Light-induced switching of HAMP domain conformation and dynamics revealed by time-resolved EPR spectroscopy

Light-induced switching of HAMP domain conformation and dynamics revealed by time-resolved EPR spectroscopy
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DOI:
10.1016/j.febslet.2014.09.012
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发表时间:
2014-11-03
期刊:
影响因子:
3.5
通讯作者:
Steinhoff, Heinz-Juergen
Steinhoff, Heinz-Juergen
中科院分区:
生物学3区
文献类型:
--
作者:
Klose, Daniel;Voskoboynikova, Natalia;Steinhoff, Heinz-Juergen

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HAMP结构域是广泛丰富的信号传导模块。其功能的假定机制包括在两种不同状态之间切换。为了解开这些构象转变,我们应用定点自旋标记和时间分辨EPR光谱的趋光受体/换能器复合物NpSRII/NpHtrII。我们表征NpHtrII到NpSRII的动力学耦合沿着与换能器的激活期,并遵循瞬态构象信号。所观察到的瞬态转变朝着一个更紧凑的状态的HAMP域光激活后同意基于结构的计算。从而验证了两个建模的信令状态,并将域的动态集成到当前模型中。(C)2014年欧洲生物化学学会联合会。Elsevier B. V.出版,保留所有权利。
HAMP domains are widely abundant signaling modules. The putative mechanism of their function comprises switching between two distinct states. To unravel these conformational transitions, we apply site-directed spin labeling and time-resolved EPR spectroscopy to the phototactic receptor/transducer complex NpSRII/NpHtrII. We characterize the kinetic coupling of NpHtrII to NpSRII along with the activation period of the transducer and follow the transient conformational signal. The observed transient shift towards a more compact state of the HAMP domain upon light-activation agrees with structure-based calculations. It thereby validates the two modeled signaling states and integrates the domain's dynamics into the current model. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.