RT Journal Article SR Electronic T1 The TUDOR domain of SMN is an H3K79me1 histone mark reader JF Life Science Alliance JO Life Sci. Alliance FD Life Science Alliance LLC SP e202201752 DO 10.26508/lsa.202201752 VO 6 IS 6 A1 Binda, Olivier A1 Kimenyi Ishimwe, Aimé Boris A1 Galloy, Maxime A1 Jacquet, Karine A1 Corpet, Armelle A1 Fradet-Turcotte, Amélie A1 Côté, Jocelyn A1 Lomonte, Patrick YR 2023 UL http://www.life-science-alliance.org/content/6/6/e202201752.abstract AB Spinal muscular atrophy is the leading genetic cause of infant mortality and results from depleted levels of functional survival of motor neuron (SMN) protein by either deletion or mutation of the SMN1 gene. SMN is characterized by a central TUDOR domain, which mediates the association of SMN with arginine methylated (Rme) partners, such as coilin, fibrillarin, and RNA pol II (RNA polymerase II). Herein, we biochemically demonstrate that SMN also associates with histone H3 monomethylated on lysine 79 (H3K79me1), defining SMN as not only the first protein known to associate with the H3K79me1 histone modification but also the first histone mark reader to recognize both methylated arginine and lysine residues. Mutational analyzes provide evidence that SMNTUDOR associates with H3 via an aromatic cage. Importantly, most SMNTUDOR mutants found in spinal muscular atrophy patients fail to associate with H3K79me1.