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首页> 外文期刊>Biochemistry >Mutational and Structural Studies of the PixD BLUF Output Signal That Affects Light-Regulated Interactions with PixE
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Mutational and Structural Studies of the PixD BLUF Output Signal That Affects Light-Regulated Interactions with PixE

机译：影响与PixE进行光调节相互作用的PixD BLUF输出信号的突变和结构研究

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摘要

PixD (Slr1694) is a BLUF (blue-light-using FAD)nphotoreceptor used by the cyanobacterium Synechocystis sp.nPCC6803 to control phototaxis toward blue light. In this study, wenprobe the involvement of a conserved Tyr8u0001Gln50u0001Met93 triad innpromoting an output signal upon blue light excitation of the boundnflavin. Analysis of acrylamide quenching of Trp91 fluorescence showsnthat the side chain of this residue remains partially solvent exposed innboth the lit and dark states. Mutational analysis demonstrates thatnsubstitution mutations at Tyr8 and Gln50 result in the loss of thenphotocycle while a mutation of Met93 does not appreciably disturbnthe formation of the light-excited state and only minimally acceleratesnits decay from 5.7 to 4.5 s. However, mutations of Tyr8, Gln50, andnMet93 disrupt the ability of PixD dimers to interact with PixE to formna higher-order PixD10u0001PixE5 complex, which is indicative of a lit conformational state. Solution nuclear magnetic resonancenspectroscopy and X-ray crystallographic analyses confirm that a Tyr8 to Phe mutation is locked in a pseudo-light-excited statenrevealing flexible areas in PixD that likely constitute part of an output signal upon light excitation of wild-type PixD.
机译：PixD（Slr1694）是蓝细菌Synechocystis sp.nPCC6803使用的BLUF（使用蓝光的FAD）n感光体，用于控制向蓝光的趋光性。在这项研究中，wenprobe参与保守的Tyr8u0001Gln50u0001Met93三合体的参与，从而在结合黄素的蓝光激发下促进输出信号。 Trp91荧光的丙烯酰胺猝灭分析表明，该残基的侧链在亮和暗状态下均部分暴露于溶剂中。突变分析表明，Tyr8和Gln50处的n取代突变会导致随后的光周期损失，而Met93的突变不会明显干扰光激发态的形成，并且只会最小程度地加快纤维断裂的衰减，从5.7到4.5 s。但是，Tyr8，Gln50和nMet93的突变破坏了PixD二聚体与PixE相互作用以形成更高阶的PixD10u0001PixE5复合体的能力，这表明该构象状态是亮的。溶液核磁共振波谱法和X射线晶体学分析证实，Tyr8到Phe突变被锁定在伪光激发状态下，揭示了PixD中的柔性区域，该区域可能构成野生型PixD的光激发后输出信号的一部分。

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    《Biochemistry》 |2011年第29期|p.6365-6375|共11页
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    Hua Yuan Vladimira Dragnea Qiong Wu Kevin H. Gardner and Carl E. Bauer;

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    †Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, Indiana 47405, United States‡Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas, Texas 75390-8816, United States;

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