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Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization
Yang, Mingjun; Pang, Xueqin; Han, Keli; Han, KL; Zhang, X; Yang, MJ
关键词Signal Recognition Particle Protein Targeting Protein Localization Molecular Machinery Protein Machinery Protein Conformational Dynamics Principal Component Analysis Targeted Molecular Dynamics
刊名PROTEIN CONFORMATIONAL DYNAMICS
2014
DOI10.1007/978-3-319-02970-2_16
805页:385-409
收录类别BSCI ; SCI
文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biology ; Medicine, Research & Experimental
研究领域[WOS]Life Sciences & Biomedicine - Other Topics ; Research & Experimental Medicine
关键词[WOS]SIGNAL-RECOGNITION-PARTICLE ; MEASURING CONFORMATIONAL DYNAMICS ; SRP-RECEPTOR INTERACTION ; MOLECULAR-ORBITAL METHOD ; CRYSTAL-STRUCTURE ; GTPASE ACTIVATION ; STRUCTURAL BASIS ; NG DOMAIN ; FLUORESCENCE SPECTROSCOPY ; CRYOELECTRON MICROSCOPY
英文摘要Proper localization of newly synthesized proteins is essential to cellular function. Among different protein localization modes, the signal recognition particle (SRP) and SRP receptor (SR) constitute the conserved targeting machinery in all three life kingdoms and mediate about one third of the protein targeting reactions. Based on experimental and computational studies, a detailed molecular model is proposed to explain how this molecular machinery governs the efficiency and fidelity of protein localizations. In this targeting machinery, two distinct SRP GTPases are contained into the SRP and SR that are responsible to the interactions between SRP and SR. These two GTPases can interact with one another through a series of sequential and discrete interaction states that are the early intermediate formation, stable complex association, and GTPase activation. In contrast to canonical GTPases, a floppy and open conformation adopted in free SRP GTPases can facilitate efficient GTP/GDP exchange without the aid of any external factors. As the apo-form free SRP GTPases can adopt the conformational states of GDP- or GTP-bound form, the binding of GTP/GDP follows a mechanism of conformational selection. In the first step of complex formation, the two SRP GTPases can rapidly assemble into an unstable early intermediate by selecting and stabilizing one another's primed states from the equilibrium conformational ensemble. Subsequently, extensive inter-and intra-domain changes rearrange the early complex into a tight and closed state of stable complex through induced fit mechanism. Upon stable complex association, further tune of several important interaction networks activates the SRP GTPase for GTP hydrolysis. These different conformational states are coupled to corresponding protein targeting events, in which the complex formation deliveries the translating ribosome to the target membrane and the GTPase activation couples to the cargo release from SRP-SR SRmachinery to the translocation channel. It is thus suggested that the SRP GTPases constitute a self-sufficient system to execute exquisite spatial and temporal control of the complex targeting process. The working mechanism of the SRP and SR provides a novel paradigm of how the protein machinery functions in controlling diverse biological processes efficiently and faithfully.
语种英语
WOS记录号WOS:000350417100016
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被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/145509
专题中国科学院大连化学物理研究所
作者单位Chinese Acad Sci, Dalian Inst Chem Phys, Grp 1101, Dalian 116023, Liaoning Provin, Peoples R China
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GB/T 7714
Yang, Mingjun,Pang, Xueqin,Han, Keli,et al. Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization[J]. PROTEIN CONFORMATIONAL DYNAMICS,2014,805:385-409.
APA Yang, Mingjun,Pang, Xueqin,Han, Keli,Han, KL,Zhang, X,&Yang, MJ.(2014).Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization.PROTEIN CONFORMATIONAL DYNAMICS,805,385-409.
MLA Yang, Mingjun,et al."Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization".PROTEIN CONFORMATIONAL DYNAMICS 805(2014):385-409.
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