Summary
Intermediate filaments are composed of a family of proteins that evolved from a common ancestor. The proteins consist of three domains: a central, alpha-helical domain similar in all intermediate filaments, bracketed by two domains that are variable in length and structure. Within the intermediate-filament family, several subfamilies have been recognized by immunologic and nucleic acid hybridization techniques. In this paper we present the sequence of the genomic DNA coding for a 65-kilodalton human keratin and compare it with the sequences of other intermediate-filament proteins. While the central, alpha-helical domains of these proteins show homologies that indicate a common ancestor, the sequences of the variable terminal domains indicate that the variable domains evolved through a series of tandem duplications and possibly by gene-conversion mechanisms.
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Klinge, E.M., Sylvestre, Y.R., Freedberg, I.M. et al. Evolution of keratin genes: Different protein domains evolve by different pathways. J Mol Evol 24, 319–329 (1987). https://doi.org/10.1007/BF02134130
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DOI: https://doi.org/10.1007/BF02134130