1. N ε -Fatty acylation of Rho GTPases by a MARTX toxin effector
- Author
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Yongqun Zhu, Chunfeng Huang, Yanhua Liu, Zhao Wang, Ni Zhang, Yan Zhou, Xiaoyun Liu, She Chen, Li Yin, Muyang Wan, Xiaofei Wang, Lin Li, Feng Shao, and Panhan Fu
- Subjects
0301 basic medicine ,Multidisciplinary ,030102 biochemistry & molecular biology ,Effector ,Protein domain ,Guanosine ,GTPase ,Biology ,Actin cytoskeleton ,Cell biology ,03 medical and health sciences ,chemistry.chemical_compound ,030104 developmental biology ,Biochemistry ,chemistry ,Acyltransferase ,Fatty acylation ,Signal transduction - 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
- Published
- 2017
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