❶The different Rpl4a constructs are schematically depicted on the right; the colour code to indicate the different features of Rpl4 is as in Fig 1C. Western blot analysis was carried out according to standard protocols. Deletion disruption and C-terminal tagging at the genomic locus were performed as described [ 5354 ].
Finley D, Bartel B, Varshavsky A The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Senior Service. One group with six sequences was excluded since it did not contain the characteristic TPR-repeat domain of this family. Old Castle. Pall Mall.
F, Acl4 is not associated with 60S subunits or translating ribosomes. Notably, the NLS region defined by amino acids 43— corresponds to the long internal loop of Rpl4. Additionally, it is also possible that Rpl4, imported via an Acl4-independent route, will encounter and be transferred to an Acl4 molecule in Firbourg nucleoplasm.
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The main principles underlying the making of ribosomes are conserved across eukaryotic organisms and this process has been studied in most detail in the yeast Saccharomyces cerevisiae.
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Most r-proteins need to be transported escorh the cytoplasm to the nucleus where they get incorporated into the evolving pre-ribosomal particles.
Due to the high abundance and difficult physicochemical properties of r-proteins, their correct folding and fail-safe targeting to the assembly site depends largely on general, as well as highly specialized, chaperone Kusnacht massage arrests transport systems.
The 60S r-protein Rpl4 is particularly interesting since it harbours a conserved long internal loop and a prominent C-terminal eukaryote-specific extension. Here we show that both the long internal loop and the C-terminal eukaryote-specific extension are strictly required for the functionality of Rpl4.
While Rpl4 contains at least five distinct nuclear localization signals NLSthe C-terminal part of the long internal loop associates with a specific binding partner, termed Acl4.
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Absence of Acl4 confers a severe slow-growth phenotype and a deficiency in the production of 60S subunits. Genetic and biochemical evidence indicates that Acl4 can be considered as a dedicated chaperone of Rpl4.
Notably, Acl4 localizes to both the cytoplasm and nucleus and it has the capacity to capture nascent Rpl4 in a co-translational manner. Taken together, our findings indicate that the dedicated chaperone Acl4 accompanies Rpl4 from the cytoplasm to its preS assembly site in the nucleus. Ribosomes are the molecular machines that generate proteins from mRNA templates.
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