Variation in LOV Photoreceptor Activation Dynamics Probed by Time-Resolved Infrared Spectroscopy

The light, oxygen, voltage (LOV) domain proteins are blue light photoreceptors that utilize a noncovalently bound flavin mononucleotide (FMN) cofactor as the chromophore. The modular nature of these proteins has led to their wide adoption in the emerging fields of optogenetics and optobiology, where...

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Published in:	Biochemistry (Easton) Vol. 57; no. 5; pp. 620 - 630
Main Authors:	Iuliano, James N, Gil, Agnieszka A, Laptenok, Sergey P, Hall, Christopher R, Tolentino Collado, Jinnette, Lukacs, Andras, Hag Ahmed, Safaa A, Abyad, Jenna, Daryaee, Taraneh, Greetham, Gregory M, Sazanovich, Igor V, Illarionov, Boris, Bacher, Adelbert, Fischer, Markus, Towrie, Michael, French, Jarrod B, Meech, Stephen R, Tonge, Peter J
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 06-02-2018
Subjects:	Binding Sites Crystallography, X-Ray Cysteine - chemistry Flavin Mononucleotide - chemistry Hydrogen Bonding Models, Molecular Photobleaching Photochemistry Photoreceptors, Microbial - chemistry Photoreceptors, Microbial - radiation effects Photoreceptors, Plant - chemistry Photoreceptors, Plant - radiation effects Protein Conformation Protein Domains Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - radiation effects Spectroscopy, Fourier Transform Infrared - methods Subtraction Technique
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Summary:	The light, oxygen, voltage (LOV) domain proteins are blue light photoreceptors that utilize a noncovalently bound flavin mononucleotide (FMN) cofactor as the chromophore. The modular nature of these proteins has led to their wide adoption in the emerging fields of optogenetics and optobiology, where the LOV domain has been fused to a variety of output domains leading to novel light-controlled applications. In this work, we extend our studies of the subpicosecond to several hundred microsecond transient infrared spectroscopy of the isolated LOV domain AsLOV2 to three full-length photoreceptors in which the LOV domain is fused to an output domain: the LOV-STAS protein, YtvA, the LOV-HTH transcription factor, EL222, and the LOV-histidine kinase, LovK. Despite differences in tertiary structure, the overall pathway leading to cysteine adduct formation from the FMN triplet state is highly conserved, although there are slight variations in rate. However, significant differences are observed in the vibrational spectra and kinetics after adduct formation, which are directly linked to the specific output function of the LOV domain. While the rate of adduct formation varies by only 3.6-fold among the proteins, the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to submillisecond time scales and vary by orders of magnitude depending on the different output function of each LOV domain.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 Current address (SPL): Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology, P.O. Box 4700, Thuwal 23955-6900, Kingdom of Saudi Arabia.
ISSN:	0006-2960 1520-4995
DOI:	10.1021/acs.biochem.7b01040