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Published Erratum
. 2015 Aug;83(8):3338.
doi: 10.1128/IAI.00587-15.

Correction for Hervet et al., protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila

Eva Hervet  1 , Xavier Charpentier  2 , Anne Vianney  1 , Jean-Claude Lazzaroni  1 , Christophe Gilbert  1 , Danièle Atlan  1 , Patricia Doublet  1
Affiliations
Published Erratum

Correction for Hervet et al., protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila

Eva Hervet et al. Infect Immun. 2015 Aug.
No abstract available

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Figures

FIG 2
FIG 2
Biochemical activities of recombinant LegK proteins. (A) SDS-PAGE analysis of purified GSTLegK1, GST-LegK2, GST-LegK3, 6His-LegK4, and 6His-LegK5 after staining with Coomassie blue. Molecular mass standards are indicated on the left. (B) Effects of cations on autokinase activities of GST-LegK2, GST-LegK3, 6His-LegK4, and 6His-LegK5. Purified LegK proteins (stained with Coomassie blue) were submitted to in vitro autophosphorylation assays in the presence of [γ-32P]ATP, myelin basic protein (MBP), and Mg2+ or Mn2+. Phosphoproteins were separated by SDS-PAGE and then revealed by autoradiography. Insets from Fig. 2C focusing on kinase autophosphorylation activities are shown. (C) Protein kinase activities of LegK proteins. The eukaryotic substrate MBP was incubated with each LegK recombinant protein in the presence of [γ-32P]ATP and the appropriate cation. Phosphoproteins were revealed by autoradiography after SDS-PAGE separation.
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