N <sup>ε</sup> -Fatty acylation of Rho GTPases by a MARTX toxin effector

Yan Zhou, Chunfeng Huang, Li Yin, Muyang Wan, Xiaofei Wang, Lin Li, Yanhua Liu, Zhao Wang, Panhan Fu, Ni Zhang,

Science · 2017 · 61 citations · 31 references

Concepts

Abstract

Bacterial toxin fatty-acylates lysine residues A toxin produced by the bacterium that causes cholera has a catalytic activity that contributes to its effects on the cytoskeleton of host cells. Zhou et al. determined the protein structure of the Rho guanosine triphosphatase (GTPase)–inactivation domain of the toxin from Vibrio cholerae and found it to be similar to that of a human fatty acyltransferase. Indeed, the toxin peptide could catalyze fatty acylation of lysine residues of Rho-family GTPases, which regulate the actin cytoskeleton. Such covalent modification of lysine residues in mammalian proteins had been noted before, but the enzymes responsible were not known. Science , this issue p. 528

References

31