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. 1990 Aug;58(8):2452–2458. doi: 10.1128/iai.58.8.2452-2458.1990

Analysis of the Streptococcus downei gtfS gene, which specifies a glucosyltransferase that synthesizes soluble glucans.

K S Gilmore 1, R R Russell 1, J J Ferretti 1
PMCID: PMC258840  PMID: 2142479

Abstract

The complete nucleotide sequence was determined for the Streptococcus downei (previously Streptococcus sobrinus) MFe28 gtfS gene which specifies a glucosyltransferase (GTF-S) producing water-soluble glucan. A single open reading frame which encodes a mature protein with a molecular weight of 147,408 (1,328 amino acids) and a putative signal peptide 36 or 37 amino acids in length was detected. GTF-S shares extensive sequence similarity with GTF-I (gtfI) from S. downei and GTF-I (gtfB) and GTF-SI (gtfC) from Streptococcus mutans. GTF-S contains a highly conserved enzymatic domain and C-terminal repeated sequences which appear to be involved in glucan binding. Comparison of the deduced GTF-S protein sequence with other sequenced GTF genes of mutans streptococci revealed that these C-terminal repeats occurred in all cases, although the patterns of repeated sequences varied with respect to each other and to the glucan-binding protein of S. mutans. GTF-S contains four C-terminal repeat sequences ranging from 49 to 51 amino acids in length and a partial repeat of 13 amino acids. Nuclear magnetic resonance analysis of the glucan produced by GTF-S revealed that the product consisted of more than 90% alpha-1,6-linked glucosyl residues.

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Selected References

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

  1. Banas J. A., Russell R. R., Ferretti J. J. Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt. Infect Immun. 1990 Mar;58(3):667–673. doi: 10.1128/iai.58.3.667-673.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Colson P., Jennings H. J., Smith I. C. Composition, sequence, and conformation of polymers and oligomers of glucose as revealed by carbon-13 nuclear magentic resonance. J Am Chem Soc. 1974 Dec 25;96(26):8081–8087. doi: 10.1021/ja00833a038. [DOI] [PubMed] [Google Scholar]
  3. Ferretti J. J., Gilpin M. L., Russell R. R. Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus MFe28. J Bacteriol. 1987 Sep;169(9):4271–4278. doi: 10.1128/jb.169.9.4271-4278.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Furuta T., Koga T., Nisizawa T., Okahashi N., Hamada S. Purification and characterization of glucosyltransferases from Streptococcus mutans 6715. J Gen Microbiol. 1985 Feb;131(2):285–293. doi: 10.1099/00221287-131-2-285. [DOI] [PubMed] [Google Scholar]
  5. García E., García J. L., García P., Arrarás A., Sánchez-Puelles J. M., López R. Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Proc Natl Acad Sci U S A. 1988 Feb;85(3):914–918. doi: 10.1073/pnas.85.3.914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gilpin M. L., Russell R. R., Morrissey P. Cloning and expression of two Streptococcus mutans glucosyltransferases in Escherichia coli K-12. Infect Immun. 1985 Aug;49(2):414–416. doi: 10.1128/iai.49.2.414-416.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hamada S., Slade H. D. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol Rev. 1980 Jun;44(2):331–384. doi: 10.1128/mr.44.2.331-384.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hanada N., Kuramitsu H. K. Isolation and characterization of the Streptococcus mutans gtfD gene, coding for primer-dependent soluble glucan synthesis. Infect Immun. 1989 Jul;57(7):2079–2085. doi: 10.1128/iai.57.7.2079-2085.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Heath D. G., Cleary P. P. Fc-receptor and M-protein genes of group A streptococci are products of gene duplication. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4741–4745. doi: 10.1073/pnas.86.12.4741. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Henikoff S. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene. 1984 Jun;28(3):351–359. doi: 10.1016/0378-1119(84)90153-7. [DOI] [PubMed] [Google Scholar]
  11. Loenen W. A., Brammar W. J. A bacteriophage lambda vector for cloning large DNA fragments made with several restriction enzymes. Gene. 1980 Aug;10(3):249–259. doi: 10.1016/0378-1119(80)90054-2. [DOI] [PubMed] [Google Scholar]
  12. Loesche W. J. Role of Streptococcus mutans in human dental decay. Microbiol Rev. 1986 Dec;50(4):353–380. doi: 10.1128/mr.50.4.353-380.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mooser G., Wong C. Isolation of a glucan-binding domain of glucosyltransferase (1,6-alpha-glucan synthase) from Streptococcus sobrinus. Infect Immun. 1988 Apr;56(4):880–884. doi: 10.1128/iai.56.4.880-884.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Müller-Hill B., Crapo L., Gilbert W. Mutants that make more lac repressor. Proc Natl Acad Sci U S A. 1968 Apr;59(4):1259–1264. doi: 10.1073/pnas.59.4.1259. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Russell R. R., Gilpin M. L., Mukasa H., Dougan G. Characterization of glucosyltransferase expressed from a Streptococcus sobrinus gene cloned in Escherichia coli. J Gen Microbiol. 1987 Apr;133(4):935–944. doi: 10.1099/00221287-133-4-935. [DOI] [PubMed] [Google Scholar]
  16. Shimamura A., Tsumori H., Mukasa H. Three kinds of extracellular glucosyltransferases from Streptococcus mutans 6715 (serotype g). FEBS Lett. 1983 Jun 27;157(1):79–84. doi: 10.1016/0014-5793(83)81120-x. [DOI] [PubMed] [Google Scholar]
  17. Shiroza T., Kuramitsu H. K. Sequence analysis of the Streptococcus mutans fructosyltransferase gene and flanking regions. J Bacteriol. 1988 Feb;170(2):810–816. doi: 10.1128/jb.170.2.810-816.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Shiroza T., Ueda S., Kuramitsu H. K. Sequence analysis of the gtfB gene from Streptococcus mutans. J Bacteriol. 1987 Sep;169(9):4263–4270. doi: 10.1128/jb.169.9.4263-4270.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Tabor S., Richardson C. C. DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc Natl Acad Sci U S A. 1987 Jul;84(14):4767–4771. doi: 10.1073/pnas.84.14.4767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ueda S., Shiroza T., Kuramitsu H. K. Sequence analysis of the gtfC gene from Streptococcus mutans GS-5. Gene. 1988 Sep 15;69(1):101–109. doi: 10.1016/0378-1119(88)90382-4. [DOI] [PubMed] [Google Scholar]
  21. Yamashita Y., Hanada N., Takehara T. Purification of a fourth glucosyltransferase from Streptococcus sobrinus. J Bacteriol. 1989 Nov;171(11):6265–6270. doi: 10.1128/jb.171.11.6265-6270.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]
  23. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

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