Source:http://linkedlifedata.com/resource/pubmed/id/21082778
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
50
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pubmed:dateCreated |
2010-12-14
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pubmed:abstractText |
Organisms adapt their physiologies in response to the quality and quantity of environmental light. Members of a recently identified photoreceptor protein family, BLUF domain proteins, use a flavin chromophore to sense blue light. Herein, we report that PapB, which contains a BLUF domain, controls the biofilm formation of the purple photosynthetic bacterium Rhodopseudomonas palustris. Purified PapB undergoes a typical BLUF-type photocycle, and light-excited PapB enhances the phosphodiesterase activity of the EAL domain protein, PapA, which degrades the second messenger, cyclic dimeric GMP (c-di-GMP). PapB directly interacts with PapA in vitro in a light-independent manner and induces a conformational change in the preformed PapA-PapB complex. A PapA-PapB docking simulation, as well as a site-directed mutagenesis study, identified amino acids partially responsible for the interaction between the PapA EAL domain and the two C-terminal ?-helices of the PapB BLUF domain. Thus, the conformational change, which involves the C-terminal ?-helices, transfers the flavin-sensed blue light signal to PapA. Deletion of papB in R. palustris enhances biofilm formation under high-intensity blue light conditions, indicating that PapB functions as a blue light sensor, which negatively regulates biofilm formation. These results demonstrate that R. palustris can control biofilm formation via a blue light-dependent modulation of its c-di-GMP level by the BLUF domain protein, PapB.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/bis(3',5')-cyclic diguanylic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1520-4995
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
21
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10647-55
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pubmed:meshHeading |
pubmed-meshheading:21082778-Bacterial Proteins,
pubmed-meshheading:21082778-Biofilms,
pubmed-meshheading:21082778-Chromatography, High Pressure Liquid,
pubmed-meshheading:21082778-Cyclic GMP,
pubmed-meshheading:21082778-Light,
pubmed-meshheading:21082778-Models, Biological,
pubmed-meshheading:21082778-Models, Molecular,
pubmed-meshheading:21082778-Phosphoric Diester Hydrolases,
pubmed-meshheading:21082778-Protein Structure, Secondary,
pubmed-meshheading:21082778-Rhodopseudomonas
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pubmed:year |
2010
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pubmed:articleTitle |
Biochemical and physiological characterization of a BLUF protein-EAL protein complex involved in blue light-dependent degradation of cyclic diguanylate in the purple bacterium Rhodopseudomonas palustris.
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pubmed:affiliation |
Graduate School of Bioscience and Biotechnology, Tokyo Institute ofTechnology, Yokohama 226-8501, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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