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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geprüft am 17.05.2024
