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Lo KY, et al.  (2009) Ribosome stalk assembly requires the dual-specificity phosphatase Yvh1 for the exchange of Mrt4 with P0. J Cell Biol 186(6):849-62

Abstract: The ribosome stalk is essential for recruitment of translation factors. In yeast, P0 and Rpl12 correspond to bacterial L10 and L11 and form the stalk base of mature ribosomes, whereas Mrt4 is a nuclear paralogue of P0. In this study, we show that the dual-specificity phosphatase Yvh1 is required for the release of Mrt4 from the pre-60S subunits. Deletion of YVH1 leads to the persistence of Mrt4 on pre-60S subunits in the cytoplasm. A mutation in Mrt4 at the protein-RNA interface bypasses the requirement for Yvh1. Pre-60S subunits associated with Yvh1 contain Rpl12 but lack both Mrt4 and P0. These results suggest a linear series of events in which Yvh1 binds to the pre-60S subunit to displace Mrt4. Subsequently, P0 loads onto the subunit to assemble the mature stalk, and Yvh1 is released. The initial assembly of the ribosome with Mrt4 may provide functional compartmentalization of ribosome assembly in addition to the spatial separation afforded by the nuclear envelope.

Status: Published Type: Journal Article | Research Support, N.I.H., Extramural | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, Non-P.H.S. PubMed ID: 19797078

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Topics Genes linked to topics
MRT4 RPL12A RPL12B RPP0 YVH1
Cellular Location blue ball blue ball blue ball
Cross-species Expression blue ball
Function/Process blue ball blue ball blue ball
Genetic Interactions blue ball blue ball blue ball blue ball
Mutants/Phenotypes blue ball blue ball blue ball blue ball
Non-Fungal Related Genes/Proteins blue ball blue ball
Primary Literature blue ball blue ball blue ball blue ball blue ball
Protein Processing/Modification/Regulation blue ball
Protein Sequence Features blue ball
Protein-protein Interactions blue ball blue ball
Protein/Nucleic Acid Structure blue ball
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