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Lookup NU author(s): Dr Graeme WellsORCiD, Franziska Weichmann, Kate Sloan, David Colvin, Dr Nick Watkins, Dr Claudia SchneiderORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Two proteins with PIN endonuclease domains, yUtp24(Fcf1)/hUTP24 and yUtp23/hUTP23 are essential for early pre-ribosomal (r)RNA cleavages at sites A0, A1/1 and A2/2a in yeast and humans. The yUtp24/hUTP24 PIN endonuclease is proposed to cleave at sites A1/1 and A2/2a, but the enzyme cleaving at site A0 is not known. Yeast yUtp23 contains a degenerate, non-essential PIN domain and functions together with the snR30 snoRNA, while human hUTP23 is associated with U17, the human snR30 counterpart. Using in vivo RNA–protein crosslinking and gel shift experiments, we reveal that yUtp23/hUTP23 makes direct contacts with expansion sequence 6 (ES6) in the 18S rRNA sequence and that yUtp23 interacts with the 3′ half of the snR30 snoRNA. Protein–protein interaction studies further demonstrated that yeast yUtp23 and human hUTP23 directly interact with the H/ACA snoRNP protein yNhp2/hNHP2, the RNA helicase yRok1/hROK1(DDX52), the ribosome biogenesis factor yRrp7/hRRP7 and yUtp24/hUTP24. yUtp23/hUTP23 could therefore be central to the coordinated integration and release of ES6 binding factors and likely plays a pivotal role in remodeling this pre-rRNA region in both yeast and humans. Finally, studies using RNAi-rescue systems in human cells revealed that intact PIN domain and Zinc finger motifs in human hUTP23 are essential for 18S rRNA maturation.
Author(s): Wells GR, Weichmann F, Sloan KE, Colvin D, Watkins NJ, Schneider C
Publication type: Article
Publication status: Published
Journal: Nucleic Acids Research
Year: 2017
Volume: 45
Issue: 8
Pages: 4796-4809
Print publication date: 05/05/2017
Online publication date: 12/01/2017
Acceptance date: 22/12/2016
Date deposited: 13/01/2017
ISSN (print): 0305-1048
ISSN (electronic): 1362-4962
Publisher: Oxford University Press
URL: http://dx.doi.org/10.1093/nar/gkw1344
DOI: 10.1093/nar/gkw1344
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