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Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri by Anne-Laure Page; Micheline Fromont-Racine; Philippe Sansonetti; Pierre Legrain; Claude Parsot is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri about?

The type III secretion (TTS) system of Gram‐negative pathogenic bacteria is composed of proteins that assemble into the TTS machinery, proteins that are secreted by this machinery and specific chaperones that are required for storage and sometimes secretion of these proteins. Many sequential protein interactions are involved in the TTS pathway to deliver effector proteins to host cells. We used the yeast two‐hybrid system to investigate the interaction partners of the __Shigella flexneri__ effectors and chaperones. Libraries of preys containing random fusions with fragments of the TTS proteins were screened using effectors and chaperones as baits. Interactions between the effectors IpaB and IpaC and their chaperone IpgC were detected by this method, and interaction domains were identified. Using a His‐tagged IpgC protein to co‐purify truncated IpaB and IpaC proteins, we showed that the chaperone‐binding domain was unique and located in the N‐terminus of these proteins. This domain was not required for the secretion of recombinant proteins but was involved in the stability of IpaC and instability of IpaB. Homotypic interactions were identified with the baits IpaA, IpaB and IpaC. Int

Who reads Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri?

Author

Anne-Laure Page; Micheline Fromont-Racine; Philippe Sansonetti; Pierre Legrain; Claude Parsot

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0950-382X)

Published

2001

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)