RNA Helicase Prp43 and Its Co-factor Pfa1 Promote 20 to 18 S rRNA Processing Catalyzed by the Endonuclease Nob1
| Autor: | Thorsten Schäfer, David Tollervey, Marén Gnädig, Ed Hurt, Brigitte Pertschy, Claudia Schneider |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Protein Conformation Molecular Sequence Data RNA-dependent RNA polymerase Saccharomyces cerevisiae Biochemistry DEAD-box RNA Helicases RNA Precursors RNA Ribosomal 18S RNA Processing Post-Transcriptional RRNA processing Molecular Biology Base Sequence biology Nuclear Proteins RNA Helicase Cell Biology RNA Helicase A Molecular biology Cell biology RNA: Processing and Catalysis RNA editing biology.protein Nucleic Acid Conformation Degradosome PIN domain |
| Zdroj: | Journal of Biological Chemistry. 284:35079-35091 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m109.040774 |
| Popis: | Many RNA nucleases and helicases participate in ribosome biogenesis, but how they cooperate with each other is largely unknown. Here we report that in vivo cleavage of the yeast pre-rRNA at site D, the 3'-end of the 18 S rRNA, requires functional interactions between PIN (PilT N terminus) domain protein Nob1 and the DEAH box RNA helicase Prp43. Nob1 showed specific cleavage on a D-site substrate analogue in vitro, which was abolished by mutations in the Nob1 PIN domain or the RNA substrate. Genetic analyses linked Nob1 to the late pre-40 S-associated factor Ltv1, the RNA helicase Prp43, and its cofactor Pfa1. In strains lacking Ltv1, mutation of Prp43 or Pfa1 led to a striking accumulation of 20 S pre-rRNA in the cytoplasm due to inhibition of site D cleavage. This phenotype was suppressed by increased dosage of wild-type Nob1 but not by Nob1 variants mutated in the catalytic site. In ltv1/pfa1 mutants the 20 S pre-rRNA was susceptible to 3' to 5' degradation by the cytoplasmic exosome. This degraded into the 3' region of the 18 S rRNA, strongly indicating that the preribosomes are structurally defective. |
| Databáze: | OpenAIRE |
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