Transmembrane signal transduction in archaeal phototaxis: The sensory rhodopsin II-transducer complex studied by electron paramagnetic resonance spectroscopy

Autor(en): Klare, Johann P.
Bordignon, Enrica
Engelhard, Martin
Steinhoff, Heinz-Juergen 
Stichwörter: ACCEPTING TAXIS PROTEINS; Cell Biology; Chemotaxis; CONFORMATIONAL-CHANGES; Electron paramagnetic resonance spectroscopy; HAMP DOMAIN; HELIX F; NATRONOBACTERIUM-PHARAONIS; NATRONOMONAS-PHARAONIS; Phototaxis; PROTON TRANSPORT; RECEPTOR; SERINE CHEMOTAXIS; Signal transduction; Site-directed spin labelling; STRUCTURAL-CHANGES; Transmembrane signalling
Erscheinungsdatum: 2011
Herausgeber: ELSEVIER GMBH
Journal: EUROPEAN JOURNAL OF CELL BIOLOGY
Volumen: 90
Ausgabe: 9
Startseite: 731
Seitenende: 739
Zusammenfassung: 
Archaeal photoreceptors, together with their cognate transducer proteins, mediate phototaxis by regulating cell motility through two-component signal transduction pathways. This sensory pathway is closely related to the bacterial chemotactic system, which has been studied in detail during the past 40 years. Structural and functional studies applying site-directed spin labelling and electron paramagnetic resonance spectroscopy on the sensory rhodopsin II/transducer (NpSRII/NpHtrIl) complex of Natronomonas pharaonis have yielded insights into the structure, the mechanisms of signal perception, the signal transduction across the membrane and provided information about the subsequent information transfer within the transducer protein towards the components of the intracellular signalling pathway. Here, we provide an overview about the findings of the last decade, which, combined with the wealth of data from research on the Escherichia colt chemotaxis system, served to understand the basic principles microorganisms use to adapt to their environment. We document the time course of a signal being perceived at the membrane, transferred across the membrane and, for the first time, how this signal modulates the dynamic properties of a HAMP domain, a ubiquitous signal transduction module found in various protein classes. (C) 2011 Elsevier GmbH. All rights reserved.
ISSN: 01719335
DOI: 10.1016/j.ejcb.2011.04.013

Zur Langanzeige

Seitenaufrufe

1
Letzte Woche
0
Letzter Monat
0
geprüft am 16.05.2024

Google ScholarTM

Prüfen

Altmetric