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Signal-sequence induced conformational changes in the signal recognition particle

a , 1 , b , 1

Nature Communications

Nature Pub. Group

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Abstract

Co-translational protein targeting is an essential, evolutionarily conserved pathway for delivering nascent proteins to the proper cellular membrane. In this pathway, the signal recognition particle (SRP) first recognizes the N-terminal signal sequence of nascent proteins and subsequently interacts with the SRP receptor. For this, signal sequence binding in the SRP54 M domain must be effectively communicated to the SRP54 NG domain that interacts with the receptor. Here we present the 2.9 Å crystal structure of unbound- and signal sequence bound SRP forms, both present in the asymmetric unit. The structures provide evidence for a coupled binding and folding mechanism in which signal sequence binding induces the concerted folding of the GM linker helix, the finger loop, and the C-terminal alpha helix αM6. This mechanism allows for a high degree of structural adaptability of the binding site and suggests how signal sequence binding in the M domain is coupled to repositioning of the NG domain.

Abstract

The signal recognition particle plays a key role in the co-translational protein targeting of membrane and secretory proteins. Here the authors report a crystal structure of the ternary SRP complex in signal sequence bound and unbound forms, providing insight into how signal sequence binding is coupled to SRP receptor interaction.

Most cited references36

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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Features and development of Coot

(2010)
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XDS

(2010)
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Author and article information

Affiliations
[1 ]Department of Chemistry, Umeå University , Umeå SE-901 87, Sweden
Journal
Nat Commun
Nat Commun
Nature Communications
Nature Pub. Group
2041-1723
08 June 2015
2015
: 6
26051119
4468861
ncomms8163
10.1038/ncomms8163