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. 1994 Dec;176(24):7730–7734. doi: 10.1128/jb.176.24.7730-7734.1994

Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6.

A Iwai 1, H Ito 1, T Mizuno 1, H Mori 1, H Matsui 1, M Honma 1, G Okada 1, S Chiba 1
PMCID: PMC197233  PMID: 8002600

Abstract

The gene encoding an extracellular isomalto-dextranase, designated imd, was isolated from the chromosomal DNA of Arthrobacter globiformis T6 and cloned and expressed in Escherichia coli. A single open reading frame consisting of 1,926 base pairs that encoded a polypeptide composed of a signal peptide of 39 amino acids and a mature protein of 602 amino acids (M(r), 65,900) was found. The primary structure had no significant homology with the structures of any other reported carbohydrases, including two other dextranases. Transformed E. coli cells carrying the 2.3-kb fragment overproduced isomalto-dextranase into the periplasmic space under control of the promoter of the imd gene itself.

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Selected References

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

  1. Amann E., Ochs B., Abel K. J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene. 1988 Sep 30;69(2):301–315. doi: 10.1016/0378-1119(88)90440-4. [DOI] [PubMed] [Google Scholar]
  2. BAILEY R. W., CLARKE R. T. A bacterial dextranase. Biochem J. 1959 May;72(1):49–54. doi: 10.1042/bj0720049. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brooks J. E., Blumenthal R. M., Gingeras T. R. The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene. Nucleic Acids Res. 1983 Feb 11;11(3):837–851. doi: 10.1093/nar/11.3.837. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Ebisu S., Misaki A., Kato K., Kotani S. The structure of water-insoluble glucans of cariogenic Streptococcus mutans, formed in the absence and presence of dextranase. Carbohydr Res. 1974 Dec;38:374–381. doi: 10.1016/s0008-6215(00)82375-7. [DOI] [PubMed] [Google Scholar]
  5. Frischauf A. M., Lehrach H., Poustka A., Murray N. Lambda replacement vectors carrying polylinker sequences. J Mol Biol. 1983 Nov 15;170(4):827–842. doi: 10.1016/s0022-2836(83)80190-9. [DOI] [PubMed] [Google Scholar]
  6. Hiraoka N., Fukumoto J., Tsuru D. Studies on mold dextranases. 3. Purification and some enzymatic properties of Aspergillus carneus dextranase. J Biochem. 1972 Jan;71(1):57–64. doi: 10.1093/oxfordjournals.jbchem.a129746. [DOI] [PubMed] [Google Scholar]
  7. Koshland D., Botstein D. Secretion of beta-lactamase requires the carboxy end of the protein. Cell. 1980 Jul;20(3):749–760. doi: 10.1016/0092-8674(80)90321-9. [DOI] [PubMed] [Google Scholar]
  8. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  9. Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem. 1987 Jul 25;262(21):10035–10038. [PubMed] [Google Scholar]
  10. Okushima M., Sugino D., Kouno Y., Nakano S., Miyahara J., Toda H., Kubo S., Matsushiro A. Molecular cloning and nucleotide sequencing of the Arthrobacter dextranase gene and its expression in Escherichia coli and Streptococcus sanguis. Jpn J Genet. 1991 Apr;66(2):173–187. doi: 10.1266/jjg.66.173. [DOI] [PubMed] [Google Scholar]
  11. Overbeeke N., Fellinger A. J., Toonen M. Y., van Wassenaar D., Verrips C. T. Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar). Plant Mol Biol. 1989 Nov;13(5):541–550. doi: 10.1007/BF00027314. [DOI] [PubMed] [Google Scholar]
  12. Richards G. N., Streamer M. Studies on dextranases. IV. Mode of action of dextranase D1 on oligosaccharides. Carbohydr Res. 1974 Feb;32(2):251–260. doi: 10.1016/s0008-6215(00)82103-5. [DOI] [PubMed] [Google Scholar]
  13. Russell R. R., Ferretti J. J. Nucleotide sequence of the dextran glucosidase (dexB) gene of Streptococcus mutans. J Gen Microbiol. 1990 May;136(5):803–810. doi: 10.1099/00221287-136-5-803. [DOI] [PubMed] [Google Scholar]
  14. SERY T. W., HEHRE E. J. Degradation of dextrans by enzymes of intestinal bacteria. J Bacteriol. 1956 Mar;71(3):373–380. doi: 10.1128/jb.71.3.373-380.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. SMOGYI M. Notes on sugar determination. J Biol Chem. 1952 Mar;195(1):19–23. [PubMed] [Google Scholar]
  16. 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]
  17. Sawai T., Toriyama K., Yano K. A bacterial dextranase releasing only isomaltose from dextrans. J Biochem. 1974 Jan;75(1):105–112. doi: 10.1093/oxfordjournals.jbchem.a130363. [DOI] [PubMed] [Google Scholar]
  18. Sugiura M., Ito A., Yamaguchi T. Studies on dextranase. II. New exo-dextranase from Brevibacterium fuscum var. Dextranlyticum. Biochim Biophys Acta. 1974 May 20;350(1):61–70. doi: 10.1016/0005-2744(74)90203-4. [DOI] [PubMed] [Google Scholar]
  19. Svensson B. Regional distant sequence homology between amylases, alpha-glucosidases and transglucanosylases. FEBS Lett. 1988 Mar 28;230(1-2):72–76. doi: 10.1016/0014-5793(88)80644-6. [DOI] [PubMed] [Google Scholar]
  20. TSUCHIYA H. M., JEANES A., BRICKER H. M., WILHAM C. A. Dextran-degrading enzymes from molds. J Bacteriol. 1952 Oct;64(4):513–519. doi: 10.1128/jb.64.4.513-519.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tonozuka T., Ohtsuka M., Mogi S., Sakai H., Ohta T., Sakano Y. A neopullulanase-type alpha-amylase gene from Thermoactinomyces vulgaris R-47. Biosci Biotechnol Biochem. 1993 Mar;57(3):395–401. doi: 10.1271/bbb.57.395. [DOI] [PubMed] [Google Scholar]
  22. Torii M., Sakakibara K., Misaki A., Sawai T. Degradation of alpha-linked D-gluco-oligosaccharides and dextrans by an isomalto-dextranase preparation from Arthrobacter globiformis T6. Biochem Biophys Res Commun. 1976 May 17;70(2):459–464. doi: 10.1016/0006-291x(76)91068-8. [DOI] [PubMed] [Google Scholar]
  23. 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]
  24. Waley S. G. A spectrophotometric assay of beta-lactamase action on penicillins. Biochem J. 1974 Jun;139(3):789–790. doi: 10.1042/bj1390789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. de Boer H. A., Comstock L. J., Vasser M. The tac promoter: a functional hybrid derived from the trp and lac promoters. Proc Natl Acad Sci U S A. 1983 Jan;80(1):21–25. doi: 10.1073/pnas.80.1.21. [DOI] [PMC free article] [PubMed] [Google Scholar]

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