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Updated: Aug 15, 2026

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions
Published on: October 13, 2015
Study of mycoloyl transferase transport across the cell envelope of Corynebacterium glutamicum
D T Nguyen1, C Houssin, N Bayan
1Laboratoire des Biomembranes, Bât. 430, CNRS UMR 8619, Université de Paris XI, 15 rue Georges Clémenceau, 91405 Cedex, Orsay, France
Abstract:
PS1 is a major exported protein of Corynebacterium glutamicum homologous to mycobacterial antigen 85. It is largely associated with the mycolic acid-containing cell wall and acts as a mycoloyl transferase. The transport of PS1 to the cell wall is slow and occurs through two energetically distinct steps: the first one, which includes processing by signal peptidase, is rapid and inhibited by sodium azide or carbonyl cyanide m-chlorophenylhydrazone. This step is probably associated with translocation across the cytoplasmic membrane. The kinetics of the second step depend on the size of the polypeptide chain to be transported but neither ATP nor proton motive force is required. This step may correspond to the diffusion of PS1 across the cell wall to its final location.
Insights
The study reveals Corynebacterium glutamicum
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- PS1 is a major exported protein in Corynebacterium glutamicum, homologous to mycobacterial antigen 85.
- PS1 is associated with the mycolic acid-containing cell wall and functions as a mycoloyl transferase.
Purpose of the Study:
- To investigate the transport mechanism of PS1 protein to the cell wall in Corynebacterium glutamicum.
- To elucidate the distinct energetic requirements and kinetics of PS1 transport steps.
Main Methods:
- Analysis of protein transport kinetics.
- Inhibition studies using sodium azide and carbonyl cyanide m-chlorophenylhydrazone.
- Investigation of ATP and proton motive force dependency.
Main Results:
- PS1 transport occurs in two energetically distinct steps.
- The first rapid step involves signal peptidase processing and is inhibited by azide or CCCP, suggesting cytoplasmic membrane translocation.
- The second step's kinetics depend on polypeptide size and do not require ATP or proton motive force, indicating diffusion across the cell wall.
Conclusions:
- The transport of PS1 protein to the cell wall is a complex, multi-step process.
- The findings provide insights into the secretion pathway of cell wall-associated proteins in Gram-positive bacteria.
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