Journal
CELL HOST & MICROBE
Volume 21, Issue 2, Pages 169-181Publisher
CELL PRESS
DOI: 10.1016/j.chom.2016.12.007
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Funding
- NIH [T32GM007310]
- NSF [DGE-1325256]
- German Academic Exchange Service (DAAD)
- American Heart Association [14POST20480308]
- NIAID [R01AI113211]
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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 multi-step biochemical pathway to control ubiquitination and tubular ER function independently of the host ubiquitin machinery.
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