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Biotechnology Information s. mutans luxs protein
Alignment of the S. <t>mutans</t> <t>LuxS</t> protein and several other representative LuxS proteins. Residues that coordinate a Zn2+ ion and comprise the catalytic center of LuxS (H, H, and C) are printed in bold. 1, V. harveyi; 2, S. mutans; 3, E. coli; 4, S. pyogenes; 5, B. subtilis.
S. Mutans Luxs Protein, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans

Journal:

doi: 10.1128/IAI.71.4.1972-1979.2003

Alignment of the S. mutans LuxS protein and several other representative LuxS proteins. Residues that coordinate a Zn2+ ion and comprise the catalytic center of LuxS (H, H, and C) are printed in bold. 1, V. harveyi; 2, S. mutans; 3, E. coli; 4, S. pyogenes; 5, B. subtilis.
Figure Legend Snippet: Alignment of the S. mutans LuxS protein and several other representative LuxS proteins. Residues that coordinate a Zn2+ ion and comprise the catalytic center of LuxS (H, H, and C) are printed in bold. 1, V. harveyi; 2, S. mutans; 3, E. coli; 4, S. pyogenes; 5, B. subtilis.

Techniques Used:

S. mutans luxS complements a frameshift mutation in E. coli DH5α. E. coli DH5α was transformed with an E. coli-S. mutans shuttle vector containing an intact copy of the S. mutans luxS gene (pLuxSm). This strain was examined for AI-2 production using the luminescence-based AI-2 reporter assay. V. harveyi strain BB170 (sensor 1−, sensor 2+) served as a positive control, while E. coli DH5α served as a negative control. Luminescence is expressed as fold induction relative to the background values.
Figure Legend Snippet: S. mutans luxS complements a frameshift mutation in E. coli DH5α. E. coli DH5α was transformed with an E. coli-S. mutans shuttle vector containing an intact copy of the S. mutans luxS gene (pLuxSm). This strain was examined for AI-2 production using the luminescence-based AI-2 reporter assay. V. harveyi strain BB170 (sensor 1−, sensor 2+) served as a positive control, while E. coli DH5α served as a negative control. Luminescence is expressed as fold induction relative to the background values.

Techniques Used: Mutagenesis, Transformation Assay, Plasmid Preparation, Reporter Assay, Positive Control, Negative Control

AI-2 induction in the presence or absence of sugar. S. mutans was grown and assayed as described in Materials and Methods. Cells were grown overnight and resuspended to an OD600 of 0.4 in reporter assay (AB) medium and incubated with aeration for 3 h at 37°C. One sample was incubated in AB alone, while for the other, sucrose was added to a final concentration of 1%. The presence of sucrose in the medium caused a potent reduction in luminescence to below background values.
Figure Legend Snippet: AI-2 induction in the presence or absence of sugar. S. mutans was grown and assayed as described in Materials and Methods. Cells were grown overnight and resuspended to an OD600 of 0.4 in reporter assay (AB) medium and incubated with aeration for 3 h at 37°C. One sample was incubated in AB alone, while for the other, sucrose was added to a final concentration of 1%. The presence of sucrose in the medium caused a potent reduction in luminescence to below background values.

Techniques Used: Reporter Assay, Incubation, Concentration Assay

luxS knockout in S. mutans. (A) Illustration of the knockout procedure. Plasmids containing cloned fragments of S. mutans DNA as well as the erythromycin cassette were cut using the indicated restriction sites and then ligated into a linearized pUC19 backbone. The resulting construct was linearized with the unique AatII site and transformed into S. mutans for double crossover. (B) Confirmation of crossover event. In lanes 1 to 4, wild-type DNA was amplified with primers: internal to luxS, the erythromycin cassette, upstream external luxS plus erythromycin, or downstream external luxS plus erythromycin. In lanes 5 to 8, luxS mutant DNA was amplified using the same primer combinations. External luxS primers bind to sites that were not subject to crossover. (C) AI-2 production was assayed to confirm that activity was lost in the mutant.
Figure Legend Snippet: luxS knockout in S. mutans. (A) Illustration of the knockout procedure. Plasmids containing cloned fragments of S. mutans DNA as well as the erythromycin cassette were cut using the indicated restriction sites and then ligated into a linearized pUC19 backbone. The resulting construct was linearized with the unique AatII site and transformed into S. mutans for double crossover. (B) Confirmation of crossover event. In lanes 1 to 4, wild-type DNA was amplified with primers: internal to luxS, the erythromycin cassette, upstream external luxS plus erythromycin, or downstream external luxS plus erythromycin. In lanes 5 to 8, luxS mutant DNA was amplified using the same primer combinations. External luxS primers bind to sites that were not subject to crossover. (C) AI-2 production was assayed to confirm that activity was lost in the mutant.

Techniques Used: Knock-Out, Clone Assay, Construct, Transformation Assay, Amplification, Mutagenesis, Activity Assay

Mutation of luxS causes an alteration in S. mutans biofilm. (A) Two images of in vitro biofilms representing both the wild type and the mutant using dark-field microscopy at magnifications ×20 and ×40. Cells were grown on glass coverslips as described in Materials and Methods. Similar results were obtained for more than 100 independent wild-type and luxS mutant biofilms examined. (B) Biofilms were tested for their ability to resist detergent treatment with SDS. Three samples of wild-type and mutant biofilms grown on glass coverslips were shaken at 150 rpm for 1 h. The OD600s of the resulting supernatants were compared.
Figure Legend Snippet: Mutation of luxS causes an alteration in S. mutans biofilm. (A) Two images of in vitro biofilms representing both the wild type and the mutant using dark-field microscopy at magnifications ×20 and ×40. Cells were grown on glass coverslips as described in Materials and Methods. Similar results were obtained for more than 100 independent wild-type and luxS mutant biofilms examined. (B) Biofilms were tested for their ability to resist detergent treatment with SDS. Three samples of wild-type and mutant biofilms grown on glass coverslips were shaken at 150 rpm for 1 h. The OD600s of the resulting supernatants were compared.

Techniques Used: Mutagenesis, In Vitro, Microscopy

Related Articles

Mutagenesis:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Transformation Assay:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Plasmid Preparation:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Reporter Assay:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Positive Control:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Negative Control:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Incubation:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Concentration Assay:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Knock-Out:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Clone Assay:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Construct:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Amplification:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Activity Assay:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

In Vitro:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.

Microscopy:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans
Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli.



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Biotechnology Information s. mutans luxs protein
Alignment of the S. <t>mutans</t> <t>LuxS</t> protein and several other representative LuxS proteins. Residues that coordinate a Zn2+ ion and comprise the catalytic center of LuxS (H, H, and C) are printed in bold. 1, V. harveyi; 2, S. mutans; 3, E. coli; 4, S. pyogenes; 5, B. subtilis.
S. Mutans Luxs Protein, supplied by Biotechnology Information, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/s%2E+mutans+luxs+protein/s++mutans+luxs+protein/pmc00152054-345-4-22
Average 90 stars, based on 1 article reviews
s. mutans luxs protein - by Bioz Stars, 2026-09
90/100 stars
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Alignment of the S. mutans LuxS protein and several other representative LuxS proteins. Residues that coordinate a Zn2+ ion and comprise the catalytic center of LuxS (H, H, and C) are printed in bold. 1, V. harveyi; 2, S. mutans; 3, E. coli; 4, S. pyogenes; 5, B. subtilis.

Journal:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans

doi: 10.1128/IAI.71.4.1972-1979.2003

Figure Lengend Snippet: Alignment of the S. mutans LuxS protein and several other representative LuxS proteins. Residues that coordinate a Zn2+ ion and comprise the catalytic center of LuxS (H, H, and C) are printed in bold. 1, V. harveyi; 2, S. mutans; 3, E. coli; 4, S. pyogenes; 5, B. subtilis.

Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Techniques:

S. mutans luxS complements a frameshift mutation in E. coli DH5α. E. coli DH5α was transformed with an E. coli-S. mutans shuttle vector containing an intact copy of the S. mutans luxS gene (pLuxSm). This strain was examined for AI-2 production using the luminescence-based AI-2 reporter assay. V. harveyi strain BB170 (sensor 1−, sensor 2+) served as a positive control, while E. coli DH5α served as a negative control. Luminescence is expressed as fold induction relative to the background values.

Journal:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans

doi: 10.1128/IAI.71.4.1972-1979.2003

Figure Lengend Snippet: S. mutans luxS complements a frameshift mutation in E. coli DH5α. E. coli DH5α was transformed with an E. coli-S. mutans shuttle vector containing an intact copy of the S. mutans luxS gene (pLuxSm). This strain was examined for AI-2 production using the luminescence-based AI-2 reporter assay. V. harveyi strain BB170 (sensor 1−, sensor 2+) served as a positive control, while E. coli DH5α served as a negative control. Luminescence is expressed as fold induction relative to the background values.

Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Techniques: Mutagenesis, Transformation Assay, Plasmid Preparation, Reporter Assay, Positive Control, Negative Control

AI-2 induction in the presence or absence of sugar. S. mutans was grown and assayed as described in Materials and Methods. Cells were grown overnight and resuspended to an OD600 of 0.4 in reporter assay (AB) medium and incubated with aeration for 3 h at 37°C. One sample was incubated in AB alone, while for the other, sucrose was added to a final concentration of 1%. The presence of sucrose in the medium caused a potent reduction in luminescence to below background values.

Journal:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans

doi: 10.1128/IAI.71.4.1972-1979.2003

Figure Lengend Snippet: AI-2 induction in the presence or absence of sugar. S. mutans was grown and assayed as described in Materials and Methods. Cells were grown overnight and resuspended to an OD600 of 0.4 in reporter assay (AB) medium and incubated with aeration for 3 h at 37°C. One sample was incubated in AB alone, while for the other, sucrose was added to a final concentration of 1%. The presence of sucrose in the medium caused a potent reduction in luminescence to below background values.

Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Techniques: Reporter Assay, Incubation, Concentration Assay

luxS knockout in S. mutans. (A) Illustration of the knockout procedure. Plasmids containing cloned fragments of S. mutans DNA as well as the erythromycin cassette were cut using the indicated restriction sites and then ligated into a linearized pUC19 backbone. The resulting construct was linearized with the unique AatII site and transformed into S. mutans for double crossover. (B) Confirmation of crossover event. In lanes 1 to 4, wild-type DNA was amplified with primers: internal to luxS, the erythromycin cassette, upstream external luxS plus erythromycin, or downstream external luxS plus erythromycin. In lanes 5 to 8, luxS mutant DNA was amplified using the same primer combinations. External luxS primers bind to sites that were not subject to crossover. (C) AI-2 production was assayed to confirm that activity was lost in the mutant.

Journal:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans

doi: 10.1128/IAI.71.4.1972-1979.2003

Figure Lengend Snippet: luxS knockout in S. mutans. (A) Illustration of the knockout procedure. Plasmids containing cloned fragments of S. mutans DNA as well as the erythromycin cassette were cut using the indicated restriction sites and then ligated into a linearized pUC19 backbone. The resulting construct was linearized with the unique AatII site and transformed into S. mutans for double crossover. (B) Confirmation of crossover event. In lanes 1 to 4, wild-type DNA was amplified with primers: internal to luxS, the erythromycin cassette, upstream external luxS plus erythromycin, or downstream external luxS plus erythromycin. In lanes 5 to 8, luxS mutant DNA was amplified using the same primer combinations. External luxS primers bind to sites that were not subject to crossover. (C) AI-2 production was assayed to confirm that activity was lost in the mutant.

Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Techniques: Knock-Out, Clone Assay, Construct, Transformation Assay, Amplification, Mutagenesis, Activity Assay

Mutation of luxS causes an alteration in S. mutans biofilm. (A) Two images of in vitro biofilms representing both the wild type and the mutant using dark-field microscopy at magnifications ×20 and ×40. Cells were grown on glass coverslips as described in Materials and Methods. Similar results were obtained for more than 100 independent wild-type and luxS mutant biofilms examined. (B) Biofilms were tested for their ability to resist detergent treatment with SDS. Three samples of wild-type and mutant biofilms grown on glass coverslips were shaken at 150 rpm for 1 h. The OD600s of the resulting supernatants were compared.

Journal:

Article Title: Mutation of luxS Affects Biofilm Formation in Streptococcus mutans

doi: 10.1128/IAI.71.4.1972-1979.2003

Figure Lengend Snippet: Mutation of luxS causes an alteration in S. mutans biofilm. (A) Two images of in vitro biofilms representing both the wild type and the mutant using dark-field microscopy at magnifications ×20 and ×40. Cells were grown on glass coverslips as described in Materials and Methods. Similar results were obtained for more than 100 independent wild-type and luxS mutant biofilms examined. (B) Biofilms were tested for their ability to resist detergent treatment with SDS. Three samples of wild-type and mutant biofilms grown on glass coverslips were shaken at 150 rpm for 1 h. The OD600s of the resulting supernatants were compared.

Article Snippet: We demonstrated that the S. mutans LuxS protein exhibited high degrees of similarity to other LuxS proteins in the National Center for Biotechnology Information database and was able to complement a LuxS defect in E. coli .

Techniques: Mutagenesis, In Vitro, Microscopy