Involvement of tyrosine residues in the protomer-protomer interaction of Proteus mirabilis flagella as studied by spectroscopic methods, chemical modification and aggregation experiments.
Using spectrophotometrical titration, chemical modification, and ultraviolet difference spectral methods, the existence of at least two distinct tyrosine groups in the isolated flagellin of Proteus mirabilis flagella has been established. Three of the five flagellin tyrosines are buried in the protein matrix, whereas the other two seem to lie on the protein surface accessible to perturbants. Also about two tyrosine residues, presumably the latter ones exposed to the environment, can be nitrated with tetranitromethane in the monomeric flagellin with a concomitant loss of the polymerization ability after about one tyrosine per mol flagellin has been nitrated. Nitrated flagellin, homogeneous with respect to molecular weight, degree of nitration and isoelectric point, could be isolated and characterized. On the other hand, it could be shown that in the polymeric flagellum the phenolic groups of all five tyrosine residues are inaccessible to perturbing and modifying reagents. It seems, therefore, that the integrity of the phenolic groups is necessary for the proper folding and aggregation of the flagellin subunits to form the stable helical flagella.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis*; D001665:Binding Sites; D002942:Circular Dichroism; D005407:Flagella / Q000032:analysis*; D005408:Flagellin / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D011485:Protein Binding; D011487:Protein Conformation; D011513:Proteus mirabilis / Q000032:analysis; D013696:Temperature; D013774:Tetranitromethane; D014443:Tyrosine / Q000032:analysis*; D014783:Viscosity
D000596:Amino Acids; D001426:Bacterial Proteins; D005408:Flagellin; D014443:Tyrosine; D013774:Tetranitromethane