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

Authors :
Pruneda JN
Bastidas RJ
Bertsoulaki E
Swatek KN
Santhanam B
Clague MJ
Valdivia RH
Urbé S
Komander D
Source :
Nature microbiology [Nat Microbiol] 2018 Dec; Vol. 3 (12), pp. 1377-1384. Date of Electronic Publication: 2018 Nov 05.
Publication Year :
2018

Abstract

Pathogenic bacteria are armed with potent effector proteins that subvert host signalling processes during infection <superscript>1</superscript> . The activities of bacterial effectors and their associated roles within the host cell are often poorly understood, particularly for Chlamydia trachomatis <superscript>2</superscript> , 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 of ChlaDUB1 and the related, dedicated DUB ChlaDUB2 to fragmentation of the host Golgi apparatus, a key process in Chlamydia infection for which effectors have remained elusive. Our work illustrates the incredible versatility of bacterial effector proteins, and provides important insights towards understanding Chlamydia pathogenesis.

Details

Language :
English
ISSN :
2058-5276
Volume :
3
Issue :
12
Database :
MEDLINE
Journal :
Nature microbiology
Publication Type :
Academic Journal
Accession number :
30397340
Full Text :
https://doi.org/10.1038/s41564-018-0271-y