4.8 Article

Nol9 is a novel polynucleotide 5′-kinase involved in ribosomal RNA processing

Journal

EMBO JOURNAL
Volume 29, Issue 24, Pages 4161-4171

Publisher

WILEY
DOI: 10.1038/emboj.2010.275

Keywords

nucleolus; polynucleotide kinase; ribosomal RNA; ribosomal RNA processing

Funding

  1. Austrian Government
  2. IMBA
  3. [FWF-P20502-B11]
  4. Austrian Science Fund (FWF) [W1207] Funding Source: Austrian Science Fund (FWF)

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In a cell, an enormous amount of energy is channelled into the biogenesis of ribosomal RNAs (rRNAs). In a multistep process involving a large variety of ribosomal and non-ribosomal proteins, mature rRNAs are generated from a long polycistronic precursor. Here, we show that the non-ribosomal protein Nol9 is a polynucleotide 5'-kinase that sediments primarily with the pre-60S ribosomal particles in HeLa nuclear extracts. Depletion of Nol9 leads to a severe impairment of ribosome biogenesis. In particular, the polynucleotide kinase activity of Nol9 is required for efficient generation of the 5.8S and 28S rRNAs from the 32S precursor. Upon Nol9 knockdown, we also observe a specific maturation defect at the 5' end of the predominant 5.8S short-form rRNA (5.8S(S)), possibly due to the Nol9 requirement for 5'>3' exonucleolytic trimming. In contrast, the endonuclease-dependent generation of the 5'-extended, minor 5.8S long-form rRNA (5.8S(L)) is largely unaffected. This is the first report of a nucleolar polynucleotide kinase with a role in rRNA processing. The EMBO Journal (2010) 29, 4161-4171. doi: 10.1038/emboj.2010.275; Published online 9 November 2010

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