Ontology highlight
ABSTRACT:
SUBMITTER: Shin D
PROVIDER: S-EPMC6941232 | biostudies-literature | 2020 Jan
REPOSITORIES: biostudies-literature
Shin Donghyuk D Mukherjee Rukmini R Liu Yaobin Y Gonzalez Alexis A Bonn Florian F Liu Yan Y Rogov Vladimir V VV Heinz Marcel M Stolz Alexandra A Hummer Gerhard G Dötsch Volker V Luo Zhao-Qing ZQ Bhogaraju Sagar S Dikic Ivan I
Molecular cell 20191112 1
The family of bacterial SidE enzymes catalyzes non-canonical phosphoribosyl-linked (PR) serine ubiquitination and promotes infectivity of Legionella pneumophila. Here, we describe identification of two bacterial effectors that reverse PR ubiquitination and are thus named deubiquitinases for PR ubiquitination (DUPs; DupA and DupB). Structural analyses revealed that DupA and SidE ubiquitin ligases harbor a highly homologous catalytic phosphodiesterase (PDE) domain. However, unlike SidE ubiquitin l ...[more]