| pubmed-article:17274596 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17274596 | lifeskim:mentions | umls-concept:C0004611 | lld:lifeskim |
| pubmed-article:17274596 | lifeskim:mentions | umls-concept:C0014346 | lld:lifeskim |
| pubmed-article:17274596 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:17274596 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:17274596 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:17274596 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17274596 | pubmed:dateCreated | 2007-2-23 | lld:pubmed |
| pubmed-article:17274596 | pubmed:abstractText | Quorum sensing is a process of chemical communication that bacteria use to assess cell population density and synchronize behavior on a community-wide scale. Communication is mediated by signal molecules called autoinducers. The LuxS autoinducer synthase produces 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor to a set of interconverting molecules that are generically called autoinducer-2 (AI-2). In enteric bacteria, AI-2 production induces the assembly of a transport apparatus (called the LuxS regulated (Lsr) transporter) that internalizes endogenously produced AI-2 as well as AI-2 produced by other bacterial species. AI-2 internalization is proposed to be a mechanism enteric bacteria employ to interfere with the signaling capabilities of neighboring species of bacteria. We have previously shown that Salmonella enterica serovar Typhimurium binds a specific cyclic derivative of DPD. Here we show that following internalization, the kinase LsrK phosphorylates carbon-5 of the open form of DPD. Phosphorylated DPD (P-DPD) binds specifically to the repressor of the lsr operon, LsrR, consistent with P-DPD being the inducer of the lsr operon. Subsequently, LsrG catalyzes the cleavage of P-DPD producing 2-phosphoglycolic acid. This series of chemical events is proposed to enable enteric bacteria to respond to the presence of competitor bacteria by sequestering and destroying AI-2, thereby eliminating the competitors' intercellular communication capabilities. | lld:pubmed |
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| pubmed-article:17274596 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17274596 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17274596 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17274596 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17274596 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17274596 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17274596 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17274596 | pubmed:issn | 1554-8937 | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:BasslerBonnie... | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:PelczerIstván... | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:KimJeong... | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:SemmelhackMar... | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:XavierKarina... | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:MillerStephen... | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:LuWenyunW | lld:pubmed |
| pubmed-article:17274596 | pubmed:author | pubmed-author:RabinowitzJos... | lld:pubmed |
| pubmed-article:17274596 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17274596 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:17274596 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:17274596 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17274596 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17274596 | pubmed:pagination | 128-36 | lld:pubmed |
| pubmed-article:17274596 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
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| pubmed-article:17274596 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17274596 | pubmed:articleTitle | Phosphorylation and processing of the quorum-sensing molecule autoinducer-2 in enteric bacteria. | lld:pubmed |
| pubmed-article:17274596 | pubmed:affiliation | Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014, USA. | lld:pubmed |
| pubmed-article:17274596 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17274596 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17274596 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17274596 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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