Public Library of Science, PLoS Genetics, 5(12), p. e1006023, 2016
DOI: 10.1371/journal.pgen.1006023
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Protein AMPylation by Fic domain-containing proteins (Fic proteins) is an ancient and conserved post-translational modification of mostly unexplored significance. Here we characterize the Caenorhabditis elegans Fic protein FIC-1 in vitro and in vivo. FIC-1 is an AMPylase that localizes to the nuclear surface and modifies core histones H2 and H3 as well as heat shock protein 70 family members and translation elongation factors. The three-dimensional structure of FIC-1 is similar to that of its human ortholog, HYPE, with 38% sequence identity. We identify a link between FIC-1-mediated AMPylation and susceptibility to the pathogen Pseudomonas aeruginosa, establishing a connection between AMPylation and innate immunity in C. elegans. ; National Institutes of Health (U.S.) (P41 GM103403) ; Swiss National Science Foundation (Advanced Postdoc Mobility Fellowship) ; National Institutes of Health (U.S.) (NIH Pioneer Award (DP01))