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Xrn1 biochemically associates with eisosome proteins after the post diauxic shift in yeast

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Courtin, Baptiste | Namane, Abdelkader | Gomard, Maite | Meyer, Laura | Jacquier, Alain | Fromont-Racine, Micheline

Edité par CCSD ; CalTech Library -

International audience. mRNA degradation is one of the main steps of gene expression, and a key player is the 5’-3’ exonuclease Xrn1. In Saccharomyces cerevisiae, it was previously shown, by a microscopy approach, that Xrn1 is located to different cellular compartments, depending on physiological state. During exponential growth, Xrn1 is distributed in the cytoplasm, while it co-localizes with eisosomes after the post-diauxic shift (PDS). Here, we biochemically characterize the Xrn1-associated complexes in different cellular states. We demonstrate that, after PDS, Xrn1 but not the decapping nor Lsm1-7/Pat1 complexes associates with eisosomal proteins, strengthening the model that sequestration of Xrn1 in eisosomes preserves mRNAs from degradation during PDS.

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