Source:http://linkedlifedata.com/resource/pubmed/id/16002996
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2005-7-8
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pubmed:abstractText |
BLUF (a sensor of Blue-Light Using FAD) is a novel putative photoreceptor domain that is found in many bacteria and some eukaryotic algae. As found on genome analysis, certain cyanobacteria have BLUF proteins with a short C-terminal extension. As typical examples, Tll0078 from thermophilic Thermosynechococcus elongatus BP-1 and Slr1694 from mesophilic Synechocystis sp. PCC 6803 were comparatively studied. FAD of both proteins was hardly reduced by exogenous reductants or mediators except methylviologen but showed a typical spectral shift to a longer wavelength upon excitation with blue light. In particular, freshly prepared Tll0078 protein showed slow but reversible aggregation, indicative of light-induced conformational changes in the protein structure. Tll0078 is far more stable as to heat treatment than Slr1694, as judged from flavin fluorescence. The slr1694-disruptant showed phototactic motility away from the light source (negative phototaxis), while the wild type Synechocystis showed positive phototaxis toward the source. Yeast two-hybrid screening with slr1694 showed self-interaction of Slr1694 (PixD) with itself and interaction with a novel PatA-like response regulator, Slr1693 (PixE). These results were discussed in relation to the signaling mechanism of the "short" BLUF proteins in the regulation of cyanobacterial phototaxis.
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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/Flavin-Adenine Dinucleotide,
http://linkedlifedata.com/resource/pubmed/chemical/Flavins,
http://linkedlifedata.com/resource/pubmed/chemical/Photoreceptors, Microbial,
http://linkedlifedata.com/resource/pubmed/chemical/T11078 protein, cyanobacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-924X
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pubmed:author |
pubmed-author:FukushimaYoshimasaY,
pubmed-author:GengXiaoxingX,
pubmed-author:HigashiShoichiS,
pubmed-author:IkeuchiMasahikoM,
pubmed-author:ItohShigeruS,
pubmed-author:KatayamaMitsunoriM,
pubmed-author:OkajimaKojiK,
pubmed-author:SatoShuseiS,
pubmed-author:ShibataYutakaY,
pubmed-author:TabataSatoshiS,
pubmed-author:WatanabeMasakatsuM,
pubmed-author:YoshiharaShizueS
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pubmed:issnType |
Print
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pubmed:volume |
137
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
741-50
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:16002996-Amino Acid Sequence,
pubmed-meshheading:16002996-Bacterial Proteins,
pubmed-meshheading:16002996-Cyanobacteria,
pubmed-meshheading:16002996-Flavin-Adenine Dinucleotide,
pubmed-meshheading:16002996-Flavins,
pubmed-meshheading:16002996-Models, Biological,
pubmed-meshheading:16002996-Molecular Sequence Data,
pubmed-meshheading:16002996-Photoreceptors, Microbial,
pubmed-meshheading:16002996-Protein Structure, Tertiary,
pubmed-meshheading:16002996-Sequence Alignment,
pubmed-meshheading:16002996-Spectrometry, Fluorescence,
pubmed-meshheading:16002996-Synechocystis,
pubmed-meshheading:16002996-Time and Motion Studies,
pubmed-meshheading:16002996-Two-Hybrid System Techniques
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pubmed:year |
2005
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pubmed:articleTitle |
Biochemical and functional characterization of BLUF-type flavin-binding proteins of two species of cyanobacteria.
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pubmed:affiliation |
Department of Life Sciences (Biology), The University of Tokyo, Komaba, Meguro, Tokyo 153-8902, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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