Protein-protein interactions between keratin polypeptides expressed in the yeast two-hybrid system.

Keratin filaments are obligatory heteropolymers of type I and type II keratin polypeptides. Specific type I/type II pairs are coexpressed in vivo. In contrast, all type I/type II pairs assemble into filaments in vitro, but the different pairs have different stabilities as demonstrated by treatment with increasing concentrations of urea. ...
We have used the yeast two-hybrid system to analyse type I/type II interactions in a cellular context. We measured interactions between two different keratin pairs and we confirm the findings that K6+K17 form very stable heterodimers whereas K8+K18 interactions were weaker. The deletion of head domains did not reduce the strength of type I/type II interactions. Rather, the affinities were increased and the differences between the two pairs were retained in headless mutants. These findings argue against a major role of the head domains in directing heterodimer interactions and in defining heterodimer stabilities.
Mesh Terms:
Intermediate Filaments, Keratins, Molecular Biology, Peptides, Protein Binding, Saccharomyces cerevisiae, Sequence Deletion
Biochim. Biophys. Acta
Date: Jun. 22, 1998
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