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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

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  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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