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Isolation and characterization of a cDNA encoding cytosolic fructose-1,6-bisphosphatase from spinach

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References

  1. Buchanan BB: Role of light in the regulation of chloroplast enzymes. Annu Rev Plant Physiol 31: 341–374 (1980).

    Article  Google Scholar 

  2. Fisher WK, Thompson EOP: Amino acid sequence studies on sheep liver fructose-bisphosphatase. II. The complete sequence. Aust J Biol Sci 33: 665–674 (1980).

    PubMed  Google Scholar 

  3. Hamilton WDO, Harrison DA, Dyer TA: Sequence of theEscherichia coli fructose-1,6-bisphosphatase gene. Nucl Acids Res 16: 8707 (1988).

    PubMed  Google Scholar 

  4. Heidecker G, Messing J: Structural analysis of plant genes. Annu Rev Plant Physiol 37: 439–466 (1988).

    Google Scholar 

  5. Henikoff S: Unidirectional digestion with Exonuclease III in DNA sequence analysis. Meth Enzymol 155: 156–165 (1987).

    PubMed  Google Scholar 

  6. Hur Y, Unger EA, Vasconcelose AC: Isolation and characterization of a cDNA encoding a cytoplasmic fructose-1,6-bisphosphatase. Plant Physiol 89: S407 (1989).

    Google Scholar 

  7. Ke H, Thorpe CM, Seaton BA, Marcus F, Lipscomb WN: Molecular structure of fructose-1,6-bisphosphatase at 2.8-Å resolution. Proc Natl Acad Sci USA 86: 1475–1479 (1989).

    PubMed  Google Scholar 

  8. Ke H, Thorpe CM, Seaton BA, Lipscomb WN: Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8-Å resolution. J Mol Biol 212: 513–539 (1989).

    Article  Google Scholar 

  9. Ke H, Zhang Y, Lipscomb WN: Crystal structure of fructose-1,6-bisphosphatase complex with fructose 6-phosphate, AMP, and magnesium. Proc Natl Acad Sci USA 87: 5243–5247 (1990).

    PubMed  Google Scholar 

  10. Ke H, Zhang Y, Liang J-Y, Lipscomb WN: Crystal structure of the neutral form of fructose-1,6-bisphosphatase complex with the product fructose 6-phosphate 2.1-Å resolution. Proc Natl Acad Sci USA 88: 2989–2993 (1991).

    PubMed  Google Scholar 

  11. Kelly JG, Zimmerman G, Latzko E: Fructose bisphosphatase from spinach chloroplast and cytoplasm. Meth Enzymol 90: 371–378 (1982).

    PubMed  Google Scholar 

  12. Ladror US, Latshaw SP, Marcus F: Spinach cytosolic fructose-1,6-bisphosphatase: purification, enzyme properties and structural comparisons. Eur J Biochem 189: 89–94 (1990).

    PubMed  Google Scholar 

  13. El-Maghrabi MR, Pilkis J, Marker AJ, Colosia AD, D'Angelo, Fraser BA, Pilkis SJ: cDNA sequence of rat liver fructose-1,6-bisphosphatase and evidence for down-regulation of its mRNA by insulin. Proc Natl Acad Sci USA 85: 8430–8434 (1988).

    PubMed  Google Scholar 

  14. Marcus F, Edelstein I, Reardon I, Heinrikson RL: Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase. Proc Natl Acad Sci USA 79: 7161–7165 (1982).

    PubMed  Google Scholar 

  15. Marcus F, Harrsch PB: Amino acid sequence of spinach chloroplast fructose-1,6-bisphosphatase: Arch Biochem Biophys 279: 11–157 (1990).

    Google Scholar 

  16. Raines CA, Lloyd JC, Longstaff M, Bradley D, Dyer T: Chloroplast fructose-1,6-bisphosphatase: the product of a mosaic gene. Nucl Acids Res 16: 7931–7942 (1988).

    PubMed  Google Scholar 

  17. Rogers DT, Hiller E, Mitsock L, Orr E: Characterization of the gene for fructose-1,6-bisphosphatase fromSaccharomyces cerevisiae andSchizosaccharomyces pombe. J Biol Chem 263: 6051–6057 (1988).

    PubMed  Google Scholar 

  18. Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain terminating inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).

    PubMed  Google Scholar 

  19. Sedivy JM, Fraenkel DG: Fructose bisphosphatase ofSaccharomyces cerevisiae: cloning, disruption and regulation of the FBP1 structural gene. J Mol Biol 186: 307–319 (1985).

    PubMed  Google Scholar 

  20. Stitt M, Quick WP: Photosynthetic carbon partitioning: its regulation and possibilities for manipulation. Physiol Plant 77: 633–641 (1989).

    Google Scholar 

  21. Tejwani GA: Regulation of fructose-bisphosphatase activity. Adv Enzymol 54: 121–194 (1983).

    PubMed  Google Scholar 

  22. Werneke JM, Zielinski RE, Ogren WL: Structure and expression of spinach leaf cDNA encoding ribulose bisphosphate carboxylase/oxygenase activase. Proc Natl Acad Sci USA 85: 787–791 (1988).

    PubMed  Google Scholar 

  23. Whusz J, Shenk T: A 64 kD nuclear protein binds to RNA segments that include the AAUAAA polyadenylation motif. Cell 52: 221–228 (1988).

    Article  PubMed  Google Scholar 

  24. Xu G-J, Datta AG, Singh VN, Suda H, Pontremoli S, Horecker BL: Rabbit liver fructose 1,6-bisphosphatase: labelling of the active and allosteric sites with pyridoxal 5-phosphate and sequence of a nonapeptide from the active site. Arch Biochem Biophys 210: 98–103 (1981).

    PubMed  Google Scholar 

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Authors and Affiliations

  1. Department of Biological Sciences, Rutgers University, 08855-1059, Piscataway, NJ, USA

    Yoonkang Hur, Erica A. Unger & Aurea C. Vasconcelos

  2. Molecular and Cell Biology, U125, University of Connecticut, 06268, Storrs, CT, USA

    Erica A. Unger

Authors
  1. Yoonkang Hur
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  2. Erica A. Unger
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  3. Aurea C. Vasconcelos
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Hur, Y., Unger, E.A. & Vasconcelos, A.C. Isolation and characterization of a cDNA encoding cytosolic fructose-1,6-bisphosphatase from spinach. Plant Mol Biol 18, 799–802 (1992). https://doi.org/10.1007/BF00020023

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  • DOI: https://doi.org/10.1007/BF00020023

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