Abstract
We have sequenced and analysed the transaldolase (tal) genes from two cyanobacteria, Anabaena variabilis (ATCC 29413) and Synechocystis sp. PCC 6803, which are filamentous heterocyst-forming and unicellular organisms, respectively. The deduced amino acid sequences of the two cyanobacterial tal genes are 78% identical and are highly homologous to both eubacterial and eukaryotic transaldolases (Escherichia coli, two yeasts, and man) with values ranging from 54 to 60% amino acid identity. In contrast, the transaldolase homologous sequences from the cyanobacterium Nostoc sp. ATCC 29133, from Mycobacterium leprae, and the partial sequence from the higher plant Arabidopsis thaliana have a much lower degree of homology with each other and relative to the sequences mentioned above. These data indicate three different types of transaldolases.
References
Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ: Basic local alignment search tool. J Mol Biol 215: 403–410 (1990).
Banki K, Halladay D, Perl A: Cloning and expression of the human gene for transaldolase. J Mol Biol 269: 2847–2851 (1994).
Chamberlain JW, Henderson G, Chang MW-M, Lam T, Dignard D, Ling V, Price GB, Stanners CP: The structure of HSAG-1, a middle repetetive genetic element which elicits a leukemia-related cellular surface antigen. Nucl Acids Res 14: 3409–3424 (1986).
Devereux J, Haeberli P, Smithies O: A comprehensive set of sequence analysis programs for the VAX. Nucl Acids Res 12: 387–395 (1984).
Higgings DH, Sharp PM: CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73: 237–244 (1988).
Horecker BL, Smyrniotis PZ: Purification and properties of yeast transaldolase. J Biol Chem 212: 811–825 (1955).
Jacoby J, Hollenberg CP, Heinisch JJ: Transaldolase mutants in the yeast Kluyveromyces lactis provide evidence that glucose can be metabolized throgh the pentose phosphate pathway. Mol Microbiol 10: 867–876 (1993).
Martin W, Brinkmann H, Savona C, Cerff R: Evidence for a chimaeric nature of nuclear genomes: Eubacterial origin of eukaryotic glyceraldehyde 3-phosphate dehydrogenase genes. Proc Natl Acad Sci USA 90: 8692–8696 (1993).
Miosga T, Schaaf-Gerstenschläger I, Franken E, Zimmermann FK: Lysine144 is essential for the catalytic activity of Saccharomyces cerevisiae transaldolase. Yeast 9: 1241–1249 (1993).
Pelroy RA, Rippka R, Stanier RY: Metabolism of glucose by unicellular blue-green algae. Arch Microbiol 87: 303–322 (1972).
Saitou N, Nei M: The neighbour-joining method: a new method for the reconstruction of phylogenetic trees. Mol Biol Evol 4: 406–425 (1987).
Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain termination inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).
Schaaf I, Hohmann S, Zimmermann FK: Molecular analysis of the structural gene for yeast transaldolase. Eur J Biochem 188: 597–603 (1990).
Southern EM: Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol 98: 503–517 (1975).
Summers ML, Meeks JC, Chu S, Wolf REJr: Nucleotide sequence of an operon in Nostoc sp. Strain ATCC 29133 encoding four genes of the oxidative pentose phosphate cycle. Plant Physiol 107: 267–268 (1995).
Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0–2.4 min region. Nucl Acids Res 20: 3305–3308 (1992).
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Köhler, U., Cerff, R. & Brinkmann, H. Transaldolase genes from the cyanobacteria Anabaena variabilis and Synechocystis sp. PCC 6803: comparison with other eubacterial and eukaryotic homologues. Plant Mol Biol 30, 213–218 (1996). https://doi.org/10.1007/BF00017817
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DOI: https://doi.org/10.1007/BF00017817