Scc1 (CP0432) and Scc4 (CP0033) function as a type III secretion chaperone for CopN of Chlamydia pneumoniae.

Authors :: Silva-Herzog E
Joseph SS
Avery AK
Coba JA
Wolf K
Fields KA
Plano GV
Source :: Journal of bacteriology [J Bacteriol] 2011 Jul; Vol. 193 (14), pp. 3490-6. Date of Electronic Publication: 2011 May 13.
Publication Year :: 2011
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.

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

Full Text Access

Tools