The H/ACA RNP assembly factor SHQ1 functions as an RNA mimic

Hélène Walbott, Rosario Machado-Pinilla, Dominique Liger, Magali Blaud, Stéphane Réty, Petar N. Grozdanov, Kate Godin, Herman van Tilbeurgh, Gabriele Varani, U. Thomas Meier, Nicolas Leulliot

Research output: Contribution to journalArticlepeer-review

30 Scopus citations

Abstract

SHQ1 is an essential assembly factor for H/ACA ribonucleoproteins (RNPs) required for ribosome biogenesis, premRNA splicing, and telomere maintenance. SHQ1 binds dyskerin/NAP57, the catalytic subunit of human H/ACA RNPs, and this interaction is modulated by mutations causing X-linked dyskeratosis congenita. We report the crystal structure of the C-terminal domain of yeast SHQ1, Shq1p, and its complex with yeast dyskerin/NAP57, Cbf5p, lacking its catalytic domain. The C-terminal domain of Shq1p interacts with the RNA-binding domain of Cbf5p and, through structural mimicry, uses the RNA-protein-binding sites to achieve a specific protein-protein interface. We propose that Shq1p operates as a Cbf5p chaperone during RNP assembly by acting as an RNA placeholder, thereby preventing Cbf5p from nonspecific RNA binding before association with an H/ACA RNA and the other core RNP proteins.

Original languageEnglish (US)
Pages (from-to)23982408
Number of pages1
JournalGenes and Development
Volume25
Issue number22
DOIs
StatePublished - 2011

Keywords

  • H/ACA RNPs
  • Ribonucleoprotein assembly
  • Telomerase
  • X-linked dyskeratosis congenita

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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