Regulation of the small GTPase Rab1 function by a bacterial glucosyltransferase.

ABSTRACT: Posttranslational modification of key host proteins by virulence factors is an important theme in bacterial pathogenesis. A remarkable example is the reversible modifications of the small GTPase Rab1 by multiple effectors of the bacterial pathogen Legionella pneumophila. Previous studies have shown that the effector SetA, dependent on a functional glucosyltransferase domain, interferes with host secretory pathways. However, the enzymatic substrate(s) of SetA in host cells remains unknown. Here, by using cross-linking mass spectrometry we uncovered Rab1 as the target of SetA during L. pneumophila infection. Biochemical studies establish that SetA covalently attaches a glucose moiety to Thr₇₅ within the switch II region of Rab1, inhibiting its intrinsic GTPase activi

SUBMITTER: Wang Z 

PROVIDER: S-EPMC6175885 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature