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Protein Conformational Dynamics pp 385–409Cite as

Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 805))

Abstract

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 machinery 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.

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Abbreviations

cpSRP:

chloroplast SRP

cpSR:

chloroplast SR

Ffh:

SRP54 homologous protein in bacteria and archaea

FtsY:

SRα homologous protein in bacteria and archera

GDP:

guanosine diphosphate

GTP:

guanosine triphosphate

IBD:

insertion box domain

RNC:

ribosome nascent chain complex

SRP:

signal recognition particle

SR:

SRP receptor

T.aq.:

Thermus aquaticus

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Acknowledgement

We thank Dr. Xin Zhang for his insightful comments to this manuscript. This work was supported by the National Basic Research Program of China (2013CB834604).

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  1. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Group 1101, Zhongshan Road 457, Dalian City, Liaoning Province, 116023, China

    Mingjun Yang, Xueqin Pang & Keli Han

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  1. Mingjun Yang
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Correspondence to Keli Han .

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  1. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, People's Republic of China

    Ke-li Han

  2. The Scripps Research Institute, La Jolla, California, USA

    Xin Zhang

  3. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, People's Republic of China

    Ming-jun Yang

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© 2014 Springer International Publishing Switzerland

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Yang, M., Pang, X., Han, K. (2014). Multi-state Targeting Machinery Govern the Fidelity and Efficiency of Protein Localization. In: Han, Kl., Zhang, X., Yang, Mj. (eds) Protein Conformational Dynamics. Advances in Experimental Medicine and Biology, vol 805. Springer, Cham. https://doi.org/10.1007/978-3-319-02970-2_16

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