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. 1992 Apr 1;89(7):3080–3082. doi: 10.1073/pnas.89.7.3080

Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase.

M K Williams 1, E R Kantrowitz 1
PMCID: PMC48807  PMID: 1313579

Abstract

A full-length clone of pig kidney fructose 1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) was isolated by screening a cDNA library for complementation of an Escherichia coli fbp deletion mutation. The open reading frame of 1011 bases corresponds to 337 amino acids, two more than have been previously reported [Marcus, F., Edelstein, I., Reardon, I. & Heinrikson, R. L. (1982) Proc. Natl. Acad. Sci. USA 79, 7161-7165]. The extra two amino acids (Ala-Lys) are located at the C-terminal end of the protein as an extension. Comparison of the deduced amino acid sequence with the reported (see above) and revised amino acid sequence [Harrsch, P. B., Kim, Y., Fox, J. L. & Marcus, F. (1985) Biochem. Biophys. Res. Commun. 133, 520-526] indicates three differences in addition to the C-terminal extension. Gln-20, Thr-96, and Asn-199 in the amino acid sequence are found to be Glu, Ser, and Asp, respectively. Since the x-ray structure of the pig kidney enzyme has been reported, the cDNA clone will allow the construction of site-specific mutants to help test possible structure-function relationships in this important metabolic enzyme.

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Selected References

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  1. Benkovic S. J., deMaine M. M. Mechanism of action of fructose 1,6-bisphosphatase. Adv Enzymol Relat Areas Mol Biol. 1982;53:45–82. doi: 10.1002/9780470122983.ch2. [DOI] [PubMed] [Google Scholar]
  2. Fisher W. K., Thompson E. O. Amino acid sequence studies on sheep liver fructose-bisphosphatase. II. The complete sequence. Aust J Biol Sci. 1983;36(3):235–250. doi: 10.1071/bi9830235. [DOI] [PubMed] [Google Scholar]
  3. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  4. Harrsch P. B., Kim Y., Fox J. L., Marcus F. Amino acid sequence similarity between spinach chloroplast and mammalian gluconeogenic fructose-1,6-bisphosphatase. Biochem Biophys Res Commun. 1985 Dec 17;133(2):520–526. doi: 10.1016/0006-291x(85)90937-4. [DOI] [PubMed] [Google Scholar]
  5. Horecker B. L., Melloni E., Pontremoli S. Fructose 1,6-bisphosphatase: properties of the neutral enzyme and its modification by proteolytic enzymes. Adv Enzymol Relat Areas Mol Biol. 1975;42:193–226. doi: 10.1002/9780470122877.ch4. [DOI] [PubMed] [Google Scholar]
  6. Ke H. M., Liang J. Y., Zhang Y. P., Lipscomb W. N. Conformational transition of fructose-1,6-bisphosphatase: structure comparison between the AMP complex (T form) and the fructose 6-phosphate complex (R form). Biochemistry. 1991 May 7;30(18):4412–4420. doi: 10.1021/bi00232a007. [DOI] [PubMed] [Google Scholar]
  7. Ke H. M., Thorpe C. M., Seaton B. a., Lipscomb W. N., Marcus F. Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8 A resolution. J Mol Biol. 1990 Apr 5;212(3):513–539. doi: 10.1016/0022-2836(90)90329-k. [DOI] [PubMed] [Google Scholar]
  8. Ke H., Thorpe C. M., Seaton B. A., Marcus F., Lipscomb W. N. Molecular structure of fructose-1,6-bisphosphatase at 2.8-A resolution. Proc Natl Acad Sci U S A. 1989 Mar;86(5):1475–1479. doi: 10.1073/pnas.86.5.1475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kozak M. The scanning model for translation: an update. J Cell Biol. 1989 Feb;108(2):229–241. doi: 10.1083/jcb.108.2.229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Marcus F., Edelstein I., Reardon I., Heinrikson R. L. Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7161–7165. doi: 10.1073/pnas.79.23.7161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rogers D. T., Hiller E., Mitsock L., Orr E. Characterization of the gene for fructose-1,6-bisphosphatase from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Sequence, protein homology, and expression during growth on glucose. J Biol Chem. 1988 May 5;263(13):6051–6057. [PubMed] [Google Scholar]
  12. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sedivy J. M., Daldal F., Fraenkel D. G. Fructose bisphosphatase of Escherichia coli: cloning of the structural gene (fbp) and preparation of a chromosomal deletion. J Bacteriol. 1984 Jun;158(3):1048–1053. doi: 10.1128/jb.158.3.1048-1053.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sheets M. D., Ogg S. C., Wickens M. P. Point mutations in AAUAAA and the poly (A) addition site: effects on the accuracy and efficiency of cleavage and polyadenylation in vitro. Nucleic Acids Res. 1990 Oct 11;18(19):5799–5805. doi: 10.1093/nar/18.19.5799. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. TAKETA K., POGELL B. M. ALLOSTERIC INHIBITION OF RAT LIVER FRUCTOSE 1,6-DIPHOSPHATASE BY ADENOSINE 5'-MONOPHOSPHATE. J Biol Chem. 1965 Feb;240:651–662. [PubMed] [Google Scholar]
  16. Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 1987;153:3–11. doi: 10.1016/0076-6879(87)53044-0. [DOI] [PubMed] [Google Scholar]
  17. el-Maghrabi M. R., Pilkis J., Marker A. J., Colosia A. D., D'Angelo G., Fraser B. A., Pilkis S. J. cDNA sequence of rat liver fructose-1,6-bisphosphatase and evidence for down-regulation of its mRNA by insulin. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8430–8434. doi: 10.1073/pnas.85.22.8430. [DOI] [PMC free article] [PubMed] [Google Scholar]

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