The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones.

Publication Type:

Journal Article

Authors:

Truttmann, Matthias C; Cruz, Victor E; Guo, Xuanzong; Engert, Christoph; Schwartz, Thomas U; Ploegh, Hidde L

Source:

PLoS Genet, Volume 12, Issue 5, p.e1006023 (2016)

Keywords:

Animals, Caenorhabditis elegans, Caenorhabditis elegans Proteins, Carrier Proteins, Crystallography, X-Ray, DNA-Binding Proteins, Heat-Shock Response, Histones, HSP70 Heat-Shock Proteins, Humans, Immunity, Innate, Membrane Proteins, Nucleotidyltransferases, Peptide Chain Elongation, Translational, Protein Conformation, Pseudomonas aeruginosa, Recombinant Proteins

Abstract:

<p>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.</p>

PDB: 
5JJ6, 5JJ7
Detector: 
PILATUS
Beamline: 
24-ID-C