期刊
MOLECULAR BIOLOGY OF THE CELL
卷 19, 期 7, 页码 2876-2884出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E07-10-1074
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资金
- Biotechnology and Biological Sciences Research Council
- Biotechnology and Biological Sciences Research Council [C20431] Funding Source: researchfish
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.
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