Abstract
Chlamydia trachomatis is an obligate intracellular bacterium that causes the most common sexually transmitted bacterial diseases in the world. With a biphasic developmental cycle, the bacteria utilize a type III secretion system (T3SS) to invade host cells as infectious elemental bodies, which then differentiate into actively dividing reticulate bodies. The regulation of the developmental cycle and the T3SS are linked by the bi-functional protein, specific Chlamydia chaperone 4 (Scc4). Scc4 is a class I T3SS chaperone forming a heterodimer with specific Chlamydia chaperone 1 (Scc1) to chaperone the essential virulence effector, Chlamydia outer membrane protein N. Scc4 also functions as a transcription factor by binding to the RNA polymerase holoenzyme between the flap region of the β subunit and region 4 of σ(66). In order to investigate the mechanism behind Scc4's dual functions and target its protein-protein interactions as a route for drug development, the structure and dynamics of Scc4 are being pursued. In the course of this effort, we assigned 89.2% of the backbone and sidechain (1)H, (15)N, and (13)C resonances of full-length Scc4. The assigned chemical shifts were used to predict the secondary structure and dynamic properties. The type and order of Scc4's determined secondary structure are consistent with the X-ray crystal structures of other bacterial T3SS chaperones.