Truncation of the Mrp20 Protein Reveals New Ribosome‐assembly Subcomplex in Mitochondria

Authors

Jasvinder Kaur, Marquette University
Rosemary A. Stuart, Marquette UniversityFollow

Document Type

Article

Language

eng

Format of Original

6 p.

Publication Date

9-2011

Publisher

Wiley

Source Publication

EMBO Reports

Source ISSN

1469-221X

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.

Comments

Accepted version. EMBO Reports, Vol. 12, No. 9 (September 2011): 950-955. DOI. © 2011 Wiley. Used with permission.

Recommended Citation

Kaur, Jasvinder and Stuart, Rosemary A., "Truncation of the Mrp20 Protein Reveals New Ribosome‐assembly Subcomplex in Mitochondria" (2011). Biological Sciences Faculty Research and Publications. 318.
https://epublications.marquette.edu/bio_fac/318