A Single Legionella Effector Catalyzes a Multistep Ubiquitination Pathway to Rearrange Tubular Endoplasmic Reticulum for Replication.

Abstract:

:Intracellular pathogens manipulate host organelles to support replication within cells. For Legionella pneumophila, the bacterium translocates proteins that establish an endoplasmic reticulum (ER)-associated replication compartment. We show here that the bacterial Sde proteins target host reticulon 4 (Rtn4) to control tubular ER dynamics, resulting in tubule rearrangements as well as alterations in Rtn4 associated with the replication compartment. These rearrangements are triggered via Sde-promoted ubiquitin transfer to Rtn4, occurring almost immediately after bacterial uptake. Ubiquitin transfer requires two sequential enzymatic activities from a single Sde polypeptide: an ADP-ribosyltransferase and a nucleotidase/phosphohydrolase. The ADP-ribosylated moiety of ubiquitin is a substrate for the nucleotidase/phosphohydrolase, resulting in either transfer of ubiquitin to Rtn4 or phosphoribosylation of ubiquitin in the absence of a ubiquitination target. Therefore, a single bacterial protein drives a multistep biochemical pathway to control ubiquitination and tubular ER function independently of the host ubiquitin machinery.

journal_name

Cell Host Microbe

journal_title

Cell host & microbe

authors

Kotewicz KM,Ramabhadran V,Sjoblom N,Vogel JP,Haenssler E,Zhang M,Behringer J,Scheck RA,Isberg RR

doi

10.1016/j.chom.2016.12.007

subject

Has Abstract

pub_date

2017-02-08 00:00:00

pages

169-181

issue

2

eissn

1931-3128

issn

1934-6069

pii

S1931-3128(16)30518-2

journal_volume

21

pub_type

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