Selected article for: "complex formation and novel mechanism"
Author: Ivanova, Elena; Berger, Audrey; Scherrer, Anne; Alkalaeva, Elena; Strub, Katharina
Title: Alu RNA regulates the cellular pool of active ribosomes by targeted delivery of SRP9/14 to 40S subunits
  • Document date: 2015_3_11
    • ID: 64cnoqpi_7
    Snippet: In the present study, we have investigated the role of Alu RNPs in regulating translation using both a rabbit reticulocyte lysate and a mammalian translation system reconstituted from purified components. Our studies demonstrate that Alu RNPs interfere with the formation of the 48S complex by a novel mechanism in which Alu RNPs act directly on the 40S ribosomal subunit to prevent its association with the mRNA. Moreover, the SRP9/14 protein dimer .....
    Document: In the present study, we have investigated the role of Alu RNPs in regulating translation using both a rabbit reticulocyte lysate and a mammalian translation system reconstituted from purified components. Our studies demonstrate that Alu RNPs interfere with the formation of the 48S complex by a novel mechanism in which Alu RNPs act directly on the 40S ribosomal subunit to prevent its association with the mRNA. Moreover, the SRP9/14 protein dimer constitutes the inhibitory component, which has to be transferred to 40S by the Alu RNA. This mechanism efficiently inhibits cap-dependent as well as IRES-mediated translation initiation. Overexpression of Alu RNA in HEK 293T cells inhibits in an SRP9/14-dependent fashion translation of mR-NAs that initiate protein synthesis de novo. Our results are consistent with a physiological role of Alu RNPs in the translational response to viral infection and stress.

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