- 作者: Wei-Wen Kuo; Hung-Wei Kuo; Chun-Chia Cheng; Hsiang-Ling Lai; Ling-Yun Chen
- 作者服務機構: Institute of Biochemistry, Chung Shan Medical University, Taichung 402, Taiwan, Republic of China
- 中文摘要: --
- 英文摘要: Due to their similarity to type IV pilus (Tfp) subunits, the pseudopilins, XpsG, -H, -I, -J and -K, have been predicted to form a pilus-like structure in the type II secretion (T2S) pathway. While overexpression of GspG can result in the formation of bundle structures, the functions of other pseudopilin are not known yet. In this study, we investigate the mutual interaction among the pseudopilins and characterize the specialized minor pseudopilin, XpsJ. By using gel filtration and Ni-NTA affinity chromatography, a linearly ordered interactive relationship is revealed among the four pseudopilins, XpsG-XpsI-XpsH-XpsJ. Notably, unlike the mutant XpsJ194 staying in the inner membrane, wild type XpsJ stayed in the outer membrane and blocked the extension of overexpressed XpsG to outside of the cell. By analogy with the Type I pilus structures, we hypothesize that the XpsH and XpsI might act as an adaptor to connect XpsJ with the major pseudopilin XpsG, and XpsJ might act as a tip to restrict the out-growth of XpsG in the pilus-like structure of the T2S pathway.
- 中文關鍵字: --
- 英文關鍵字: major pseudopilin, minor pseudopilin, tip, type IV pili, type I pili, type II secretion pathway