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Dalley JA, et al.  (2008) Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation. Mol Biol Cell 19(7):2876-84

Abstract: 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.

Status: Published Type: Journal Article | Research Support, Non-U.S. Gov't PubMed ID: 18448667

Topics addressed in this paper

Number of different genes curated to this paper: 19

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Topics Genes linked to topics (#1 - 10 )
BTT1 EGD1 EGD2 HSP104 HSP60 RPL25 RPL39 SCR1 SEC61 SEC65
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Topics Genes linked to topics (#11 - 19 )
SRP14 SRP21 SRP54 SRP68 SRP72 SSA1 SSA2 STI1 ZUO1
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Protein-protein Interactions blue ball blue ball blue ball blue ball blue ball
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