The precise function of the RNA helicases in ribosome synthesis

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A new study published in Nature Communications sheds light on the molecular function of one of the enzymes with RNA helicase activity involved in the synthesis process of the large ribosome subunit. By combining biochemical, genetic and molecular techniques and making use of the model organism Saccharomyces cerevisiae, this study shows that the small nucleolar RNA snR190 functions as an RNA chaperone that makes it possible to initiate the compaction of ribosomal RNA precursors into early pre-ribosomal particles.

In addition, this work demonstrates that the RNA helicase Dbp7 is the enzyme responsible for the specific dissociation of the snR190 complex from ribosomal RNA precursors, thus enabling the progression of the maturation of the ribosoma's peptidyl transferase center.

The group led by Jesús de la Cruz at the Institute of Biomedicine of Seville focuses on the of the biogenesis process of the eukaryotic cytoplasmic ribosome, using both the microorganism Saccharomyces cerevisiae and several human cell lines as biological study models.

Other lines of research are the study of point mutations of ribosomal proteins linked to human ribosomopathies, the relationship between ribosomal assembly factors and cell cycle progression and finally, in collaboration with the "Oncological Surgery" group of IBiS, the molecular impact of the drug Sorafenib on synthesis, translation and in human hepatocarcinoma cells.

More information: Mariam Jaafar et al, Association of snR190 snoRNA chaperone with early pre-60S particles is regulated by the RNA helicase Dbp7 in yeast, Nature Communications (2021). DOI: 10.1038/s41467-021-26207-w

Journal information: Nature Communications

Citation: The precise function of the RNA helicases in ribosome synthesis (2021, November 3) retrieved 6 February 2023 from
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