Spectral properties of three quaternary arrangements of Pseudomonas pilin.
Pseudomonas aeruginosa possess multisubunit, filamentous appendages called pili which are involved in adhesion, twitching motility, and bacteriophage adsorption. The spectral properties of three forms of pili have been compared. These are native pili, pilin dimers in octyl glycoside, and an in vitro assembled form of pilin which we call reassembled pilin filaments. Alkaline pH titrations, solvent perturbation, quenching of tryptophan fluorescence with acrylamide, and circular dichroism were used to demonstrate that tyrosines-24 and -27 are at a dimer/dimer interface in both native pili and in the reassembled pilin filaments. Dissociation of pili by octyl glucoside results in exposure of the two tyrosines and in partial exposure of a least one tryptophan in pilin.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification*; D002942:Circular Dichroism; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000648:ultrastructure*; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000302:isolation & purification*; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000648:ultrastructure*; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D008565:Membrane Proteins; D036781:Fimbriae Proteins