Rrp5 binding at multiple sites coordinates pre-rRNA processing and assembly

Simon Lebaron, Asa Segerstolpe, Sarah L French, Tatiana Dudnakova, Flavia de Lima Alves, Sander Granneman, Juri Rappsilber, Ann L Beyer, Lars Wieslander, David Tollervey

Research output: Contribution to journalArticlepeer-review


In vivo UV crosslinking identified numerous preribosomal RNA (pre-rRNA) binding sites for the large, highly conserved ribosome synthesis factor Rrp5. Intramolecular complementation has shown that the C-terminal domain (CTD) of Rrp5 is required for pre-rRNA cleavage at sites A0-A2 on the pathway of 18S rRNA synthesis, whereas the N-terminal domain (NTD) is required for A3 cleavage on the pathway of 5.8S/25S rRNA synthesis. The CTD was crosslinked to sequences flanking A2 and to the snoRNAs U3, U14, snR30, and snR10, which are required for cleavage at A0-A2. The NTD was crosslinked to sequences flanking A3 and to the RNA component of ribonuclease MRP, which cleaves site A3. Rrp5 could also be directly crosslinked to several large structural proteins and nucleoside triphosphatases. A key role in coordinating preribosomal assembly and processing was confirmed by chromatin spreads. Following depletion of Rrp5, cotranscriptional cleavage was lost and preribosome compaction greatly reduced.
Original languageEnglish
Pages (from-to)707-19
Number of pages13
JournalMolecular Cell
Issue number5
Publication statusPublished - 12 Dec 2013


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