Membrane Localization Contributes to the In Vivo ADP-Ribosylation of Ras by Pseudomonas aeruginosa ExoS

AUTOR(ES)

Riese, Matthew J.

FONTE

American Society for Microbiology

RESUMO

Type III-delivered exoenzyme S (ExoS) preferentially ADP-ribosylated membrane-associated His6HRas, relative to its cytosolic derivative His6HRasΔCAAX. This indicates that the subcellular protein distribution contributes to in vivo ADP-ribosylation by ExoS.

Documentos Relacionados

• ADP-Ribosylation of Rab5 by ExoS of Pseudomonas aeruginosa Affects Endocytosis
• ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S.
• In Vivo Rho GTPase-Activating Protein Activity of Pseudomonas aeruginosa Cytotoxin ExoS
• ADP-ribosylation in inner membrane of rat liver mitochondria.
• Regulation of ExoS Production and Secretion by Pseudomonas aeruginosa in Response to Tissue Culture Conditions