The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones
Name
Truttmann-2016-The Caenorhabditis e.pdf
Size
6.26 MB
Format
Adobe PDF
Checksum (MD5)
07be92682b59654d0ea19fc5e7d299f4
Author(s)
Truttmann, Matthias
Cruz, Victor Emmanuel
Guo, Xuanzong
Engert, Christoph
Schwartz, Thomas
Ploegh, Hidde
Date Issued
May 2016
Journal
PLOS Genetics
Publisher
Public Library of Science
Citation
Truttmann, Matthias C., Victor E. Cruz, Xuanzong Guo, Christoph Engert, Thomas U. Schwartz, and Hidde L. Ploegh. “The Caenorhabditis Elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones.” Edited by Man-Wah Tan. PLOS Genetics 12, no. 5 (May 3, 2016): e1006023.
Version
Final published version
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Computational and Systems Biology Program
Massachusetts Institute of Technology. Department of Biology
Whitehead Institute for Biomedical Research
Terms of Use
Creative Commons Attribution 4.0 International License
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1371/journal.pgen.1006023
