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. 1989 Sep;91(1):345–351. doi: 10.1104/pp.91.1.345

Two Isozymes of Dihydroxyacetone Phosphate Reductase in Dunaliella1

Robert Gee 1, Arun Goyal 1, Richard U Byerrum 1, N Edward Tolbert 1
PMCID: PMC1061997  PMID: 16667023

Abstract

Two isoforms of dihydroxyacetone phosphate reductase were present in Dunaliella tertiolecta. The major form was located in the chloroplast and the minor form in the cytosol. The chloroplastic reductase eluted first from a DEAE cellulose column followed immediately by the cytosolic form. Both forms were unstable and cold labile. Addition of 5 millimolar dithiothreitol helped to stabilize the enzymes. The cytosolic isoform of DHAP reductase was detected only if the cells were in an active log phase of growth. Then its activity was 20 to 30% of the total reductase activity. When cell cultures entered late log phase of growth the activity of the cytosolic form of the enzyme disappeared, but the chloroplastic form remained. The cytosolic DHAP reductase from Dunaliella has some properties similar to the cytosolic isoform from spinach leaves. Detergents inhibited both enzymes. However, neither form of the algal dihydroxyacetone phosphate reductase was stimulated by fructose 2,6-bisphosphate. In Dunaliella the properties of the chloroplastic form were those expected for glycerol production for osmoregulation, whereas the cytosolic form, like the reductases in leaves, is more likely involved in glycerol phosphate formation for lipid synthesis.

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Selected References

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

  1. Gee R. W., Byerrum R. U., Gerber D. W., Tolbert N. E. Differential inhibition and activation of two leaf dihydroxyacetone phosphate reductases : role of fructose 2,6-bisphosphate. Plant Physiol. 1988 Jun;87(2):379–383. doi: 10.1104/pp.87.2.379. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Gee R. W., Byerrum R. U., Gerber D. W., Tolbert N. E. Dihydroxyacetone phosphate reductase in plants. Plant Physiol. 1988 Jan;86(1):98–103. doi: 10.1104/pp.86.1.98. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Gee R., Byerrum R. U., Gerber D., Tolbert N. E. Changes in the Activity of the Chloroplastic and Cytosolic Forms of Dihydroxyacetone Phosphate Reductase during Maturation of Leaves. Plant Physiol. 1989 Jan;89(1):305–308. doi: 10.1104/pp.89.1.305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gee R., Goyal A., Gerber D., Byerrum R. U., Tolbert N. E. Isolation of dihydroxyacetone phosphate reductase from dunaliella chloroplasts and comparison with isozymes from spinach leaves. Plant Physiol. 1988 Nov;88(3):896–903. doi: 10.1104/pp.88.3.896. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Goyal A., Betsche T., Tolbert N. E. Isolation of Intact Chloroplasts from Dunaliella tertiolecta. Plant Physiol. 1988 Nov;88(3):543–546. doi: 10.1104/pp.88.3.543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Goyal A., Tolbert N. E. Uptake of inorganic carbon by isolated chloroplasts from air-adapted dunaliella. Plant Physiol. 1989 Apr;89(4):1264–1269. doi: 10.1104/pp.89.4.1264. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Sueoka N. MITOTIC REPLICATION OF DEOXYRIBONUCLEIC ACID IN CHLAMYDOMONAS REINHARDI. Proc Natl Acad Sci U S A. 1960 Jan;46(1):83–91. doi: 10.1073/pnas.46.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]

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