Document Detail

Single-molecule force spectroscopy measures structural changes induced by light activation and transducer binding in sensory rhodopsin II.
MedLine Citation:
PMID:  19651144     Owner:  NLM     Status:  MEDLINE    
Microbial rhodopsins are a family of seven-helical transmembrane proteins containing retinal as chromophore. Sensory rhodopsin II (SRII) triggers two very different responses upon light excitation, depending on the presence or the absence of its cognate transducer HtrII: Whereas light activation of the NpSRII/NpHtrII complex activates a signalling cascade that initiates the photophobic response, NpSRII alone acts as a proton pump. Using single-molecule force spectroscopy, we analysed the stability of NpSRII and its complex with the transducer in the dark and under illumination. By improving force spectroscopic data analysis, we were able to reveal the localisation of occurring forces within the protein chain with a resolution of about six amino acids. Distinct regions in helices G and F were affected differently, depending on the experimental conditions. The results are generally in line with previous data on the molecular stability of NpSRII. Interestingly, new interaction sites were identified upon light activation, whose functional importance is discussed in detail.
Leoni Oberbarnscheidt; Richard Janissen; Swetlana Martell; Martin Engelhard; Filipp Oesterhelt
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-08-03
Journal Detail:
Title:  Journal of molecular biology     Volume:  394     ISSN:  1089-8638     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-11-13     Completed Date:  2009-12-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  383-90     Citation Subset:  IM    
Institut für molekulare physikalische Chemie, Düsseldorf, Germany.
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MeSH Terms
Archaeal Proteins / chemistry*,  metabolism,  radiation effects
Carotenoids / chemistry*,  metabolism,  radiation effects
Halorhodopsins / chemistry*,  metabolism,  radiation effects
Models, Molecular
Natronobacterium / chemistry
Photochemical Processes
Protein Conformation
Protein Structure, Secondary
Recombinant Proteins / chemistry,  metabolism,  radiation effects
Sensory Rhodopsins / chemistry*,  metabolism,  radiation effects
Signal Transduction
Spectrum Analysis
Reg. No./Substance:
0/Archaeal Proteins; 0/Halorhodopsins; 0/HtrII protein, Natronobacterium pharaonis; 0/Recombinant Proteins; 0/Sensory Rhodopsins; 0/phototaxis receptor sensory rhodopsin II, Natronobacterium pharaonis; 0/sensory rhodopsin II protein, archaeal; 36-88-4/Carotenoids

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