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J Phys Chem Lett. 2015 Sep 3;6(17):3379-83. doi: 10.1021/acs.jpclett.5b01629. Epub 2015 Aug 14.

Ubiquitous Structural Signaling in Bacterial Phytochromes.

Author information

1
Department of Chemistry and Molecular Biology, University of Gothenburg , Box 462, 40530 Gothenburg, Sweden.
2
Nanoscience Center, Department of Biological and Environmental Science, University of Jyväskylä , 40014 Jyväskylä, Finland.
3
Department of Biology, Northeastern Illinois University , 5500 North St. Louis Avenue, Chicago, Illinois 60625, United States.
4
Botanical Institute, Karlsruhe Institute of Technology KIT , Kaiserstr. 2, 76131 Karlsruhe, Germany.
5
Centre for Advanced Molecular Imaging, La Trobe Institute for Molecular Science, La Trobe University , Melbourne, Victoria 3086, Australia.
6
MAX IV Laboratory, Lund University , P.O. Box 118, Lund SE-221 00, Sweden.
7
Paul Scherrer Institut , 5232 Villigen PSI, Switzerland.

Abstract

The phytochrome family of light-switchable proteins has long been studied by biochemical, spectroscopic and crystallographic means, while a direct probe for global conformational signal propagation has been lacking. Using solution X-ray scattering, we find that the photosensory cores of several bacterial phytochromes undergo similar large-scale structural changes upon red-light excitation. The data establish that phytochromes with ordinary and inverted photocycles share a structural signaling mechanism and that a particular conserved histidine, previously proposed to be involved in signal propagation, in fact tunes photoresponse.

KEYWORDS:

X-ray scattering; phytochromes; protein dynamics; signal transduction

PMID:
26275765
DOI:
10.1021/acs.jpclett.5b01629
[Indexed for MEDLINE]

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