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

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    acs.biochem.7b01040.pdf
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    Type
    Article
    Authors
    Iuliano, James N.
    Gil, Agnieszka A.
    Laptenok, Siarhei cc
    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
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Date
    2018-01-04
    Online Publication Date
    2018-01-04
    Print Publication Date
    2018-02-06
    Permanent link to this record
    http://hdl.handle.net/10754/626423
    
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    Abstract
    The light, oxygen, voltage (LOV) domain proteins are blue light photoreceptors that utilize a non-covalently 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 the present work, we extend our studies of the sub-picosecond 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 amongst the proteins, the subsequent large-scale structural changes in the full-length LOV photoreceptors occur over the micro- to sub-millisecond timescales and vary by orders of magnitude depending on the different output function of each LOV domain.
    Citation
    Iuliano JN, Gil AA, Laptenok SP, Hall CR, Tolentino Collado J, et al. (2017) Variation in LOV Photoreceptor Activation Dynamics Probed by Time Resolved Infrared Spectroscopy. Biochemistry. Available: http://dx.doi.org/10.1021/acs.biochem.7b01040.
    Sponsors
    We are grateful to STFC for access to the ULTRA laser facility. We are grateful to Professor Ray Owens and Anil Verma for assistance in protein preparation and access to the Oxford Protein Production Facility-UK.
    Publisher
    American Chemical Society (ACS)
    Journal
    Biochemistry
    DOI
    10.1021/acs.biochem.7b01040
    Additional Links
    http://pubs.acs.org/doi/10.1021/acs.biochem.7b01040
    ae974a485f413a2113503eed53cd6c53
    10.1021/acs.biochem.7b01040
    Scopus Count
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    Articles; Biological and Environmental Science and Engineering (BESE) Division

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