Structure and assembly of the Alu domain of the mammalian signal recognition particle

Oliver Weichenrieder, Klemens Wild, Katharina Strub and Stephen Cusack ()
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Oliver Weichenrieder: European Molecular Laboratory Biology, Grenoble Outstation, BP 156X
Klemens Wild: European Molecular Laboratory Biology, Grenoble Outstation, BP 156X
Katharina Strub: Sciences III
Stephen Cusack: European Molecular Laboratory Biology, Grenoble Outstation, BP 156X

Nature, 2000, vol. 408, issue 6809, 167-173

Abstract: Abstract The Alu domain of the mammalian signal recognition particle (SRP) comprises the heterodimer of proteins SRP9 and SRP14 bound to the 5′ and 3′ terminal sequences of SRP RNA. It retards the ribosomal elongation of signal-peptide-containing proteins before their engagement with the translocation machinery in the endoplasmic reticulum. Here we report two crystal structures of the heterodimer SRP9/14 bound either to the 5′ domain or to a construct containing both 5′ and 3′ domains. We present a model of the complete Alu domain that is consistent with extensive biochemical data. SRP9/14 binds strongly to the conserved core of the 5′ domain, which forms a U-turn connecting two helical stacks. Reversible docking of the more weakly bound 3′ domain might be functionally important in the mechanism of translational regulation. The Alu domain structure is probably conserved in other cytoplasmic ribonucleoprotein particles and retroposition intermediates containing SRP9/14-bound RNAs transcribed from Alu repeats or related elements in genomic DNA.

Date: 2000
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DOI: 10.1038/35041507

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