Gene cloning and overexpression of a geranylgeranyl diphosphate synthase of an extremely thermophilic bacterium, thermu

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 2, 1999, Pages 261-270

  Ohto, Chikara ^a,b   Ishida, Chika ^a   Koike Takeshita, Ayumi ^a   Yokoyama, Ken ^a,c   Muramatsu, Masayoshi ^a   Nishino, Tokuzo ^b   Obata, Shusei ^a  

^a TOYOTA MOTOR CORPORATION   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

^c KANAZAWA UNIVERSITY   (Japan)

Author keywords

Expression; Leader peptide; Phylogenetic tree

Indexed keywords

BACTERIAL DNA; FARNESYL TRANS TRANSFERASE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; TRANSFERASE;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; DNA PROBE; DNA SEQUENCE; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; KINETICS; MOLECULAR CLONING; MOLECULAR GENETICS; PHYLOGENY; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SOUTHERN BLOTTING; THERMUS THERMOPHILUS; THIN LAYER CHROMATOGRAPHY;

ALKYL AND ARYL TRANSFERASES; AMINO ACID SEQUENCE; BLOTTING, SOUTHERN; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, THIN LAYER; CLONING, MOLECULAR; DNA PROBES; DNA, BACTERIAL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FARNESYLTRANSTRANSFERASE; GENE EXPRESSION REGULATION, BACTERIAL; GLUTATHIONE TRANSFERASE; KINETICS; MOLECULAR SEQUENCE DATA; PHYLOGENY; POLYMERASE CHAIN REACTION; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; THERMUS THERMOPHILUS;

EID: 0033071951     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.261     Document Type: Article

References (41)

1. Bartley, G. E. and Scolnik, P. A., Molecular biology of carote-noid biosynthesis in plants. Ann. Rev. Plant Physiol. Plant Mol. Biol., 45, 287-301 (1994).
2. Casey, P. J. and Seabra, M. C., Protein prenyltransferases. J. Biol. Chem., 271, 5289-5292 (1996).
3. Zang, F. L. and Casey, P. J., Protein Prenylation. Annu. Rev. Biochem 65, 241-547 (1996).
4. Chappell, J., Biochemistry and molecular biology of the isopre-noid biosynthetic pathway in plants. Ann. Rev. Plant Physiol. Plant Mol. Biol., 46, 521-547 (1995).
5. Hedden, P. and Kamiya, Y., Gibberellin biosynthesis. Annu. Rev. Plant Physiol. Plant Mol. Biol., 48, 431-460 (1997).
6. Ohnuma, S.-i., Suzuki, ML, and Nishino, T., Archaebacterial ether-linked lipid biosynthetic gene. Expression cloning, sequencing, and characterization of geranylgeranyl-diphosphate synthase. J. Biol. Chem., 269, 14792-14797 (1994).
7. Armstrong, G. A., Alberti, M., Leach, F., and Hearst, J. E., Nucleotide sequence, organization, and nature of the protein products of the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus. Mol. Gen. Genet., 216, 254-268 (1989).
8. Misawa, N., Nakagawa, M., Kobayashi, K., Yamano, S., Izawa, Y., Nakamura, K., and Harashima, K., Elucidation of the Er-winia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli. J. Bac-teriol., 172, 6704-6712 (1990).
9. Math, S. K., Hearst, J. E., and Poulter, C. D., The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate synthase. Proc. Natl. Acad. Sci. U.S.A., 89, 6761-6764 (1992).
10. Carattoli, A., Romano, N., Ballario, P., Morelli, G., and Macino, G., The Neurospora crassa carotenoid biosynthetic gene (albino 3) reveals highly conserved regions among prenyltransferases. J. Biol. Chem., 266, 5854-5859 (1991).
11. Jiang, Y., Proteau, P., Poulter, D., and Ferro-Novick, S., BTS1 encodes a geranylgeranyl diphosphate synthase in Sac-charomyces cerevisiae. J. Biol. Chem., 270, 21793-21799 (1995).
12. Michalowski, C. B., Lofelhardt, W., and Bohnert, H. J., An ORF323 with homology to crtE, specifying prephytoene pyrophosphate dehydrogenase, is encoded by cyanelle DNA in the eukaryotic alga Cyanophora paradoxa. J. Biol. Chem., 266, 11866-11870 (1991).
13. Kuntz, M., Romer, S., Suire, C., Hugueney, P., Weil, J. H., Schantz, R., and Camara, B., Identification of a cDNA for the plastid-located geranylgeranyl pyrophosphate synthase from Capsicum annuum: correlative increase in enzyme activity and transcript level during fruit ripening. Plant J., 2, 25-34 (1992).
14. Zhu, X., Suzuki, K., Okada, K., Tanaka, K., Nakagawa, T., Kawamukai, M., and Matsuda, K., Cloning and functional expression of a novel geranylgeranyl yrophosphate synthase gene from Arabidopsis thaliana in Escherichia coli. Plant Cell Physiol, 38, 357-361 (1997).
15. Aitken, S. M., Attucci, S., Ibrahim, R. K., and Gulick, P. J., A cDNA encoding geranylgeranyl pyrophosphate synthase from white lupin. Plant Physiol., 108, 837-838 (1995).
16. Ohto, C., Nakane, H., Hemmi, H., Ohnuma, S.-i., Obata, S., and Nishino, T., Overexpression of an archaeal geranylgeranyl diphosphate synthase in Escherichia coli cells. Biosci. Biotechnol. Biochem., 62, 1243-1246 (1998).
17. Wiedemann, M., Misawa, N., and Sandmann, G., Purification and enzymatic characterization of the geranylgeranyl pyrophosphate synthase from Erwinia uredovora after expression in Escherichia coli. Arch Biochem Biophys, 306, 152-7 (1993).
18. Tachibana, A., Tanaka, T., Taniguchi, M., and Oi, S., Purification and characterization of geranylgeranyl diphosphate synthase from Methanobacterium thermoformicicum SF-4. Biosci. Biotechnol Biochem., 57, 1129-1133 (1993).
19. Koyama, T., Saito, K., Ogura, K., Obata, S., and Takeshita, A., Site-directed mutagenesis of farnesyl diphosphate synthase effect of substitution on the three carboxyl-terminal amino acids. Can. J. Chem., 72, 75-79 (1994).
20. Oshima, T. and Imahori, K., Description of Thermus thermophilus (Yoshida and Oshima) comb, nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa. Int. J. Syst. Bacteriol, 24, 102-112 (1974).
21. Hoshino, T., Juii, R., and Nakahara, T., Molecular cloning and sequence analysis of the crfB gene of Thermus thermophilus HB27, an extreme thermophile producing carotenoid pigments. Appl. Environ. Microbiol., 59, 3150-3153 (1993).
22. Tabata, K., Ishida, S., Nakahara, T., and Hoshino, T., A carotenogenic gene cluster exists on a large plasmid in Thermus thermophilus. FEBS Lett., 341, 251-255 (1994).
23. Ishida, M. and Oshima, T., A leader open reading frame is essential for the expression in Escherichia coli of GC-rich leuB gene of an extreme thermophile, Thermus thermophilus. FEMS Microbiol. Lett., 135, 137-142 (1996).
24. Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, (1989).
25. Thompson, J.D., Higgins, D.G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nuc. Acid Res., 22, 4673-4680 (1994).
26. Kyte, J. and Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132 (1982).
27. Smith, D. B. and Corcoran, L. M., Expression and purification of glutathione-S-transferase fusion proteins. In “Current Protocols in Molecular Biology”, eds. F. M. Ausubel, et ah, John Wiley & Sons, New York, pp. 16.7.1-16.7.8 (1991).
28. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
29. Koyama, T., Obata, S., Osabe, M., Takeshita, A., Yokoyama, K., Uchida, M., Nishino, T., and Ogura, K., Thermostable far-nesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification. J. Biochem. (Tokyo), 113, 355-363 (1993).
30. Koyama, T., Fujii, H., and Ogura, K., Enzymatic hydrolysis of polyprenyl pyrophosphates. Methods Enzymol., 110, 153-155 (1985).
31. Chen, A., Kroon, P. A., and Poulter, C. D., Isoprenyl diphosphate synthases: protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure. Protein Sci., 3, 600-607 (1994).
32. Koyama, T., Tajima, M., Sano, H., Doi, T., Koike-Takeshita, A., Obata, S., Nishino, T., and Ogura, K., Identification of significant residues in the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase. Biochemistry, 35, 9533-9538 (1996).
33. Tarshis, L., Proteau, P., Kellogg, B., Sacchettini, J., and Poulter, C., Regulation of product chain length by isoprenyl diphosphate synthases. Proc. Natl. Acad. Sci. U.S.A., 93, 15018-15023 (1996).
34. Ohnuma, S.-i., Narita, K., Nakazawa, T., Ishida, C., Takeuchi, Y., Ohto, C., and Nishino, T., A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J. Biol. Chem., 271, 30748-30754 (1996).
35. Ohnuma, S.-i., Hirooka, K., Ohto, C., and Nishino, T., Conversion from archaeal geranylgeranyl diphosphate synthase to farnesyl diphosphate synthase. Two amino acids before the first aspartate-rich motif solely determine eukaryotic farnesyl diphosphate synthase activity. J. Biol. Chem., 272, 5192-5198 (1997).
36. Tarshis, L. C., Yan, M., Poulter, C. D., and Sacchettini, J. C., Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution. Biochemistry, 33, 10871-7 (1994).
37. Sagami, H., Morita, Y., and Ogura, K., Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain. J. Biol. Chem., 269, 20561-20566 (1994).
38. Fujisaki, S., Hara, H., Nishimura, Y., Horiuchi, K., and Nishino, T., Cloning and nucleotide sequence of the ispA gene responsible for farnesyl diphosphate synthase activity in Escherichia coli. J. Biochem. (Tokyo), 108, (1990).
39. Kaneko, T., et al., Sequence analysis of the genome of the unicellular Cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res., 3, 109-136 (1996).
40. Okada, K., Minehira, M., Zhu, X., Suzuki, K., Nakagawa, T., Matsuda, H., and Kawamukai, M., The ispB gene encoding oc-taprenyl diphosphate synthase is essential for growth of Escherichia coli. J. Bacteriol., 179, 3058-3060 (1997).
41. Asai, K., Fujisaki, S., Nishimura, Y., Nishino, T., Okada, K., Nakagawa, T., Kawamukai, M., and Matsuda, H., The identification of Escherichia coli ispB (cel) gene encoding the oc-taprenyl diphosphate synthase. Biochem. Biophys. Res. Com-mun., 202, 340-345 (1994).