|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins
| Title: | Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins |
| Authors: | Yamashita, Daichi Browse this author | | Sugawara, Takaki Browse this author | | Takeshita, Miyu Browse this author | | Kaneko, Jun Browse this author →KAKEN DB | | Kamio, Yoshiyuki Browse this author →KAKEN DB | | Tanaka, Isao Browse this author →KAKEN DB | | Tanaka, Yoshikazu Browse this author →KAKEN DB | | Yao, Min Browse this author →KAKEN DB |
| Issue Date: | Sep-2014 |
| Publisher: | Nature Publishing Group |
| Journal Title: | Nature Communications |
| Volume: | 5 |
| Start Page: | 4897 |
| Publisher DOI: | 10.1038/ncomms5897 |
| PMID: | 25263813 |
| Abstract: | Pathogenic bacteria secrete pore-forming toxins (PFTs) to attack target cells. PFTs are expressed as water-soluble monomeric proteins, which oligomerize into nonlytic prepore intermediates on the target cell membrane before forming membrane-spanning pores. Despite a wealth of biochemical data, the lack of high-resolution prepore structural information has hampered understanding of the beta-barrel formation process. Here, we report crystal structures of staphylococcal gamma-haemolysin and leucocidin prepores. The structures reveal a disordered bottom half of the beta-barrel corresponding to the transmembrane region, and a rigid upper extramembrane half. Spectroscopic analysis of fluorescently labelled mutants confirmed that the prepore is distinct from the pore within the transmembrane region. Mutational analysis also indicates a pivotal role for the glycine residue located at the lipid-solvent interface as a 'joint' between the two halves of the beta-barrel. These observations suggest a two-step transmembrane beta-barrel pore formation mechanism in which the upper extramembrane and bottom transmembrane regions are formed independently. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/58223 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 田中 良和
|
