Hauptseite > Publikationsdatenbank > Sensory rhodopsin II/transducer complex formation in detergent and in lipid bilayers studied with FRET > print

001     5168
005     20200402205627.0
024 7 _ |2 pmid
|a pmid:19094962
024 7 _ |2 DOI
|a 10.1016/j.bbamem.2008.11.011
024 7 _ |2 WOS
|a WOS:000263794700025
037 _ _ |a PreJuSER-5168
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Biophysics
100 1 _ |0 P:(DE-Juel1)VDB60877
|a Kriegsmann, J.
|b 0
|u FZJ
245 _ _ |a Sensory rhodopsin II/transducer complex formation in detergent and in lipid bilayers studied with FRET
260 _ _ |a Amsterdam
|b Elsevier
|c 2009
300 _ _ |a 522 - 531
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |0 19423
|a BBA - Biomembranes
|v 1788
|x 0005-2736
|y 2
500 _ _ |a J. F. thanks G. Buldt (Forschungszentrum Julich) for continuous and sustainable support in his institute. This work was supported by the Deutsche Forschungsgerneinschaft (M.E.) and by a priority program SPP 1128 of Deutsche Forschungsgerneinschaft (FI 841/3-1,2 to J.F.). We are indebted to R. Schlesinger for providing us with bacteriorhodopsin and to R. Batra-Safferling for the discussions and comments on the manuscript.
520 _ _ |a The photophobic receptor from Natronomonas pharaonis (NpSRII) forms a photo-signalling complex with its cognate transducer (NpHtrII). In order to elucidate the complex formation in more detail, we have studied the intermolecular binding of both constituents (NpSRII and NpHtrII157; truncated at residue 157) in detergent buffers, and in lipid bilayers using FRET. The data for hetero-dimer formation of NpSRII/NpHtrII in detergent agrees well with KD values (approximately 200 nM) described in the literature. In lipid bilayers, the binding affinity between proteins in the NpSRII/NpHtrII complex is at least one order of magnitude stronger. In detergent the strength of binding is similar for both homo-dimers (NpSRII/NpSRII and NpHtrII/NpHtrII) but significantly weaker (KD approximately 16 microM) when compared to the hetero-dimer. The intermolecular binding is again considerably stronger in lipid bilayers; however, it is not as strong as that observed for the hetero-dimer. At a molar transducer/lipid ratio of 1:2000, which is still well above physiological concentrations, only 40% homo-dimers are formed. Apparently, in cell membranes the formation of the assumed functionally active oligomeric 2:2 complex depends on the full-length transducer including the helical cytoplasmic part, which is thought to tighten the transducer-dimer association.
536 _ _ |0 G:(DE-Juel1)FUEK443
|2 G:(DE-HGF)
|a Programm Biosoft
|c N03
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Archaeal Proteins: chemistry
650 _ 2 |2 MeSH
|a Archaeal Proteins: genetics
650 _ 2 |2 MeSH
|a Archaeal Proteins: metabolism
650 _ 2 |2 MeSH
|a Biophysical Phenomena
650 _ 2 |2 MeSH
|a Detergents
650 _ 2 |2 MeSH
|a Halobacteriaceae: chemistry
650 _ 2 |2 MeSH
|a Halobacteriaceae: genetics
650 _ 2 |2 MeSH
|a Halobacteriaceae: metabolism
650 _ 2 |2 MeSH
|a Lipid Bilayers: chemistry
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Multimerization
650 _ 2 |2 MeSH
|a Protein Structure, Quaternary
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: chemistry
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: genetics
650 _ 2 |2 MeSH
|a Sensory Rhodopsins: metabolism
650 _ 2 |2 MeSH
|a Signal Transduction
650 _ 2 |2 MeSH
|a Spectrophotometry
650 _ 7 |0 0
|2 NLM Chemicals
|a Archaeal Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Detergents
650 _ 7 |0 0
|2 NLM Chemicals
|a HtrII protein, Natronobacterium pharaonis
650 _ 7 |0 0
|2 NLM Chemicals
|a Lipid Bilayers
650 _ 7 |0 0
|2 NLM Chemicals
|a Sensory Rhodopsins
650 _ 7 |2 WoSType
|a J
653 2 0 |2 Author
|a Fluorescence spectroscopy
653 2 0 |2 Author
|a Lipid vesicle
653 2 0 |2 Author
|a Photo signalling
653 2 0 |2 Author
|a Sensory rhodopsin
653 2 0 |2 Author
|a Membrane protein interaction
653 2 0 |2 Author
|a Dissociation constant
700 1 _ |0 P:(DE-Juel1)VDB77075
|a Brehs, M.
|b 1
|u FZJ
700 1 _ |0 P:(DE-HGF)0
|a Klare, J.P.
|b 2
700 1 _ |0 P:(DE-HGF)0
|a Engelhard, M.
|b 3
700 1 _ |0 P:(DE-Juel1)131961
|a Fitter, J.
|b 4
|u FZJ
773 _ _ |0 PERI:(DE-600)2209384-9
|a 10.1016/j.bbamem.2008.11.011
|g Vol. 1788, p. 522 - 531
|p 522 - 531
|q 1788<522 - 531
|t Biochimica et biophysica acta / Biomembranes
|v 1788
|x 0005-2736
|y 2009
856 7 _ |u http://dx.doi.org/10.1016/j.bbamem.2008.11.011
909 C O |o oai:juser.fz-juelich.de:5168
|p VDB
913 1 _ |0 G:(DE-Juel1)FUEK443
|a DE-HGF
|b Schlüsseltechnologien
|k N03
|l BioSoft
|v Programm Biosoft
|x 0
|z entfällt
914 1 _ |y 2009
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |0 I:(DE-Juel1)ISB-2-20090406
|d 31.12.2010
|g ISB
|k ISB-2
|l Molekulare Biophysik
|x 0
970 _ _ |a VDB:(DE-Juel1)112626
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)ISB-2-20090406

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21