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Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment Subcomplex Mutations.


ABSTRACT:

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Type IV pili (T4P) are dynamic protein filaments that mediate bacterial adhesion, biofilm formation, and twitching motility. The highly conserved PilMNOP proteins form an inner membrane alignment subcomplex required for function of the T4P system, though their exact roles are unclear. Three potential interaction interfaces for PilNO were identified: core-core, coiled coils (CC), and the transmembrane segments (TMSs). A high-confidence PilNO heterodimer model was used to select key residues for mutation, and the resulting effects on protein-protein interactions were examined both in a bacterial two-hybrid (BTH) system and in their native Pseudomonas aeruginosa context. Mutations in the oppositely charged CC regions or the TMS disrupted PilNO heterodimer formation in the B

SUBMITTER: Leighton TL 

PROVIDER: S-EPMC4455263 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature