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Originally published as MBC in Press, 10.1091/mbc.E07-10-1074 on April 30, 2008

Vol. 19, Issue 7, 2876-2884, July 2008

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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

Submitted October 24, 2007; Revised April 10, 2008; Accepted April 18, 2008
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 co- but not posttranslational 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.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-10-1074) on April 30, 2008.

* Present address: Department of Clinical Biochemistry, University Hospital of North Stafford, Stoke on Trent, ST4 7PX, UK.

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

Abbreviations used: CPY, carboxypeptidase Y; DPAP B, dipeptidyl aminopeptidase B; ER, endoplasmic reticulum; GFP, green fluorescent protein; NAC, nascent polypeptide chain-associated complex; RAC, ribosome-associated complex; RNC, ribosome-nascent chain; SRP, signal recognition particle; SR, SRP receptor.






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