The N-terminal Region of Yeast Mitoribosomal Mrp7/bL27m Protein Serves to Optimize Translation of Nascent Chains Competent for OXPHOS Complex Assembly

Authors

Jessica M. Anderson, Marquette University
Jodie M. Box, Marquette University
Rosemary A. Stuart, Marquette UniversityFollow

Document Type

Article

Publication Date

6-2023

Publisher

Wiley

Source Publication

FEBS Letter

Source ISSN

1742-464X

Original Item ID

10.1002/1873-3468.14631

Abstract

The extreme N-terminal residues of the mitochondrial ribosomal bL27m proteins reside within the ribosomal peptidyl transferase center (PTC) and are conserved from their bacterial ancestors. Mutation or truncation of the N-terminal region of the yeast Mrp7/bL27m protein did not inhibit protein synthesis but significantly impacted the efficacy of the mitochondrial translational process with respect to yielding proteins competent to assemble into functional oxidative phosphorylation enzymes. The requirement for the N-terminal residues of Mrp7/bL27m to support normal mitotranslation was more apparent under respiratory growth. We demonstrate that the N-terminal region of Mrp7/bL27m impacts the environment of the PTC and speculate the bL27m proteins serve to fine-tune and optimize mitoribosomal activity with respect to the downstream fate of the nascent chain.

Comments

Accepted version. FEBS Letter, Vol. 597, No. 12 (June 2023): 1579-1594. DOI. © 2023 Wiley. Used with permission.

Recommended Citation

Anderson, Jessica M.; Box, Jodie M.; and Stuart, Rosemary A., "The N-terminal Region of Yeast Mitoribosomal Mrp7/bL27m Protein Serves to Optimize Translation of Nascent Chains Competent for OXPHOS Complex Assembly" (2023). Biological Sciences Faculty Research and Publications. 965.
https://epublications.marquette.edu/bio_fac/965