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000059010 0247_ $$2pmid$$apmid:17655327
000059010 0247_ $$2DOI$$a10.1021/bi700563f
000059010 0247_ $$2WOS$$aWOS:000248692400005
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000059010 041__ $$aeng
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000059010 084__ $$2WoS$$aBiochemistry & Molecular Biology
000059010 1001_ $$0P:(DE-Juel1)VDB58062$$aMironova, O. S.$$b0$$uFZJ
000059010 245__ $$aFT-IR difference spectroscopy elucidates crucial interactions of sensory rhodopsin I with the cognate transducer Htrl
000059010 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2007
000059010 300__ $$a9399 - 9405
000059010 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000059010 3367_ $$2BibTeX$$aARTICLE
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000059010 3367_ $$2DRIVER$$aarticle
000059010 440_0 $$0798$$aBiochemistry$$v46$$x0006-2960$$y33
000059010 500__ $$aRecord converted from VDB: 12.11.2012
000059010 520__ $$aThe phototaxis receptor sensory rhodopsin I (SRI) from Halobacterium salinarum interacts with its cognate transducer (HtrI) forming a transmembrane complex. After light excitation of the chromophore all-trans retinal, SRI undergoes structural changes that are ultimately transmitted to HtrI. The interaction of SRI with HtrI results in the closure of the receptor's proton pathway, which renders the photocycle recovery kinetics of SRI pH-independent. We demonstrate on heterologously expressed and reconstituted SRI-HtrI fusion proteins that the transmembrane part of HtrI (residues 1-52) as well as the downstream cytoplasmic part (residues 53-147) exhibit conformational changes after light excitation. The sum of these conformational changes is similar to those observed in the fusion constructs SRI-HtrI 1-71 and SRI-HtrI 1-147, which display pH-independent receptor kinetics. These results indicate the occurrence of spatially distinct conformational changes that are required for functional signal transmission. Kinetic and spectroscopic analysis of HtrI point mutants of Asn53 provides evidence that this residue is involved in the receptor-transducer interaction. We suggest that Asn53 plays a role similar to that of Asn74 of the HtrII from Natronobacterium pharaonis, the latter forming a hydrogen bond to the receptor within the membrane.
000059010 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000059010 588__ $$aDataset connected to Web of Science, Pubmed
000059010 650_2 $$2MeSH$$aArchaeal Proteins: chemistry
000059010 650_2 $$2MeSH$$aArchaeal Proteins: genetics
000059010 650_2 $$2MeSH$$aArchaeal Proteins: radiation effects
000059010 650_2 $$2MeSH$$aAsparagine: chemistry
000059010 650_2 $$2MeSH$$aAsparagine: genetics
000059010 650_2 $$2MeSH$$aHalorhodopsins: chemistry
000059010 650_2 $$2MeSH$$aHalorhodopsins: genetics
000059010 650_2 $$2MeSH$$aHalorhodopsins: radiation effects
000059010 650_2 $$2MeSH$$aLight
000059010 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000059010 650_2 $$2MeSH$$aMembrane Proteins: genetics
000059010 650_2 $$2MeSH$$aMembrane Proteins: radiation effects
000059010 650_2 $$2MeSH$$aPoint Mutation
000059010 650_2 $$2MeSH$$aProtein Interaction Mapping
000059010 650_2 $$2MeSH$$aRecombinant Fusion Proteins: chemistry
000059010 650_2 $$2MeSH$$aRecombinant Fusion Proteins: genetics
000059010 650_2 $$2MeSH$$aRecombinant Fusion Proteins: radiation effects
000059010 650_2 $$2MeSH$$aSensory Rhodopsins: chemistry
000059010 650_2 $$2MeSH$$aSensory Rhodopsins: genetics
000059010 650_2 $$2MeSH$$aSensory Rhodopsins: radiation effects
000059010 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared
000059010 650_7 $$00$$2NLM Chemicals$$aArchaeal Proteins
000059010 650_7 $$00$$2NLM Chemicals$$aHalorhodopsins
000059010 650_7 $$00$$2NLM Chemicals$$aMembrane Proteins
000059010 650_7 $$00$$2NLM Chemicals$$aRecombinant Fusion Proteins
000059010 650_7 $$00$$2NLM Chemicals$$aSRI protein, Halobacterium
000059010 650_7 $$00$$2NLM Chemicals$$aSensory Rhodopsins
000059010 650_7 $$00$$2NLM Chemicals$$ahtrI protein, Halobacterium salinarium
000059010 650_7 $$07006-34-0$$2NLM Chemicals$$aAsparagine
000059010 650_7 $$2WoSType$$aJ
000059010 7001_ $$0P:(DE-Juel1)VDB58065$$aBudyak, I. L.$$b1$$uFZJ
000059010 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b2$$uFZJ
000059010 7001_ $$0P:(DE-Juel1)VDB1421$$aSchlesinger, R.$$b3$$uFZJ
000059010 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b4$$uFZJ
000059010 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi700563f$$gVol. 46, p. 9399 - 9405$$p9399 - 9405$$q46<9399 - 9405$$tBiochemistry$$v46$$x0006-2960$$y2007
000059010 8567_ $$uhttp://dx.doi.org/10.1021/bi700563f
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000059010 9141_ $$y2007
000059010 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
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