Yeast and human RNA helicases involved in ribosome biogenesis: Current status and perspectives
Ribosome biogenesis is a fundamental process that is conserved in eukaryotes. Although spectacular progress has been made in understanding mammalian ribosome synthesis in recent years, by far, this process has still been best characterised in the yeast Saccharomyces cerevisiae. In yeast, besides the...
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Veröffentlicht in: | Biochimica et biophysica acta 2013-08, Vol.1829 (8), p.775-790 |
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Zusammenfassung: | Ribosome biogenesis is a fundamental process that is conserved in eukaryotes. Although spectacular progress has been made in understanding mammalian ribosome synthesis in recent years, by far, this process has still been best characterised in the yeast Saccharomyces cerevisiae. In yeast, besides the rRNAs, the ribosomal proteins and the 75 small nucleolar RNAs, more than 250 non-ribosomal proteins, generally referred to as trans-acting factors, are involved in ribosome biogenesis. These factors include nucleases, RNA modifying enzymes, ATPases, GTPases, kinases and RNA helicases. Altogether, they likely confer speed, accuracy and directionality to the ribosome synthesis process, however, the precise functions for most of them are still largely unknown. This review summarises our current knowledge on eukaryotic RNA helicases involved in ribosome biogenesis, particularly focusing on the most recent advances with respect to the molecular roles of these enzymes and their co-factors in yeast and human cells. This article is part of a Special Issue entitled: The Biology of RNA helicases—Modulation for life.
► We review on yeast and human RNA helicases involved in ribosome biogenesis. ► We discuss on the dynamics of yeast RNA helicases during ribosome synthesis. ► We describe the molecular roles of these enzymes and discuss on their cofactors. ► We describe the role of human RNA helicases involved in ribosome synthesis. ► We discuss on the future challenges for the research on these enzymes. |
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ISSN: | 1874-9399 0006-3002 1876-4320 |
DOI: | 10.1016/j.bbagrm.2013.01.007 |