Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers1. (May 2017)
- Record Type:
- Journal Article
- Title:
- Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers1. (May 2017)
- Main Title:
- Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers1
- Authors:
- Orekhov, Philipp
Bothe, Arne
Steinhoff, Heinz‐Jürgen
Shaitan, Konstantin V.
Raunser, Stefan
Fotiadis, Dimitrios
Schlesinger, Ramona
Klare, Johann P.
Engelhard, Martin - Abstract:
- Abstract: Archaeal photoreceptors consist of sensory rhodopsins in complex with their cognate transducers. After light excitation, a two‐component signaling chain is activated, which is homologous to the chemotactic signaling cascades in enterobacteria. The latter system has been studied in detail. From structural and functional studies, a picture emerges which includes stable signaling complexes, which assemble to receptor arrays displaying hexagonal structural elements. At this higher order structural level, signal amplification and sensory adaptation occur. Here, we describe electron microscopy data, which show that also the archaeal phototaxis receptors sensory rhodopsin I and II in complex with their cognate transducers can form hexagonal lattices even in the presence of a detergent. This result could be confirmed by molecular dynamics calculations, which revealed similar structural elements. Calculations of the global modes of motion displayed one mode, which resembles the "U"‐"V" transition of the Np SRII: Np HtrII complex, which was previously argued to represent a functionally relevant global conformational change accompanying the activation process [Ishchenko et al. (2013) J. Photochem. Photobiol. B 123, 55‐58]. A model of cooperativity at the transmembrane level is discussed. Abstract : Archaeal rhodopsins in complex with their cognate transducers trigger on light excitation a two‐component signaling cascade which is homologous to the chemotactic signalAbstract: Archaeal photoreceptors consist of sensory rhodopsins in complex with their cognate transducers. After light excitation, a two‐component signaling chain is activated, which is homologous to the chemotactic signaling cascades in enterobacteria. The latter system has been studied in detail. From structural and functional studies, a picture emerges which includes stable signaling complexes, which assemble to receptor arrays displaying hexagonal structural elements. At this higher order structural level, signal amplification and sensory adaptation occur. Here, we describe electron microscopy data, which show that also the archaeal phototaxis receptors sensory rhodopsin I and II in complex with their cognate transducers can form hexagonal lattices even in the presence of a detergent. This result could be confirmed by molecular dynamics calculations, which revealed similar structural elements. Calculations of the global modes of motion displayed one mode, which resembles the "U"‐"V" transition of the Np SRII: Np HtrII complex, which was previously argued to represent a functionally relevant global conformational change accompanying the activation process [Ishchenko et al. (2013) J. Photochem. Photobiol. B 123, 55‐58]. A model of cooperativity at the transmembrane level is discussed. Abstract : Archaeal rhodopsins in complex with their cognate transducers trigger on light excitation a two‐component signaling cascade which is homologous to the chemotactic signal transduction chains in enterobacteria. Important results from the latter system indicated that amplification and adaptation occur on the level of higher order receptor arrays. Here, electron microscopy and molecular dynamics data are presented which show that also sensory rhodopsins–transducer complexes can form arrays consisting of trimers of dimers. … (more)
- Is Part Of:
- Photochemistry and photobiology. Volume 93:Number 3(2017)
- Journal:
- Photochemistry and photobiology
- Issue:
- Volume 93:Number 3(2017)
- Issue Display:
- Volume 93, Issue 3 (2017)
- Year:
- 2017
- Volume:
- 93
- Issue:
- 3
- Issue Sort Value:
- 2017-0093-0003-0000
- Page Start:
- 796
- Page End:
- 804
- Publication Date:
- 2017-05
- Subjects:
- Photochemistry -- Periodicals
Light -- Physiological effect -- Periodicals
541.35 - Journal URLs:
- http://www.blackwellpublishing.com/journal.asp?ref=0031-8655&site=1 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/php.12763 ↗
- Languages:
- English
- ISSNs:
- 0031-8655
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6465.985000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2184.xml