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Spb4p, an essential putative RNA helicase, is required for a late step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae

Published online by Cambridge University Press:  01 October 1998

JESÚS DE LA CRUZ
Affiliation:
Département de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Geneva, Switzerland
DIETER KRESSLER
Affiliation:
Département de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Geneva, Switzerland
MANUEL ROJO
Affiliation:
Département de Biochimie, Sciences II, Université de Genève, CH-1211 Geneva, Switzerland
DAVID TOLLERVEY
Affiliation:
Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH93JR, United Kingdom
PATRICK LINDER
Affiliation:
Département de Biochimie Médicale, Centre Médical Universitaire, Université de Genève, CH-1211 Geneva, Switzerland
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Abstract

Spb4p is a putative ATP-dependent RNA helicase that is required for synthesis of 60S ribosomal subunits. Polysome analyses of strains genetically depleted of Spb4p or carrying the cold-sensitive spb4-1 mutation revealed an under-accumulation of 60S ribosomal subunits. Analysis of pre-rRNA processing by pulse-chase labeling, northern hybridization, and primer extension indicated that these strains exhibited a reduced synthesis of the 25S/5.8S rRNAs, due to inhibition of processing of the 27SB pre-rRNAs. At later times of depletion of Spb4p or following transfer of the spb4-1 strain to more restrictive temperatures, the early pre-rRNA processing steps at sites A0, A1, and A2 were also inhibited. Sucrose gradient fractionation showed that the accumulated 27SB pre-rRNAs are associated with a high-molecular-weight complex, most likely the 66S pre-ribosomal particle. An HA epitope-tagged Spb4p is localized to the nucleolus and the adjacent nucleoplasmic area. On sucrose gradients, HA-Spb4p was found almost exclusively in rapidly sedimenting complexes and showed a peak in the fractions containing the 66S pre-ribosomes. We propose that Spb4p is involved directly in a late and essential step during assembly of 60S ribosomal subunits, presumably by acting as an rRNA helicase.

Type
Research Article
Information
RNA , Volume 4 , Issue 10 , October 1998 , pp. 1268 - 1281
Copyright
© 1998 RNA Society

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Spb4p, an essential putative RNA helicase, is required for a late step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae
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Spb4p, an essential putative RNA helicase, is required for a late step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae
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Spb4p, an essential putative RNA helicase, is required for a late step in the assembly of 60S ribosomal subunits in Saccharomyces cerevisiae
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