Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers.

Orekhov, Philipp; Bothe, Arne; Steinhoff, Heinz-Jürgen; Shaitan, Konstantin V; Raunser, Stefan; Fotiadis, Dimitrios José; Schlesinger, Ramona; Klare, Johann P; Engelhard, Martin (2017). Sensory Rhodopsin I and Sensory Rhodopsin II Form Trimers of Dimers in Complex with their Cognate Transducers. Photochemistry and photobiology, 93(3), pp. 796-804. Blackwell Publishing 10.1111/php.12763

[img] Text
Sensory DF.pdf - Published Version
Restricted to registered users only
Available under License Publisher holds Copyright.

Download (994kB)

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 NpSRII:NpHtrII 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.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Fotiadis, Dimitrios José

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

0031-8655

Publisher:

Blackwell Publishing

Language:

English

Submitter:

Barbara Franziska Järmann-Bangerter

Date Deposited:

22 Mar 2018 09:10

Last Modified:

05 Dec 2022 15:10

Publisher DOI:

10.1111/php.12763

PubMed ID:

28500714

BORIS DOI:

10.7892/boris.111361

URI:

https://boris.unibe.ch/id/eprint/111361

Actions (login required)

Edit item Edit item
Provide Feedback