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

MPG-Autoren
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Schnabel,  J.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Weber,  K.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Zitation

Schnabel, J., Weber, K., & Hatzfeld, M. (1998). Protein-protein interactions between keratin polypeptides expressed in the yeast two-hybrid system. Biochimica et Biophysica Acta-Molecular Cell Research, 1403(2), 158-168. doi:10.1016/S0167-4889(98)00036-6.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0010-2406-C
Zusammenfassung
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 If 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 TI 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.