Microarray analysis reveals a partial dependence of tRNA splicing on tRNA 5′ end processing

<p><b>Copyright information:</b></p><p>Taken from "Global analysis of yeast RNA processing identifies new targets of RNase III and uncovers a link between tRNA 5′ end processing and tRNA splicing"</p><p>Nucleic Acids Research 2005;33(9):3048-3056.</p><p>Published online 26 May 2005</p><p>PMCID:PMC1140755.</p><p>© The Author 2005. Published by Oxford University Press. All rights reserved</p> () Relative fluorescence of probes complementary to select tRNAs are shown with schematic diagrams below. () Relative fluorescence of LeuCAA tRNA probes is shown for the nine microarray experiments shown in . () Northern blot analysis of LeuCAA tRNA species present in TetO- and strains is shown. The same blot was probed sequentially with three different probes, as indicated by the schematic diagrams at the top of each blot (with the red line indicating the position of the probe). The identity of each tRNA species is shown to the right

Assembly factors Rpf2 and Rrs1 recruit 5S rRNA and ribosomal proteins rpL5 and rpL11 into nascent ribosomes.

More than 170 proteins are necessary for assembly of ribosomes in eukaryotes. However, cofactors that function with each of these proteins, substrates on which they act, and the precise functions of assembly factors--e.g., recruiting other molecules into preribosomes or triggering structural rearrangements of pre-rRNPs--remain mostly unknown. Here we investigated the recruitment of two ribosomal proteins and 5S ribosomal RNA (rRNA) into nascent ribosomes. We identified a ribonucleoprotein neighborhood in preribosomes that contains two yeast ribosome assembly factors, Rpf2 and Rrs1, two ribosomal proteins, rpL5 and rpL11, and 5S rRNA. Interactions between each of these four proteins have been confirmed by binding assays in vitro. These molecules assemble into 90S preribosomal particles containing 35S rRNA precursor (pre-rRNA). Rpf2 and Rrs1 are required for recruiting rpL5, rpL11, and 5S rRNA into preribosomes. In the absence of association of these molecules with pre-rRNPs, processing of 27SB pre-rRNA is blocked. Consequently, the abortive 66S pre-rRNPs are prematurely released from the nucleolus to the nucleoplasm, and cannot be exported to the cytoplasm.</p