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Dbp9p, a putative ATP-dependent RNA helicase involved in 60S-ribosomal-subunit biogenesis, functionally interacts with Dbp6p

Published online by Cambridge University Press:  25 September 2001

MARIE-CLAIRE DAUGERON
Affiliation:
Département de Biochimie médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Genève 4, Switzerland Present address: Equipe “Epissage et dégradation des ARNs messagers eucaryotes”, Bat 24 CGM CNRS, Avenue de la Terrasse, 91198 Gif sur Yvette, Cedex, France.
DIETER KRESSLER
Affiliation:
Département de Biochimie médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Genève 4, Switzerland Present address: Division of Biochemistry, Biozentrum of the University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
PATRICK LINDER
Affiliation:
Département de Biochimie médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Genève 4, Switzerland
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Abstract

Ribosome synthesis is a highly complex process and constitutes a major cellular activity. The biogenesis of this ribonucleoprotein assembly requires a multitude of protein trans-acting factors including several putative ATP-dependent RNA helicases of the DEAD-box and related protein families. Here we show that the previously uncharacterized Saccharomyces cerevisiae open reading frame YLR276C, hereafter named DBP9 (DEAD-box protein 9), encodes an essential nucleolar protein involved in 60S-ribosomal-subunit biogenesis. Genetic depletion of Dbp9p results in a deficit in 60S ribosomal subunits and the appearance of half-mer polysomes. This terminal phenotype is likely due to the instability of early pre-ribosomal particles, as evidenced by the low steady-state levels and the decreased synthesis of the 27S precursors to mature 25S and 5.8S rRNAs. In agreement with a role of Dbp9p in 60S subunit synthesis, we find that increased Dbp9p dosage efficiently suppresses certain dbp6 alleles and that dbp6/dbp9 double mutants show synthetic lethality. Furthermore, Dbp6p and Dbp9p weakly interact in a yeast two-hybrid assay. Altogether, our findings indicate an intimate functional interaction between Dbp6p and Dbp9p during the process of 60S-ribosomal-subunit assembly.

Type
Research Article
Information
RNA , Volume 7 , Issue 9 , September 2001 , pp. 1317 - 1334
Copyright
2001 RNA Society

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