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Molecular Characterization of LubX. AP-MS using Legionella lysate

ABSTRACT: Legionella pneumophila delivers over 300 effector proteins into the host cytosol. One of these effectors, LubX contains 2 U-box domains, and directs the proeosomal degradation of another translocated protein, SidH, however this 'metaeffector' activity is pooly understood. As part of our investigation of the interaction of LubX and SidH, we idenified a LubX mutant that was no longer able to abrogate the toxicity of ectopically expressed SidH in yeast. This dataset belongs to AP-MS experiments conducted to test the ability of these mutants for their ability to bind directly to SidH in Legionella lysate mixtures

INSTRUMENT(S): LTQ

ORGANISM(S): Legionella Pneumophila Subsp. Pneumophila (strain Philadelphia 1 / Atcc 33152 / Dsm 7513)

SUBMITTER: Andrew Quaile

LAB HEAD: Alexei Savchenko

PROVIDER: PXD001525 | Pride | 2020-01-27

REPOSITORIES: Pride

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Molecular Characterization of LubX: Functional Divergence of the U-Box Fold by Legionella pneumophila.

Quaile Andrew T AT Urbanus Malene L ML Stogios Peter J PJ Nocek Boguslaw B Skarina Tatiana T Ensminger Alexander W AW Savchenko Alexei A

Structure (London, England : 1993) 20150702 8

LubX is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. Despite such unique features as the presence of two U-box motifs and its targeting of another effector SidH, the molecular basis of LubX activity remains poorly understood. Here we show that the N terminus of LubX is able to activate an extended number of ubiquitin-conjugating (E2) enzymes including UBE2W, UBEL6, and all tested members of UBE2D and UBE2E families ...[more]

PMID: 26146184

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