| The influence of HtrA expression on the growth of Streptococcus mutans during acid stress. | |
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MedLine Citation:
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PMID: 20387036 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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When proteins are damaged under stresses conditions, these proteins are either refolded or degraded by quality control system of molecular chaperones and protease. High-temperature requirement A (htrA) is of particular interest because it can perform the roles of both protease and a chaperone. HtrA plays an important role in maintaining the physiological homeostasis of bacteria against environmental stress such as elevated temperature, oxidative and osmotic stress. Inactivation of htrA genes can thus restrict the survival ability of bacteria. These observations suggested that htrA might be responsible for acid tolerance of Streptococcus mutans. In this study, we have generated an htrA mutant and an htrA-complemented strain of S. mutans K7 isolated from a Korean in order to investigate the role of htrA in growth under acidic conditions. In terms of growth under cidic conditions, the htrA mutant exhibited 20% to 23% lower growth than the control group. In addition, glucosyltransferase B and glucosyltransferase C expression levels significantly decreased. When the htrA expression level was restored by adding the htrA gene to the htrA mutant strain, the normal growth phenotype was restored under acid stress. Further, similar results were obtained for S. mutans UA159. Thus, htrA in S. mutans K7, as well as S. mutans UA159, can be concluded to play an important role during acid stress. |
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Authors:
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Kyung-hee Kang; Jung-Sook Lee; Min Yoo; Ingnyol Jin |
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Publication Detail:
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Type: Comparative Study; Journal Article Date: 2010-01-14 |
Journal Detail:
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Title: Molecules and cells Volume: 29 ISSN: 0219-1032 ISO Abbreviation: Mol. Cells Publication Date: 2010 Mar |
Date Detail:
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Created Date: 2010-04-13 Completed Date: 2010-09-13 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9610936 Medline TA: Mol Cells Country: United States |
Other Details:
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Languages: eng Pagination: 297-304 Citation Subset: IM |
Affiliation:
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Department of Dental Hygiene, Konyang University, Daejeon, 302-718, Korea. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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genetics,
physiology* Base Sequence Child Computer Systems Dental Caries / microbiology Drug Resistance, Bacterial Enzyme Induction Gene Expression Regulation, Bacterial Glucosyltransferases / biosynthesis, genetics Humans Hydrogen-Ion Concentration Korea Lactic Acid / pharmacology Molecular Chaperones / genetics, physiology* Molecular Sequence Data Peptide Hydrolases / genetics, physiology* Protein Folding Recombinant Fusion Proteins / physiology Reverse Transcriptase Polymerase Chain Reaction Sequence Alignment Sequence Homology, Nucleic Acid Streptococcus mutans / drug effects, enzymology, genetics*, growth & development, isolation & purification |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Molecular Chaperones; 0/Recombinant Fusion Proteins; 50-21-5/Lactic Acid; EC 2.4.1.-/1,3-alpha-D-glucan synthase; EC 2.4.1.-/Glucosyltransferases; EC 2.4.1.-/glucosyltransferase C; EC 3.4.-/Peptide Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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