Variation in LOV Photoreceptor Activation Dynamics Probed by Time-Resolved Infrared Spectroscopy.
Variation in LOV Photoreceptor Activation Dynamics Probed by Time-Resolved Infrared Spectroscopy.
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DOI：
10.1021/acs.biochem.7b01040
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发表时间：
2018-02-06
期刊：
影响因子：
2.9
通讯作者：
Tonge PJ
中科院分区：
文献类型：
--
作者：
Iuliano JN;Gil AA;Laptenok SP;Hall CR;Tolentino Collado J;Lukacs A;Hag Ahmed SA;Abyad J;Daryaee T;Greetham GM;Sazanovich IV;Illarionov B;Bacher A;Fischer M;Towrie M;French JB;Meech SR;Tonge PJ
光、氧、电压（LOV）结构域蛋白是蓝光光感受器，其利用非共价结合的黄素单核苷酸（FMN）辅因子作为发色团。这些蛋白质的模块化性质导致它们在光遗传学和光生物学的新兴领域中被广泛采用，其中LOV结构域已融合到各种输出结构域，从而导致新颖的光控应用。在目前的工作中，我们扩展我们的研究的亚皮秒到几百微秒的瞬态红外光谱的隔离LOV域AsLOV 2到三个全长的光感受器，其中LOV域融合到一个输出域：LOV-STAS蛋白，YtvA，LOV-HTH转录因子，EL 222，和LOV-组氨酸激酶，LovK。尽管三级结构存在差异，但导致从FMN三重态形成半胱氨酸加合物的总体途径是高度保守的，尽管速率略有变化。然而，在加合物形成后的振动光谱和动力学中观察到显着差异，这与LOV域的特定输出函数直接相关。虽然加合物形成的速率在蛋白质之间仅变化3.6倍，但全长LOV光感受器中随后的大规模结构变化发生在微米至亚毫秒的时间尺度上，并且取决于每个LOV结构域的不同输出功能而按数量级变化。
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.
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