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Abstract
Specific ribosomal protein (RP) paralogs affect cellular processes, such as actin organization, mRNA localization, and others. However, whether paralog specificity directly influences mRNA translation related to these processes remains obscure. Here, we employed a non-biased proteomic approach to isolate translating polysomes from respiration-incompetent RP yeast mutants and mapped their translatome. Our findings demonstrate that specific RP paralogs favor translation of a distinct subset of mRNAs encoding mitochondrial proteins, which consequently regulates respiration. Thus, specialized ribosomes, which vary in the composition of RP paralogs, define an additional level of translational regulation essential for cellular function and environmental responsiveness.
