A ribosome exit tunnel component is required for robust expression of the Drosophila hox gene, abdominal A
- 1University of Nottingham
Abstract
Ribosomes, the molecular machines responsible for protein synthesis, are fundamental to all cellular life. Although the higher-level architecture of ribosomes is conserved, a small subunit acting as the mRNA decoding site and a large subunit that catalyses peptide bond formation, there are differences in the numbers of components of each of the subunits between the 3 domains of life. Despite their well-established role in translating genetic information into functional proteins, many complexities in ribosome biology and functionality are only just being revealed. Defects in ribosomal components contribute to a class of disorders termed ribosomopathies that come with a range of symptoms and severities. Here we show that a mutation in the Drosophila ribosomal protein RpL39 causes an anterior-posterior embryonic patterning defect through impaired accumulation of the hox protein Abdominal-A (abdA). Deletions uncovering subunits of the Nascent peptide-Associated Complex (NAC) and Ribosome-Associated Complex (RAC) act as genetic enhancers of the RpL39 mutation leading us to speculate that RpL39 forms a relay between the nascent peptide in the exit tunnel and the exterior surface of the ribosome, modulating the interaction with these ribosomally-associated complexes. This work enhances our knowledge of the roles played by individual ribosome components and feeds into our understanding of the mechanisms of ribosome quality control.
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BibTeX
@misc{mcfarland2026ribosome,
title = {{A ribosome exit tunnel component is required for robust expression of the Drosophila hox gene, abdominal A}},
author = {M. R. McFarland and R. Tripathy and J. K. Bergman and M. L. Wood and A. D. Renault},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.23.761343},
url = {https://www.biorxiv.org/content/10.64898/2026.10.23.761343v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - A ribosome exit tunnel component is required for robust expression of the Drosophila hox gene, abdominal A
AU - M. R. McFarland
AU - R. Tripathy
AU - J. K. Bergman
AU - M. L. Wood
AU - A. D. Renault
PY - 2026
DA - 2026/10/23
PB - bioRxiv
DO - 10.64898/2026.10.23.761343
UR - https://www.biorxiv.org/content/10.64898/2026.10.23.761343v1
AB - Ribosomes, the molecular machines responsible for protein synthesis, are fundamental to all cellular life. Although the higher-level architecture of ribosomes is conserved, a small subunit acting as the mRNA decoding site and a large subunit that catalyses peptide bond formation, there are differences in the numbers of components of each of the subunits between the 3 domains of life. Despite their well-established role in translating genetic information into functional proteins, many complexities in ribosome biology and functionality are only just being revealed. Defects in ribosomal components contribute to a class of disorders termed ribosomopathies that come with a range of symptoms and severities. Here we show that a mutation in the Drosophila ribosomal protein RpL39 causes an anterior-posterior embryonic patterning defect through impaired accumulation of the hox protein Abdominal-A (abdA). Deletions uncovering subunits of the Nascent peptide-Associated Complex (NAC) and Ribosome-Associated Complex (RAC) act as genetic enhancers of the RpL39 mutation leading us to speculate that RpL39 forms a relay between the nascent peptide in the exit tunnel and the exterior surface of the ribosome, modulating the interaction with these ribosomally-associated complexes. This work enhances our knowledge of the roles played by individual ribosome components and feeds into our understanding of the mechanisms of ribosome quality control.
ER -