of the native cytosolic and cyanoplast aldolases are about 90 and 85 kD, respectively, as estimated by velocity centrifugation in sucrose gradients. Implications for the evolution of class I and II aldolases in chloroplasts of higher plants and algae will be discussed.

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Selected References

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  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  2. Bryant D. A., Stirewalt V. L. The cyanelle genome of Cyanophora paradoxa encodes ribosomal proteins not encoded by the chloroplasts genomes of higher plants. FEBS Lett. 1990 Jan 1;259(2):273–280. doi: 10.1016/0014-5793(90)80026-f. [DOI] [PubMed] [Google Scholar]
  3. Evrard J. L., Johnson C., Janssen I., Löffelhardt W., Weil J. H., Kuntz M. The cyanelle genome of Cyanophora paradoxa, unlike the chloroplast genome, codes for the ribosomal L3 protein. Nucleic Acids Res. 1990 Mar 11;18(5):1115–1119. doi: 10.1093/nar/18.5.1115. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. JAGANNATHAN V., SINGH K., DAMODARAN M. Carbohydrate metabolism in citric acid fermentation. 4. Purification and properties of aldolase from Aspergillus niger. Biochem J. 1956 May;63(1):94–105. doi: 10.1042/bj0630094. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kelley P. M., Tolan D. R. The complete amino Acid sequence for the anaerobically induced aldolase from maize derived from cDNA clones. Plant Physiol. 1986 Dec;82(4):1076–1080. doi: 10.1104/pp.82.4.1076. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kobes R. D., Simpson R. T., Vallee R. L., Rutter W. J. A functional role of metal ions in a class II aldolase. Biochemistry. 1969 Feb;8(2):585–588. doi: 10.1021/bi00830a018. [DOI] [PubMed] [Google Scholar]
  7. Lebherz H. G., Rutter W. J. A class I (Schiff base) fructose diphosphate aldolase of prokaryotic origin. Purification and properties of Micrococcus aerogenes aldolase. J Biol Chem. 1973 Mar 10;248(5):1650–1659. [PubMed] [Google Scholar]
  8. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  9. Marsh J. J., Lebherz H. G. Fructose-bisphosphate aldolases: an evolutionary history. Trends Biochem Sci. 1992 Mar;17(3):110–113. doi: 10.1016/0968-0004(92)90247-7. [DOI] [PubMed] [Google Scholar]
  10. Mateyka C., Schnarrenberger C. Purification and Properties of Mesophyll and Bundle Sheath Cell alpha-Glucan Phosphorylases from Zea mays L. : Equivalence of the Enzymes with the Cytosol and Plastid Phosphorylases from Spinach. Plant Physiol. 1988 Feb;86(2):417–422. doi: 10.1104/pp.86.2.417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Morden C. W., Golden S. S. psbA genes indicate common ancestry of prochlorophytes and chloroplasts. Nature. 1989 Jan 26;337(6205):382–385. doi: 10.1038/337382a0. [DOI] [PubMed] [Google Scholar]
  12. Neumann-Spallart C., Brandtner M., Kraus M., Jakowitsch J., Bayer M. G., Maier T. L., Schenk H. E., Löffelhardt W. The petFI gene encoding ferredoxin I is located close to the str operon on the cyanelle genome of Cyanophora paradoxa. FEBS Lett. 1990 Jul 30;268(1):55–58. doi: 10.1016/0014-5793(90)80971-k. [DOI] [PubMed] [Google Scholar]
  13. Pelzer-Reith B., Penger A., Schnarrenberger C. Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach. Plant Mol Biol. 1993 Jan;21(2):331–340. doi: 10.1007/BF00019948. [DOI] [PubMed] [Google Scholar]
  14. RICHARDS O. C., RUTTER W. J. Comparative properties of yeast and muscle aldolase. J Biol Chem. 1961 Dec;236:3185–3192. [PubMed] [Google Scholar]
  15. RICHARDS O. C., RUTTER W. J. Preparation and properties of yeast aldolase. J Biol Chem. 1961 Dec;236:3177–3184. [PubMed] [Google Scholar]
  16. RUTTER W. J. EVOLUTION OF ALDOLASE. Fed Proc. 1964 Nov-Dec;23:1248–1257. [PubMed] [Google Scholar]
  17. Schnarrenberger C., Jacobshagen S., Müller B., Krüger I. Evolution of isozymes of sugar phosphate metabolism in green algae. Prog Clin Biol Res. 1990;344:743–764. [PubMed] [Google Scholar]
  18. Stanier R. Y. Jacques Monod, 1910-1976. J Gen Microbiol. 1977 Jul;101(1):1–12. doi: 10.1099/00221287-101-1-1. [DOI] [PubMed] [Google Scholar]
  19. Turner S., Burger-Wiersma T., Giovannoni S. J., Mur L. R., Pace N. R. The relationship of a prochlorophyte Prochlorothrix hollandica to green chloroplasts. Nature. 1989 Jan 26;337(6205):380–382. doi: 10.1038/337380a0. [DOI] [PubMed] [Google Scholar]
  20. Willard J. M., Gibbs M. Purification and characterization of the fructose diphosphate aldolases from Anacystis is nidulans and Saprospira thermalis. Biochim Biophys Acta. 1968 Feb 5;151(2):438–448. doi: 10.1016/0005-2744(68)90112-5. [DOI] [PubMed] [Google Scholar]

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