Faculty Opinions recommendation of Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.

Author(s):  
Elena Conti
Science ◽  
2014 ◽  
Vol 344 (6179) ◽  
pp. 101-104 ◽  
Author(s):  
Jan Timo Grotwinkel ◽  
Klemens Wild ◽  
Bernd Segnitz ◽  
Irmgard Sinning

The signal recognition particle (SRP) is central to membrane protein targeting; SRP RNA is essential for SRP assembly, elongation arrest, and activation of SRP guanosine triphosphatases. In eukaryotes, SRP function relies on the SRP68-SRP72 heterodimer. We present the crystal structures of the RNA-binding domain of SRP68 (SRP68-RBD) alone and in complex with SRP RNA and SRP19. SRP68-RBD is a tetratricopeptide-like module that binds to a RNA three-way junction, bends the RNA, and inserts an α-helical arginine-rich motif (ARM) into the major groove. The ARM opens the conserved 5f RNA loop, which in ribosome-bound SRP establishes a contact to ribosomal RNA. Our data provide the structural basis for eukaryote-specific, SRP68-driven RNA remodeling required for protein translocation.


2011 ◽  
Vol 18 (3) ◽  
pp. 389-391 ◽  
Author(s):  
Tobias Hainzl ◽  
Shenghua Huang ◽  
Gitte Meriläinen ◽  
Kristoffer Brännström ◽  
A Elisabeth Sauer-Eriksson

1999 ◽  
Vol 98 (2) ◽  
pp. 253-264 ◽  
Author(s):  
Staffan G. Svärd ◽  
Colleen Rafferty ◽  
J.Michael McCaffery ◽  
Michael W. Smith ◽  
David S. Reiner ◽  
...  

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