The Involvement of IYNR069C/I in Protein Synthesis in the Baker’s Yeast, ISaccharomyces cerevisiae/I

Preserving the integrity of protein biosynthesis involves maintaining a delicate equilibrium between translation accuracy and speed. In the current study we observed that deletion of YNR069C resulted in a notable increase in readthrough at premature stop codons, suggesting its participation in the process of translation. Moreover, the absence of YNR069C led to an acceleration of the translation rate. These observations indicate that YNR069C may play a role in translation integrity. Our comprehensive genetic interaction analysis reinforces this idea, establishing a clear link between YNR069C and the regulation of translation. These findings contribute to our understanding of how cells may control gene expression. Maintaining translation fidelity is a critical step within the process of gene expression. It requires the involvement of numerous regulatory elements to ensure the synthesis of functional proteins. The efficient termination of protein synthesis can play a crucial role in preserving this fidelity. Here, we report on investigating a protein of unknown function, YNR069C (also known as BSC5), for its activity in the process of translation. We observed a significant increase in the bypass of premature stop codons upon the deletion of YNR069C. Interestingly, the genomic arrangement of this ORF suggests a compatible mode of expression reliant on translational readthrough, incorporating the neighboring open reading frame. We also showed that the deletion of YNR069C results in an increase in the rate of translation. Based on our results, we propose that YNR069C may play a role in translation fidelity, impacting the overall quantity and quality of translation. Our genetic interaction analysis supports our hypothesis, associating the role of YNR069C to the regulation of protein synthesis.