Pathogen-defending deubiquitinase possesses distinct specificity towards K6-polyubiquitination

Zhengrui Zhang; Chittaranjan Das

doi:10.1016/j.tim.2023.02.013

Pathogen-defending deubiquitinase possesses distinct specificity towards K6-polyubiquitination

Trends Microbiol. 2023 May;31(5):423-425. doi: 10.1016/j.tim.2023.02.013. Epub 2023 Mar 6.

Authors

Zhengrui Zhang¹, Chittaranjan Das²

Affiliations

¹ Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA.
² Department of Chemistry, Purdue University, West Lafayette, Indiana 47907, USA. Electronic address: cdas@purdue.edu.

PMID: 36890008
DOI: 10.1016/j.tim.2023.02.013

Abstract

The bacterial pathogen Legionella pneumophila encodes numerous effectors to manipulate host ubiquitin signaling. Recently, Warren et al. revealed the structural basis of K6-polyubiquitination recognition by Legionella deubiquitinase LotA, while validating its potential as an enzymatic tool to study linkage-specific ubiquitination. During Legionella infection, LotA counteracts valosin-containing protein (VCP) recruitment to the Legionella-containing vacuole.

Keywords: Legionella; bacterial effector; deubiquitinase; substrate-assisted catalysis; ubiquitination.

MeSH terms

Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Deubiquitinating Enzymes / chemistry
Deubiquitinating Enzymes / metabolism
Humans
Legionella pneumophila* / genetics
Legionnaires' Disease* / microbiology
Ubiquitin / metabolism
Ubiquitination

Substances

Ubiquitin
Deubiquitinating Enzymes
Bacterial Proteins