Source:http://linkedlifedata.com/resource/pubmed/id/18681938
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rdf:type | |
lifeskim:mentions |
umls-concept:C0019868,
umls-concept:C0029073,
umls-concept:C0038409,
umls-concept:C0449432,
umls-concept:C1179435,
umls-concept:C1514873,
umls-concept:C1524073,
umls-concept:C1546857,
umls-concept:C1548799,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1705248,
umls-concept:C1710548,
umls-concept:C2700640
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pubmed:issue |
1
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pubmed:dateCreated |
2008-10-2
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pubmed:abstractText |
Streptococcus mutans is a primary pathogen for dental caries in humans. CiaR and CiaH of S. mutans comprise a two-component signal transduction system (TCS) involved in regulating various virulent factors. However, the signal that triggers the CiaRH response remains unknown. In this study, we show that calcium is a signal for regulation of the ciaRH operon, and that a double-glycine-containing small peptide encoded within the ciaRH operon (renamed ciaX) mediates this regulation. CiaX contains a serine + aspartate (SD) domain that is shared by calcium-binding proteins. A markerless in-frame deletion of ciaX reduced ciaRH operon expression and diminished the calcium repression of operon transcription. Point mutations of the SD domain resulted in the same phenotype as the in-frame deletion, indicating that the SD domain is required for CiaX function. Further characterization of ciaX demonstrated that it is involved in calcium-mediated biofilm formation. Furthermore, inactivation of ciaR or ciaH led to the same phenotype as the in-frame deletion of ciaX, suggesting that all three genes are involved in the same regulatory pathway. Sequence analysis and real-time RT-PCR identified a putative CiaR binding site upstream of ciaX. We conclude that the ciaXRH operon is a three-component, self-regulatory system modulating cellular functions in response to calcium.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1365-2958
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
112-26
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:18681938-Amino Acid Sequence,
pubmed-meshheading:18681938-Bacterial Proteins,
pubmed-meshheading:18681938-Biofilms,
pubmed-meshheading:18681938-Calcium,
pubmed-meshheading:18681938-Gene Deletion,
pubmed-meshheading:18681938-Gene Expression Regulation, Bacterial,
pubmed-meshheading:18681938-Genes, Bacterial,
pubmed-meshheading:18681938-Genetic Complementation Test,
pubmed-meshheading:18681938-Homeostasis,
pubmed-meshheading:18681938-Humans,
pubmed-meshheading:18681938-Molecular Sequence Data,
pubmed-meshheading:18681938-Mutagenesis, Site-Directed,
pubmed-meshheading:18681938-Operon,
pubmed-meshheading:18681938-Phenotype,
pubmed-meshheading:18681938-Point Mutation,
pubmed-meshheading:18681938-RNA, Bacterial,
pubmed-meshheading:18681938-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:18681938-Sequence Alignment,
pubmed-meshheading:18681938-Signal Transduction,
pubmed-meshheading:18681938-Streptococcus mutans
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pubmed:year |
2008
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pubmed:articleTitle |
The cia operon of Streptococcus mutans encodes a unique component required for calcium-mediated autoregulation.
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pubmed:affiliation |
UCLA School of Dentistry, Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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