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MBC in Press, published online ahead of print April 30, 2008
Mol. Biol. Cell 10.1091/mbc.E07-10-1074

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Submitted on October 24, 2007
Revised on April 10, 2008
Accepted on April 18, 2008

Access to Ribosomal Protein Rpl25p by the Signal Recognition Particle Is Required for Efficient Cotranslational Translocation

Jane A. Dalley,* Alexander Selkirk, and Martin R. Pool

Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom

Monitoring Editor: Reid Gilmore

Targeting of proteins to the endoplasmic reticulum (ER) occurs cotranslationally necessitating the interaction of the signal recognition particle (SRP) and the translocon with the ribosome. Biochemical and structural studies implicate ribosomal protein Rpl25p as a major ribosome interaction site for both these factors. Here we characterize an RPL25GFP fusion, which behaves as a dominant mutant leading to defects in cobut not post-translational translocation in vivo. In these cells, ribosomes still interact with ER membrane and the translocon, but are defective in binding SRP. Overexpression of SRP can restore ribosome binding of SRP, but only partially rescues growth and translocation defects. Our results indicate that Rpl25p plays a critical role in the recruitment of SRP to the ribosome.

*Present Address: Department of Clinical Biochemistry, University Hospital of North Stafford, Stoke-on-Trent ST4 7PX, United Kingdom.

Address correspondence to: Martin R. Pool (martin.r.pool{at}manchester.ac.uk)






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