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© Carmen Buchrieser, Marie-Christine Prevost
Legionella pneumophila et son flagelle, bactérie responsable de pneumopathie aigue grave. Bactérie de l'environnement , l'émergence récente de cette maladie s'explique par son affinité pour les systèmes modernes d'alimentation en eau comme les tours de refroidissement. Image colorisée.
Publication : Nature communications

A Ca-regulated deAMPylation switch in human and bacterial FIC proteins

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 08 Mar 2019

Veyron S, Oliva G, Rolando M, Buchrieser C, Peyroche G, Cherfils J

Link to Pubmed [PMID] – 30850593

Nat Commun 2019 Mar;10(1):1142

FIC proteins regulate molecular processes from bacteria to humans by catalyzing post-translational modifications (PTM), the most frequent being the addition of AMP or AMPylation. In many AMPylating FIC proteins, a structurally conserved glutamate represses AMPylation and, in mammalian FICD, also supports deAMPylation of BiP/GRP78, a key chaperone of the unfolded protein response. Currently, a direct signal regulating these FIC proteins has not been identified. Here, we use X-ray crystallography and in vitro PTM assays to address this question. We discover that Enterococcus faecalis FIC (EfFIC) catalyzes both AMPylation and deAMPylation and that the glutamate implements a multi-position metal switch whereby Mg and Ca control AMPylation and deAMPylation differentially without a conformational change. Remarkably, Ca concentration also tunes deAMPylation of BiP by human FICD. Our results suggest that the conserved glutamate is a signature of AMPylation/deAMPylation FIC bifunctionality and identify metal ions as diffusible signals that regulate such FIC proteins directly.

https://www.ncbi.nlm.nih.gov/pubmed/30850593