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Regulation of Recombination between gtfB/gtfC Genes in Streptococcus mutans by Recombinase A
Streptococcus mutans produces 3 types of glucosyltransferases (GTFs), whose cooperative action is essential for cellular adhesion. The recombinase A (RecA) protein is required for homologous recombination. In our previous study, we isolated several strains with a smooth colony morphology and low GTF...
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Published in: | TheScientificWorld 2013-01, Vol.2013 (2013), p.1-7 |
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description | Streptococcus mutans produces 3 types of glucosyltransferases (GTFs), whose cooperative action is essential for cellular adhesion. The recombinase A (RecA) protein is required for homologous recombination. In our previous study, we isolated several strains with a smooth colony morphology and low GTF activity, characteristics speculated to be derived from the GTF fusions. The purpose of the present study was to investigate the mechanism of those fusions. S. mutans strain MT8148 was grown in the presence of recombinant RecA (rRecA) protein, after which smooth colonies were isolated. The biological functions and sequences of the gtfB and gtfC genes of this as well as other clinical strains were determined. The sucrose-dependent adherence rates of those strains were reduced as compared to that of MT8148. Determination of the sequences of the gtfB and gtfC genes showed that an approximately 3500 bp region was deleted from the area between them. Furthermore, expression of the recA gene was elevated in those strains as compared to MT8148. These results suggest that RecA has an important role in fusions of gtfB and gtfC genes, leading to alteration of colony morphology and reduction in sucrose-dependent adhesion. |
doi_str_mv | 10.1155/2013/405075 |
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The recombinase A (RecA) protein is required for homologous recombination. In our previous study, we isolated several strains with a smooth colony morphology and low GTF activity, characteristics speculated to be derived from the GTF fusions. The purpose of the present study was to investigate the mechanism of those fusions. S. mutans strain MT8148 was grown in the presence of recombinant RecA (rRecA) protein, after which smooth colonies were isolated. The biological functions and sequences of the gtfB and gtfC genes of this as well as other clinical strains were determined. The sucrose-dependent adherence rates of those strains were reduced as compared to that of MT8148. Determination of the sequences of the gtfB and gtfC genes showed that an approximately 3500 bp region was deleted from the area between them. Furthermore, expression of the recA gene was elevated in those strains as compared to MT8148. These results suggest that RecA has an important role in fusions of gtfB and gtfC genes, leading to alteration of colony morphology and reduction in sucrose-dependent adhesion.</description><identifier>ISSN: 2356-6140</identifier><identifier>ISSN: 1537-744X</identifier><identifier>EISSN: 1537-744X</identifier><identifier>DOI: 10.1155/2013/405075</identifier><identifier>PMID: 23476132</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><subject>Adhesion ; Bacterial Adhesion ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Base Sequence ; Cell adhesion ; Colonies ; Dental caries ; Dentistry ; DNA, Bacterial - genetics ; Enzyme Activation ; Gene expression ; Gene Expression Regulation, Bacterial ; Gene Expression Regulation, Enzymologic ; Gene Fusion ; Gene sequencing ; Genes ; Genes, Bacterial ; Genetic aspects ; Genetic recombination ; Genetic research ; Homology ; Microbiological research ; Microbiology ; Morphology ; Pediatrics ; Plasmids ; Proteins ; Rec A Recombinases - genetics ; Rec A Recombinases - metabolism ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Recombination, Genetic ; Sequence Analysis, DNA ; Signal transduction ; Streptococcus ; Streptococcus infections ; Streptococcus mutans ; Streptococcus mutans - drug effects ; Streptococcus mutans - enzymology ; Streptococcus mutans - genetics ; Stress response ; Sucrose ; Sucrose - pharmacology ; University graduates</subject><ispartof>TheScientificWorld, 2013-01, Vol.2013 (2013), p.1-7</ispartof><rights>Copyright © 2013 Satoko Inagaki et al.</rights><rights>COPYRIGHT 2013 John Wiley & Sons, Inc.</rights><rights>Copyright © 2013 Satoko Inagaki et al. This is an open access article distributed under the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. https://creativecommons.org/licenses/by/4.0</rights><rights>Copyright © 2013 Satoko Inagaki et al. 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c699t-59c8d999ad656b3bd5f5bf0213dcef9f53fc60d8c21acedac3dbf8bc738acf363</citedby><cites>FETCH-LOGICAL-c699t-59c8d999ad656b3bd5f5bf0213dcef9f53fc60d8c21acedac3dbf8bc738acf363</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/1420078428/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/1420078428?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23476132$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Sato, Yutaka</contributor><contributor>Mattos-Graner, Renata O.</contributor><contributor>Childers, Noel K.</contributor><contributor>Alallusua, Satu</contributor><contributor>Satu Alallusua</contributor><contributor>Yutaka Sato</contributor><contributor>Renata O Mattos-Graner</contributor><contributor>Noel K Childers</contributor><creatorcontrib>Matsumoto-Nakano, Michiyo</creatorcontrib><creatorcontrib>Matsumi, Yuki</creatorcontrib><creatorcontrib>Ardin, Arifah C.</creatorcontrib><creatorcontrib>Nagayama, Kayoko</creatorcontrib><creatorcontrib>Takashima, Yukiko</creatorcontrib><creatorcontrib>Fujita, Kazuyo</creatorcontrib><creatorcontrib>Inagaki, Satoko</creatorcontrib><title>Regulation of Recombination between gtfB/gtfC Genes in Streptococcus mutans by Recombinase A</title><title>TheScientificWorld</title><addtitle>ScientificWorldJournal</addtitle><description>Streptococcus mutans produces 3 types of glucosyltransferases (GTFs), whose cooperative action is essential for cellular adhesion. The recombinase A (RecA) protein is required for homologous recombination. In our previous study, we isolated several strains with a smooth colony morphology and low GTF activity, characteristics speculated to be derived from the GTF fusions. The purpose of the present study was to investigate the mechanism of those fusions. S. mutans strain MT8148 was grown in the presence of recombinant RecA (rRecA) protein, after which smooth colonies were isolated. The biological functions and sequences of the gtfB and gtfC genes of this as well as other clinical strains were determined. The sucrose-dependent adherence rates of those strains were reduced as compared to that of MT8148. Determination of the sequences of the gtfB and gtfC genes showed that an approximately 3500 bp region was deleted from the area between them. Furthermore, expression of the recA gene was elevated in those strains as compared to MT8148. These results suggest that RecA has an important role in fusions of gtfB and gtfC genes, leading to alteration of colony morphology and reduction in sucrose-dependent adhesion.</description><subject>Adhesion</subject><subject>Bacterial Adhesion</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Cell adhesion</subject><subject>Colonies</subject><subject>Dental caries</subject><subject>Dentistry</subject><subject>DNA, Bacterial - genetics</subject><subject>Enzyme Activation</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Bacterial</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Gene Fusion</subject><subject>Gene sequencing</subject><subject>Genes</subject><subject>Genes, Bacterial</subject><subject>Genetic aspects</subject><subject>Genetic recombination</subject><subject>Genetic research</subject><subject>Homology</subject><subject>Microbiological research</subject><subject>Microbiology</subject><subject>Morphology</subject><subject>Pediatrics</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Rec A Recombinases - 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The recombinase A (RecA) protein is required for homologous recombination. In our previous study, we isolated several strains with a smooth colony morphology and low GTF activity, characteristics speculated to be derived from the GTF fusions. The purpose of the present study was to investigate the mechanism of those fusions. S. mutans strain MT8148 was grown in the presence of recombinant RecA (rRecA) protein, after which smooth colonies were isolated. The biological functions and sequences of the gtfB and gtfC genes of this as well as other clinical strains were determined. The sucrose-dependent adherence rates of those strains were reduced as compared to that of MT8148. Determination of the sequences of the gtfB and gtfC genes showed that an approximately 3500 bp region was deleted from the area between them. Furthermore, expression of the recA gene was elevated in those strains as compared to MT8148. These results suggest that RecA has an important role in fusions of gtfB and gtfC genes, leading to alteration of colony morphology and reduction in sucrose-dependent adhesion.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><pmid>23476132</pmid><doi>10.1155/2013/405075</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adhesion Bacterial Adhesion Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Base Sequence Cell adhesion Colonies Dental caries Dentistry DNA, Bacterial - genetics Enzyme Activation Gene expression Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic Gene Fusion Gene sequencing Genes Genes, Bacterial Genetic aspects Genetic recombination Genetic research Homology Microbiological research Microbiology Morphology Pediatrics Plasmids Proteins Rec A Recombinases - genetics Rec A Recombinases - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism Recombination, Genetic Sequence Analysis, DNA Signal transduction Streptococcus Streptococcus infections Streptococcus mutans Streptococcus mutans - drug effects Streptococcus mutans - enzymology Streptococcus mutans - genetics Stress response Sucrose Sucrose - pharmacology University graduates |
title | Regulation of Recombination between gtfB/gtfC Genes in Streptococcus mutans by Recombinase A |
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