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题名: Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization
作者: Yang, Mingjun1;  Pang, Xueqin1;  Han, Keli1;  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
发表日期: 2014
DOI: 10.1007/978-3-319-02970-2_16
卷: 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
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.
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
语种: 英语
WOS记录号: WOS:000350417100016
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/145509
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Acad Sci, Dalian Inst Chem Phys, Grp 1101, Dalian 116023, Liaoning Provin, Peoples R China

Recommended Citation:
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.
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