Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 419, Issue 1-2, Pages 61-74Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2012.02.037
Keywords
LOV domains; PAS domains; NMR
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Funding
- U.S. National Institutes of Health [GM088668, 5T32GM007183-34]
- Chicago Biomedical Consortium
- Chicago Community Trust
- National Science Foundation [TG-MCB090169]
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The mechanism of light-triggered conformational change and signaling in light-oxygen-voltage (LOV) domains remains elusive in spite of extensive investigation and their use in optogenetic studies. The LOV2 domain of Avena sativa phototropin 1 (AsLOV2), a member of the Per-Arnt-Sim (PAS) family, contains a flavin mononucleotide chromophore that forms a covalent bond with a cysteine upon illumination. This event leads to the release of the carboxy-terminal J alpha helix, the biological output signal. Using mutational analysis, circular dichroism, and NMR, we find that the largely ignored amino-terminal helix is a control element in AsLOV2's light-activated conformational change. We further identify a direct amino-to-carboxy-terminal input-output signaling pathway. These findings provide a framework to rationalize the LOV domain architecture, as well as the signaling mechanisms in both isolated and tandem arrangements of PAS domains. This knowledge can be applied in engineering LOV-based photoswitches, opening up new design strategies and improving existing ones. (C) 2012 Elsevier Ltd. All rights reserved.
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