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Article
Subject Categories: RNA | Cellular Metabolism
The EMBO Journal (2005) 24, 580–588, doi:10.1038/sj.emboj.7600540
Published online 20 January 2005
Functional link between ribosome formation and biogenesis of iron–sulfur proteins
Alexander Yarunin1, Vikram Govind Panse1, Elisabeth Petfalski2, Christophe Dez2, David Tollervey2 and Ed Hurt1
1 Biochemie-Zentrum der Universität Heidelberg (BZH), Heidelberg, Germany
2 Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK

To whom correspondence should be addressed
Ed Hurt, Biochemie-Zentrum der Universität Heidelberg (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. Tel.: +49 6221 544173; Fax: +49 6221 544369; E-mail: cg5@ix.urz.uni-heidelberg.de

Received 29 April 2004; Accepted 8 December 2004; Published online 20 January 2005.
Abstract
In genetic screens for ribosomal export mutants, we identified CFD1, NBP35 and NAR1 as factors involved in ribosome biogenesis. Notably, these components were recently reported to function in extramitochondrial iron–sulfur (Fe–S) cluster biosynthesis. In particular, Nar1 was implicated to generate the Fe–S clusters within Rli1, a potential substrate protein of unknown function. We tested whether the Fe–S protein Rli1 functions in ribosome formation. We report that rli1 mutants are impaired in pre-rRNA processing and defective in the export of both ribosomal subunits. In addition, Rli1p is associated with both pre-40S particles and mature 40S subunits, and with the eIF3 translation initiation factor complex. Our data reveal an unexpected link between ribosome biogenesis and the biosynthetic pathway of cytoplasmic Fe–S proteins.
Keywords: eIF3, iron–sulfur cluster, Nar1, ribosome export, Rli1
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