Methods for Noncanonical Ubiquitination and Deubiquitination Catalyzed by Legionella pneumophila Effector Proteins.

Methods for Noncanonical Ubiquitination and Deubiquitination Catalyzed by Legionella pneumophila Effector Proteins. Methods Mol Biol. 2019;1921:267-276 Authors: Qiu J, Luo ZQ Abstract Protein ubiquitination is one of the most prevalent posttranslational modifications; it regulates a wide range of critical cellular processes in eukaryotes. This modification occurs by covalent attachment of the ubiquitin molecule to other proteins via an isopeptide bond in reactions typically catalyzed by sequential actions of three enzymes, including ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). Ubiquitination is a reversible process catalyzed by a group of proteins known as deubiquitinase (DUB), which specifically cleaves the isopeptide bond between ubiquitin and modified proteins. Recently, a novel form of ubiquitination catalyzed by the SidE family of effectors from the bacterial pathogen Legionella pneumophila was reported. These proteins ubiquitinate structurally diverse host proteins such as reticulons and ER-associated Rab small GTPases by a two-step mechanism that uses NAD as the energy source for ubiquitin activation prior to being transferred to serine residues in target proteins. This process bypasses the need for E1 and E2 enzymes. Intriguingly, ubiquitination induced by SidEs is regulated by SidJ, another L. pneumophila effector protein which reverses the modification by functioning as an ...
Source: Mol Biol Cell - Category: Molecular Biology Authors: Tags: Methods Mol Biol Source Type: research