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Ded1p is an essential ATP‐dependent RNA helicase that promotes nuclear export (1), stress granule accumulation, and translation initiation through association with translation factors, such as eIF4A and eIF4G (2, 3). Ded1 is methylated by Hmt1 at five arginine residues in its intrinsically disordered domains (4, 5). Methylation strengthens the interaction between Ded1 and Npl3, a protein involved in nuclear export (4), but it is unclear if methylation impacts translation.

We find that Ded1 methylation is stably detected under a range of growth conditions and stresses, suggesting that this modification is common within in vivo stores of Ded1. To test the function of Ded1 methylation in vivo, we mutated four of the five methylated arginines to either alanine (ded1‐quadA) or lysine (ded1‐quadK). We are currently testing the effects of a recently discovered fifth methylation site (5). The ded1‐quadA and quadK mutants show …