Abstract
Proteins in a cell are universally synthesized by ribosomes. Mitochondria contain their own ribosomes, which specialize in the synthesis of a handful of proteins required for oxidative phosphorylation. The pathway of mitoribosomal biogenesis and factors involved are poorly characterized. An example is the DEAD box proteins, widely known to participate in the biogenesis of bacterial and cytoplasmic eukaryotic ribosomes as either RNA helicases or RNA chaperones, whose mitochondrial counterparts remain completely unknown. Here, we have identified the Saccharomyces cerevisiae mitochondrial DEAD box protein Mrh4 as essential for large mitoribosome subunit biogenesis. Mrh4 interacts with the 21S rRNA, mitoribosome subassemblies, and fully assembled mitoribosomes. In the absence of Mrh4, the 21S rRNA is matured and forms part of a large on-pathway assembly intermediate missing proteins Mrpl16 and Mrpl39. We conclude that Mrh4 plays an essential role during the late stages of mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions.
| Original language | English |
|---|---|
| Pages (from-to) | 712-725 |
| Number of pages | 14 |
| Journal | Cell Metabolism |
| Volume | 18 |
| Issue number | 5 |
| DOIs | |
| State | Published - Nov 5 2013 |
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ASJC Scopus subject areas
- Cell Biology
- Molecular Biology
- Physiology
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The DEAD box protein Mrh4 functions in the assembly of the mitochondrial large ribosomal subunit. / De Silva, Dasmanthie; Fontanesi, Flavia; Barrientos, Antonio.
In: Cell Metabolism, Vol. 18, No. 5, 05.11.2013, p. 712-725.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The DEAD box protein Mrh4 functions in the assembly of the mitochondrial large ribosomal subunit
AU - De Silva, Dasmanthie
AU - Fontanesi, Flavia
AU - Barrientos, Antonio
PY - 2013/11/5
Y1 - 2013/11/5
N2 - Proteins in a cell are universally synthesized by ribosomes. Mitochondria contain their own ribosomes, which specialize in the synthesis of a handful of proteins required for oxidative phosphorylation. The pathway of mitoribosomal biogenesis and factors involved are poorly characterized. An example is the DEAD box proteins, widely known to participate in the biogenesis of bacterial and cytoplasmic eukaryotic ribosomes as either RNA helicases or RNA chaperones, whose mitochondrial counterparts remain completely unknown. Here, we have identified the Saccharomyces cerevisiae mitochondrial DEAD box protein Mrh4 as essential for large mitoribosome subunit biogenesis. Mrh4 interacts with the 21S rRNA, mitoribosome subassemblies, and fully assembled mitoribosomes. In the absence of Mrh4, the 21S rRNA is matured and forms part of a large on-pathway assembly intermediate missing proteins Mrpl16 and Mrpl39. We conclude that Mrh4 plays an essential role during the late stages of mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions.
AB - Proteins in a cell are universally synthesized by ribosomes. Mitochondria contain their own ribosomes, which specialize in the synthesis of a handful of proteins required for oxidative phosphorylation. The pathway of mitoribosomal biogenesis and factors involved are poorly characterized. An example is the DEAD box proteins, widely known to participate in the biogenesis of bacterial and cytoplasmic eukaryotic ribosomes as either RNA helicases or RNA chaperones, whose mitochondrial counterparts remain completely unknown. Here, we have identified the Saccharomyces cerevisiae mitochondrial DEAD box protein Mrh4 as essential for large mitoribosome subunit biogenesis. Mrh4 interacts with the 21S rRNA, mitoribosome subassemblies, and fully assembled mitoribosomes. In the absence of Mrh4, the 21S rRNA is matured and forms part of a large on-pathway assembly intermediate missing proteins Mrpl16 and Mrpl39. We conclude that Mrh4 plays an essential role during the late stages of mitoribosome assembly by promoting remodeling of the 21S rRNA-protein interactions.
UR - http://www.scopus.com/inward/record.url?scp=84887478008&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84887478008&partnerID=8YFLogxK
U2 - 10.1016/j.cmet.2013.10.007
DO - 10.1016/j.cmet.2013.10.007
M3 - Article
C2 - 24206665
AN - SCOPUS:84887478008
VL - 18
SP - 712
EP - 725
JO - Cell Metabolism
JF - Cell Metabolism
SN - 1550-4131
IS - 5
ER -