The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by non-covalent ESI-MS

摘要

Evidence of a role for all three Usher domains in pilus assembly has been presented allowing a possible mechanism for pilus biogenesis to be proposed (Figure 6). Further, the data suggest a binding interface between the N-terminal domain of UsherN and the adhesin domain of PapG, the first subunit in the assembling pilus. These data provide new information about the protein-protein interactions that determine pilus biogenesis and highlight the power of non-covalent MS to interrrogate biological mechanisms[2].