Display Settings:

Format

Send to:

Choose Destination
EMBO Rep. 2011 Sep 1;12(9):950-5. doi: 10.1038/embor.2011.133.

Truncation of the Mrp20 protein reveals new ribosome-assembly subcomplex in mitochondria.

Author information

  • 1Department of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53233, USA.

Abstract

Mitochondrial ribosomal protein 20 (Mrp20) is a component of the yeast mitochondrial large (54S) ribosomal subunit and is homologous to the bacterial L23 protein, located at the ribosomal tunnel exit site. The carboxy-terminal mitochondrial-specific domain of Mrp20 was found to have a crucial role in the assembly of the ribosomes. A new, membrane-bound, ribosomal-assembly subcomplex composed of known tunnel-exit-site proteins, an uncharacterized ribosomal protein, MrpL25, and the mitochondrial peroxiredoxin (Prx), Prx1, accumulates in an mrp20ΔC yeast mutant. Finally, data supporting the idea that the inner mitochondrial membrane acts as a platform for the ribosome assembly process are discussed.

PMID:
21779004
[PubMed - indexed for MEDLINE]
PMCID:
PMC3166459
Free PMC Article

Images from this publication.See all images (4)Free text

Figure 1
Figure 2
Figure 3
Figure 4
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk