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Title [sv]
Strukturella och funktionella studier på den signaligenkännande partikeln
Title [en]
Structural and functional studies on the signal recognition particle
Abstract [sv]
Our work is focused on structural and functional studies of the signal recognition particle (SRP) based on crystallographic methods. The SRP is a multi-subunit ribonucleoprotein found in all three kingdoms of life, which reflects its significance for protein targeting in normal cell function. Signal-sequence binding to SRP54 at the ribosome, leads to GTP and receptor binding, followed by mutual GTP hydrolysis. We have previously determined the structures of a 97-nt fragment of free SRPRNA, the complex of SRP19 and SRPRNA, and the complex of SRP19, SRP54 and SRPRNA (ternary complex). Recently we solved the 3.2 Å structure of a variant of the ternary complex, where an artificial linker is added to SRP54 (SRP54+ss) including the 15 residue hydrophobic signal sequence. The signal sequence is clearly visible in our structure, and when this work is completed, we will for the first time report the proper signal-sequence binding site in SRP54. In support, GTP hydrolysis studies show that only the SRP54+ss ternary complex can hydrolyze GTP in the presence of the receptor FtsY, verifying proper function of the complex. Work on the quaternary structure including SRP54+ss, GTP analogues, and FtsY is in progress and we have crystals diffracting at 4Å. In parallel with the structural work, mutagenesis and biochemical studies will be carried out, which will direct us towards a full understanding of SRP function.
Principal InvestigatorSauer-Eriksson, Elisabeth
Coordinating organisation
Umeå University
Funder
Period
2009-01-01 － 2011-12-31
Identifiers
DiVA, id: project:863Project, id: 2008-04303_VR

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