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Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments

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Abstract

We have determined the complete primary structure of an intermediate filament subunit, the 59,000 molecular weight subunit of mouse epidermal keratin, from the nucleotide sequence of cDNA clones. The central portion of the sequence forms extended tracts of a coiled-coil α-helical conformation. This is flanked at both termini by similar non-α-helical sequences that are extremely rich in glycine residues, frequently configured in tandem peptide repeats. Limited chymotryptic digestion of keratin filaments containing this protein suggests a structural organization whereby the terminal glycine-rich sequences protrude from a conserved core structure into which the coiled-coil α-helical segments are packed.

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Authors and Affiliations

  1. Dermatology Branch, National Cancer Institute, NIH, Building 10, Rm 12N238, Bethesda, Maryland, 20205, USA

    Peter M. Steinert & Robert H. Rice

  2. Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, NIH, Building 10, Rm 12N238, Bethesda, Maryland, 20205, USA

    Dennis R. Roop

  3. Computer Systems Laboratory, Division of Computer Research and Technology, National Institutes of Health, Bethesda, Maryland, 20205, USA

    Benes L. Trus

  4. Laboratory of Physical Biology, National Institute of Arthritis, Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, Maryland, 20205, USA

    Alasdair C. Steven

Authors
  1. Peter M. Steinert
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  2. Robert H. Rice
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  3. Dennis R. Roop
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  4. Benes L. Trus
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  5. Alasdair C. Steven
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Steinert, P., Rice, R., Roop, D. et al. Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments. Nature 302, 794–800 (1983). https://doi.org/10.1038/302794a0

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  • DOI: https://doi.org/10.1038/302794a0

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