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The hair follicle consists of a complex system ofmultiple tissue compartments that are clearly distinguishable by theirmorphology and type of differentiation. We have synthesized hairfolliclespecific keratins from the companion layer (K6hf, K17) and the haircortex (Ha1, Hb3, Hb6) in Escherichia coli. The assembly of purified keratinsin mixtures of K6hf/K17 and in mixtures of hair cortex keratins was compared inurea solutions, low ionic strength and physiological strength buffers, by ureamelting gels, electron microscopy and analytical ultracentrifugation. Bothtypes of keratin mixtures, keratins from the companion layer and keratins fromthe hair cortex, formed heterotypic complexes at 5 M urea. In low ionicstrength buffers, the keratins from the companion layer were assembled to bonafide intermediate filaments. In contrast, mixtures of hair cortex keratinsstayed in an oligomeric state with a mean s value of 9 as determined insedimentation velocity experiments. Hair cortex keratins were, however,assembled into intermediate filaments at physiological salt conditions. A pointmutated hair cortex keratin [Hb6(Glu402Lys)] formed no long filaments whenmixed with Ha1; instead, the assembled structures showed a length distributionof 50.8±13.4 nm, comparable to the size distribution of assembly intermediatescalled unitlength filaments.

The in vitro Assembly of Hair Follicle Keratins: Comparison of Cortex and Companion Layer Keratins