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 Microbejournal_title
Cell host & microbeauthors
Kotewicz KM,Ramabhadran V,Sjoblom N,Vogel JP,Haenssler E,Zhang M,Behringer J,Scheck RA,Isberg RRdoi
10.1016/j.chom.2016.12.007subject
Has Abstractpub_date
2017-02-08 00:00:00pages
169-181issue
2eissn
1931-3128issn
1934-6069pii
S1931-3128(16)30518-2journal_volume
21pub_type
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