DNA sequence of the glucosyltransferase gene of serotype d<i>Streptococcus sobrinus</i>

Sato, Setsuko; Inoue, Masakazu; Hanada, Nobuhiro; Aizawa, Yuzuru; Isobe, Yutaka; Katayama, Tsuyoshi

doi:10.3109/10425179309015618

Cited by 12 publications

(9 citation statements)

References 21 publications

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“…that of S. sobrinus 6715. The first 38 amino acids contained the signal sequence of GTF proteins, and these amino acids were similar to those by previously reported GTFs (Ferretti et al, 1987;Shiroza et al, 1987;Abo et al, 1991;Sato et al, 1993). Then, Mooser et al (1991) reported the putative active-site sequence (DSIRDAVD) from GTF-I enzyme of S. sobrinus 6715, and the corresponding sequence was identified in the amino acid sequence of S. orisuis JCM14035.…”

Section: (A ) (B)mentioning

confidence: 69%

Sequence and phylogenetic analyses of novel glucosyltransferase genes of mutans streptococci isolated from pig oral cavity

2008

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Nucleotide sequences of water-insoluble glucan-producing glucosyltransferase (gtf) genes of new mutans streptococci isolated from pig oral cavity, Streptococcus orisuis JCM14035, and of Streptococcus criceti HS-6 were determined. The gtf gene of S. orisuis JCM14035 consisted of a 4,401 bp ORF encoding for a 1,466 amino acids, and was revealed to belong to the gtfI group. The percent homology of amino acid sequence of the GTF-I from S. orisuis and S. criceti are 95.0%, however, this score ranges from 77.0% to 78.0% when compared to Streptococcus sobrinus 6715. The deduced N-terminal amino acid sequence was considered responsible for the secretion of GTF-I in S. orisuis JCM14035 and S. criceti HS-6 with high similarity to known GTF proteins from other streptococci. In addition, two other conserved regions, i.e., N-terminal putative catalytic-site and C-terminal glucan binding domain, were also found in GTF-Is of S. orisuis JCM14035 and S. criceti HS-6. Phylogenetic analysis suggested that S. orisuis JCM14035 and S. criceti HS-6, closely related to each other, resemble S. sobrinus and S. downei based on the amino acid sequences of the GTFs.

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Section: (A ) (B)mentioning

confidence: 69%

Sequence and phylogenetic analyses of novel glucosyltransferase genes of mutans streptococci isolated from pig oral cavity

2008

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“…Studies initiated more than 10 years ago allowed the isolation and sequencing of 17 genes coding for glucansucrases produced by oral streptococci involved in the cariogenesis process, S. mutans GS5 or LM7, S. sobrinus serotype h ( S. downei Mfe28), serotype g ( S. sobrinus 6715), serotype d ( S. sobrinus OMZ176), by S. salivarius ATCC 25975 and by L. mesenteroides NRRL B‐512F and B‐1299 (Table 1) [12–36]. Isolated glucansucrases are all large enzymes with an average M r of 160 000.…”

Section: Structural and Functional Organisation Of The Glucansucrasesmentioning

confidence: 99%

“…Isolated glucansucrases are all large enzymes with an average M r of 160 000. Streptococci glucansucrases synthesise primarily α(1–3) rich mutan polysaccharides and α(1–6) rich dextran polysaccharides [12–33]. L. mesenteroides glucansucrases produce α(1–6) rich dextrans [34–36, 84].…”

Section: Structural and Functional Organisation Of The Glucansucrasesmentioning

confidence: 99%

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Glucansucrases: mechanism of action and structure–function relationships

1999

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Glucansucrases are produced principally by Leuconostoc mesenteroides and oral Streptococcus species, but also by the lactic acid bacteria (Lactococci, Lactobacilli). They catalyse the synthesis of high molecular weight D-glucose polymers, named glucans, from sucrose. In the presence of efficient acceptors, they catalyse the synthesis of low molecular weight oligosaccharides. Glucosidic bond synthesis occurs without the mediation of nucleotide activated sugars and cofactors are not necessary. Glucansucrases have an industrial value because of the production of dextrans and oligosaccharides and a biological importance by their key role in the cariogenic process. They were identified more than 50 years ago. The first glucansucrase encoding gene was cloned more than 10 years ago. But the mechanism of their action remains incompletely understood. However, in order to synthesise oligosaccharides of biological interest or to develop vaccines against dental caries, elucidation of the factors determining the regiospecificity and the regioselectivity of glucansucrases is necessary. The cloning of glucansucrase encoding genes in addition to structure-function relationship studies have allowed the identification of important amino acid residues and have shown that glucansucrases are composed of two functional domains: a core region (ca. 1000 amino acids) involved in sucrose binding and splitting and a C-terminal domain (ca. 500 amino acids) composed of a series of tandem repeats involved in glucan binding. Enzymology studies have enabled different models for their action mechanism to be proposed. The use of secondary structure prediction has led to a clearer knowledge of structure-function relationships of glucansucrases. However, mainly due to the large size of these enzymes, data on the three-dimensional structure of glucansucrases (given by crystallography and modelling) remain necessary to clearly identify those features which determine function.

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“…Despite the significant ecological roles of GTF enzymes and their glucan products, little is known about their regulation. The mutans streptococci and Streptococcus salivarius have multiple GTF enzymes coded for by multiple gtf genes (3,8,9,12,24,25,30). No genetic regulatory mechanisms for these gtf genes have been described.…”

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confidence: 99%

Oral streptococci with genetic determinants similar to the glucosyltransferase regulatory gene, rgg

1995

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The Streptococcus gordonii Challis glucosyltransferase structural gene, gtfG, is positively regulated by the upstream gene, rgg, the only described gtf regulatory determinant in oral streptococci. Southern hybridization analyses indicated that rgg-like and gtfG-like determinants were present on the same HindIII fragment in strains of S. gordonii, Streptococcus sanguis, and Streptococcus oralis, whereas no rgg-like determinants were detected in mutans streptococci, Streptococcus mitis, and Streptococcus salivarius.

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DNA sequence of the glucosyltransferase gene of serotype dStreptococcus sobrinus

Cited by 12 publications

References 21 publications

Sequence and phylogenetic analyses of novel glucosyltransferase genes of mutans streptococci isolated from pig oral cavity

Sequence and phylogenetic analyses of novel glucosyltransferase genes of mutans streptococci isolated from pig oral cavity

Glucansucrases: mechanism of action and structure–function relationships

Oral streptococci with genetic determinants similar to the glucosyltransferase regulatory gene, rgg

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