Light-induced switching of HAMP domain conformation and dynamics revealed by time-resolved EPR spectroscopy

Autor(en): Klose, Daniel 
Voskoboynikova, Natalia 
Orban-Glass, Ioan
Rickert, Christian
Engelhard, Martin
Klare, Johann P.
Steinhoff, Heinz-Juergen 
Stichwörter: ARCHAEAL PHOTOTAXIS; BACTERIAL CHEMOTAXIS; Biochemistry & Molecular Biology; Biophysics; Cell Biology; Chemoreceptor; Chemotaxis; COGNATE TRANSDUCER; Coiled-coil signaling; COLI SERINE CHEMORECEPTOR; HAMP domain; MOLECULAR-DYNAMICS; PARAMAGNETIC-RESONANCE SPECTROSCOPY; Phototaxis; PROTEIN-KINASE ACTIVATION; SENSORY-RHODOPSIN-II; SIGNAL TRANSFER; Spin labeling; TRANSDUCER COMPLEX
Erscheinungsdatum: 2014
Herausgeber: WILEY
Journal: FEBS LETTERS
Volumen: 588
Ausgabe: 21
Startseite: 3970
Seitenende: 3976
Zusammenfassung: 
HAMP domains are widely abundant signaling modules. The putative mechanism of their function comprises switching between two distinct states. To unravel these conformational transitions, we apply site-directed spin labeling and time-resolved EPR spectroscopy to the phototactic receptor/transducer complex NpSRII/NpHtrII. We characterize the kinetic coupling of NpHtrII to NpSRII along with the activation period of the transducer and follow the transient conformational signal. The observed transient shift towards a more compact state of the HAMP domain upon light-activation agrees with structure-based calculations. It thereby validates the two modeled signaling states and integrates the domain's dynamics into the current model. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
ISSN: 18733468
DOI: 10.1016/j.febslet.2014.09.012

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