A Chlamydia effector combining deubiquitination and acetylation activities induces Golgi fragmentation.

ABSTRACT: Pathogenic bacteria are armed with potent effector proteins that subvert host signalling processes during infection¹. The activities of bacterial effectors and their associated roles within the host cell are often poorly understood, particularly for Chlamydia trachomatis², a World Health Organization designated neglected disease pathogen. We identify and explain remarkable dual Lys63-deubiquitinase (DUB) and Lys-acetyltransferase activities in the Chlamydia effector ChlaDUB1. Crystal structures capturing intermediate stages of each reaction reveal how the same catalytic centre of ChlaDUB1 can facilitate such distinct processes, and enable the generation of mutations that uncouple the two activities. Targeted Chlamydia mutant strains allow us to link the DUB activity o

SUBMITTER: Pruneda JN 

PROVIDER: S-EPMC6319605 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature