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Duplicated ribosomal protein paralogs promote alternative translation and drug resistance

Author

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  • Mustafa Malik Ghulam

    (Université de Sherbrooke)

  • Mathieu Catala

    (Université de Sherbrooke)

  • Gaspard Reulet

    (Université de Sherbrooke)

  • Michelle S. Scott

    (Université de Sherbrooke)

  • Sherif Abou Elela

    (Université de Sherbrooke)

Abstract

Ribosomes are often seen as monolithic machines produced from uniformly regulated genes. However, in yeast most ribosomal proteins come from duplicated genes. Here, we demonstrate that gene duplication may serve as a stress-adaptation mechanism modulating the global proteome through the differential expression of ribosomal protein paralogs. Our data indicate that the yeast paralog pair of the ribosomal protein L7/uL30 produces two differentially acetylated proteins. Under normal conditions most ribosomes incorporate the hypo-acetylated major form favoring the translation of genes with short open reading frames. Exposure to drugs, on the other hand, increases the production of ribosomes carrying the hyper-acetylated minor paralog that increases translation of long open reading frames. Many of these paralog-dependent genes encode cell wall proteins that could promote tolerance to drugs as their translation increases after exposure to drugs. Together our data suggest a mechanism of translation control that functions through a differential use of near-identical ribosomal protein isoforms.

Suggested Citation

  • Mustafa Malik Ghulam & Mathieu Catala & Gaspard Reulet & Michelle S. Scott & Sherif Abou Elela, 2022. "Duplicated ribosomal protein paralogs promote alternative translation and drug resistance," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32717-y
    DOI: 10.1038/s41467-022-32717-y
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    References listed on IDEAS

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    1. Rikke B. LangkjAEr & Paul F. Cliften & Mark Johnston & Jure Piškur, 2003. "Yeast genome duplication was followed by asynchronous differentiation of duplicated genes," Nature, Nature, vol. 421(6925), pages 848-852, February.
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