1. Scc1 (CP0432) and Scc4 (CP0033) function as a type III secretion chaperone for CopN of Chlamydia pneumoniae.
- Author
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Silva-Herzog E, Joseph SS, Avery AK, Coba JA, Wolf K, Fields KA, and Plano GV
- Subjects
- Amino Acid Motifs, Bacterial Proteins chemistry, Bacterial Proteins genetics, Chlamydophila pneumoniae chemistry, Chlamydophila pneumoniae genetics, Molecular Chaperones chemistry, Molecular Chaperones genetics, Protein Binding, Protein Transport, Bacterial Proteins metabolism, Chlamydophila pneumoniae metabolism, Molecular Chaperones metabolism
- Abstract
The Chlamydia pneumoniae CopN protein is a member of the YopN/TyeA/InvE/MxiC family of secreted proteins that function to regulate the secretion of type III secretion system (T3SS) translocator and effector proteins. In this study, the Scc1 (CP0432) and Scc4 (CP0033) proteins of C. pneumoniae AR-39 were demonstrated to function together as a type III secretion chaperone that binds to an N-terminal region of CopN. The Scc1/Scc4 chaperone promoted the efficient secretion of CopN via a heterologous T3SS, whereas, the Scc3 chaperone, which binds to a C-terminal region of CopN, reduced CopN secretion.
- Published
- 2011
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