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. 2016 Jul 14;44(18):9016. doi: 10.1093/nar/gkw645

The PIN domain endonuclease Utp24 cleaves pre-ribosomal RNA at two coupled sites in yeast and humans

Graeme R Wells 1, Franziska Weichmann 1, David Colvin 1, Katherine E Sloan 1, Grzegorz Kudla 2,3, David Tollervey 2, Nicholas J Watkins 1, Claudia Schneider 1,*
PMCID: PMC5062985  PMID: 27418679

Nucl. Acids Res. (2016) 44 (11): 5399–5409. doi: 10.1093/nar/gkw213

On two occasions (page 5405), the authors have misquoted a residue in Rcl1 that was shown to be important for Bms1 interaction. The correct residue is R327, and not R237 as entered in the article. The correct sentences are shown below.

Recent mutational analysis of Rcl1 based on the crystal structure of the yeast Rcl1-Bms1 dimer showed that mutation of R327, within the RDK motif, disrupts interaction with Bms1 (10). The Rcl1-Bms1 interaction is required for nuclear import of Rcl1 (34) and, consistent with this, an R327A mutation severely impaired the nucleolar localization of yeast Rcl1 (10).

10. Delprato,A., Al Kadri,Y., Perebaskine,N., Monfoulet,C., Henry,Y., Henras,A.K. and Fribourg,S. (2014) Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing. Nucleic Acids Res., 42, 10161–10172.

34. Karbstein,K., Jonas,S. and Doudna,J.A. (2005) An essential GTPase promotes assembly of preribosomal RNA processing complexes. Mol. Cell, 20, 633–643.


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