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Biogenesis of cytosolic ribosomes requires the essential iron–sulphur protein Rli1p and mitochondria
Author(s) -
Kispal Gyula,
Sipos Katalin,
Lange Heike,
Fekete Zsuzsanna,
Bedekovics Tibor,
Janáky Tamás,
Bassler Jochen,
Aguilar Netz Daili J,
Balk Janneke,
Rotte Carmen,
Lill Roland
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600541
Subject(s) - ribosome biogenesis , biogenesis , ribosome , mitochondrion , microbiology and biotechnology , mitochondrial ribosome , ribosomal protein , cytosol , biology , biochemistry , translation (biology) , organelle biogenesis , chemistry , rna , messenger rna , gene , enzyme
Mitochondria perform a central function in the biogenesis of cellular iron–sulphur (Fe/S) proteins. It is unknown to date why this biosynthetic pathway is indispensable for life, the more so as no essential mitochondrial Fe/S proteins are known. Here, we show that the soluble ATP‐binding cassette (ABC) protein Rli1p carries N‐terminal Fe/S clusters that require the mitochondrial and cytosolic Fe/S protein biogenesis machineries for assembly. Mutations in critical cysteine residues of Rli1p abolish association with Fe/S clusters and lead to loss of cell viability. Hence, the essential character of Fe/S clusters in Rli1p explains the indispensable character of mitochondria in eukaryotes. We further report that Rli1p is associated with ribosomes and with Hcr1p, a protein involved in rRNA processing and translation initiation. Depletion of Rli1p causes a nuclear export defect of the small and large ribosomal subunits and subsequently a translational arrest. Thus, ribosome biogenesis and function are intimately linked to the crucial role of mitochondria in the maturation of the essential Fe/S protein Rli1p.