Effects of solubilization on the structure and function of the sensory rhodopsin II/transducer complex

DC FieldValueLanguage
dc.contributor.authorKlare, JP
dc.contributor.authorBordignon, E
dc.contributor.authorDoebber, M
dc.contributor.authorFitter, J
dc.contributor.authorKriegsmann, J
dc.contributor.authorChizhov, I
dc.contributor.authorSteinhoff, HJ
dc.contributor.authorEngelhard, M
dc.date.accessioned2021-12-23T16:20:56Z-
dc.date.available2021-12-23T16:20:56Z-
dc.date.issued2006
dc.identifier.issn00222836
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/13659-
dc.description.abstractLipid-protein interactions are known to play a crucial role in structure and physiological activity of integral membrane proteins. However, current technology for membrane protein purification necessitates extraction from the membrane into detergent micelles. Also, due to experimental protocols, most of the data available for membrane proteins is obtained using detergent-solubilized samples. Stable solubilization of membrane proteins is therefore an important issue in biotechnology as well as in biochemistry and structural biology. An understanding of solubilization effects on structural and functional properties of specific proteins is of utmost relevance for the evaluation and interpretation of experimental results. In this study, a comparison of structural and kinetic data obtained for the archaebacterial photoreceptor/transducer complex from Natronomonas pharaonis (NpSRII/NpHtrII) in detergent-solubilized and lipid-reconstituted states is presented. Laser flash photolysis, fluorescence spectroscopy, and electron paramagnetic resonance spectroscopy data reveal considerable influence of solubilization on the photocycle kinetics of the receptor protein and on the structure of the transducer protein. Especially the protein-membrane proximal region and the protein-protein interfacial domains are sensitive towards non-native conditions. These data demonstrate that relevance of biochemical and structural information obtained from solubilized membrane proteins or membrane protein complexes has to be evaluated carefully. (c) 2006 Elsevier Ltd. All rights reserved.
dc.language.isoen
dc.publisherACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
dc.relation.ispartofJOURNAL OF MOLECULAR BIOLOGY
dc.subjectBACTERIORHODOPSIN
dc.subjectBiochemistry & Molecular Biology
dc.subjectCOGNATE TRANSDUCER
dc.subjectCONFORMATIONAL-CHANGES
dc.subjectdetergents
dc.subjectHELIX F
dc.subjectLINKER REGION
dc.subjectmembrane proteins
dc.subjectNATRONOBACTERIUM-PHARAONIS
dc.subjectPHARAONIS PHOBORHODOPSIN
dc.subjectphoborhodopsin
dc.subjectphototaxis
dc.subjectPROTEIN-STRUCTURE
dc.subjectPURPLE MEMBRANE
dc.subjectSIDE-CHAINS
dc.subjectsite-directed spin labeling EPR
dc.titleEffects of solubilization on the structure and function of the sensory rhodopsin II/transducer complex
dc.typejournal article
dc.identifier.doi10.1016/j.jmb.2005.12.015
dc.identifier.isiISI:000235432400013
dc.description.volume356
dc.description.issue5
dc.description.startpage1207
dc.description.endpage1221
dc.contributor.orcid0000-0002-4503-2079
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0002-5761-5968
dc.contributor.researcheridJ-3294-2013
dc.contributor.researcheridH-3791-2014
dc.contributor.researcheridC-1428-2009
dc.identifier.eissn10898638
dc.publisher.place24-28 OVAL RD, LONDON NW1 7DX, ENGLAND
dcterms.isPartOf.abbreviationJ. Mol. Biol.
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptidfb04-
crisitem.author.deptidfb04-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidKlJo010-
crisitem.author.netidStHe633-
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