Legionella pneumophila subversion of host vesicular transport by SidC effector proteins.
Tethering proteins play a key role in vesicular transport, ensuring that cargo arrives at a specific destination. The bacterial effector protein SidC and its paralog SdcA have been described as tethering factors encoded by the intracellular pathogen Legionella pneumophila. Here, we demonstrate that SidC proteins are important for early events unique to maturation of vacuoles containing Legionella and discover monoubiquitination of Rab1 as a new SidC-dependent activity. The crystal structure of the SidC N-terminus revealed a novel fold that is important for function and could be involved in Legionella adaptations to evolutionarily divergent host cells it encounters in natural environments.
Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.
Florian A
FA
Horenkamp
Shaeri
S
Mukherjee
Eric
E
Alix
Curtis M
CM
Schauder
Andree M
AM
Hubber
Craig R
CR
Roy
Karin M
KM
Reinisch
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport / Q000502:physiology*; D018360:Crystallography, X-Ray; D016952:Legionella pneumophila / Q000378:metabolism*; D008969:Molecular Sequence Data; D054875:Ubiquitination / Q000502:physiology; D014617:Vacuoles / Q000378:metabolism*; D020761:rab1 GTP-Binding Proteins / Q000378:metabolism
D001426:Bacterial Proteins; C534216:SidC protein, Legionella pneumophila; D020761:rab1 GTP-Binding Proteins
Rab1 modification; Tethering