Cell
Volume 33, Issue 3, July 1983, Pages 915-924
Journal home page for Cell

Article
The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural domains among keratins

https://doi.org/10.1016/0092-8674(83)90034-XGet rights and content

Abstract

We present the cDNA and amino acid sequences of a cytoskeletal keratin from human epidermis (Mr = 56K) that belongs to one of the two classes of keratins (Type I and Type II) present in all vertebrates. In these two types of keratins the central ∼300 residue long regions share ∼30% homology both with one another and with the sequences of other IF proteins. Within this region, all IF proteins are predicted to contain four helical domains demarcated from one another by three regions of β-turns. The amino and carboxy termini of the Type II keratin are very different from those of microfibrillar keratins and other nonkeratin IF proteins. However, they contain unusual glycine-rich tandem repeats similar to the amino terminus of the Type I keratin. Thus the size heterogeneity among keratins appears to be a result of differences in the length of the terminal ends rather than the structurally conserved central region.

References (50)

  • D. Henderson et al.

    A periodic ultrastructure in intermediate filaments

    J. Mol. Biol.

    (1982)
  • B.-S. Hong et al.

    Isolation and characterization of a soluble, immunoactive peptide of glial fibrillary acidic protein

    Biochim. Biophys. Acta

    (1981)
  • L.N. Jones

    The isolation and characterization of a-keratin microfibrils

    Biochim. Biophys. Acta.

    (1975)
  • A.D. McLachlan

    Coiled coil formation and sequence regularities in the helical regions of α-keratin

    J. Mol. Biol.

    (1978)
  • A.D. McLachlan et al.

    Periodic charge distribution in the intermediate filament proteins desmin and vimentin

    J. Mol. Biol.

    (1982)
  • R. Moll et al.

    The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells

    Cell

    (1982)
  • D.A.D. Parry et al.

    Structure of a-keratin: structural implications of the amino acid sequence of the Type I and Type II chain segments

    J. Mol. Biol.

    (1977)
  • D. Skerrow et al.

    Isolation and characterization of the helical regions of epidermal prekeratin

    J. Biol. Chem.

    (1973)
  • P.M. Steinert et al.

    Self-assembly of bovine epidermal keratin filaments in vitro

    J. Mol. Biol.

    (1976)
  • P.M. Steinert

    Structure of the three-chain unit of the bovine epidermal keratin filament

    J. Mol. Biol.

    (1978)
  • S. Wain-Hobson et al.

    Preferential codon usage in genes

    Gene

    (1981)
  • D.L. Brutlag et al.

    SEQ: a nucleotide sequence analysis and recombination system

    Nucl. Acids Res.

    (1982)
  • P.Y. Chou et al.

    Prediction of protein conformation

    Biochemistry

    (1974)
  • P.Y. Chou et al.

    Prediction of the secondary structure of proteins from their amino acid sequence

    Adv. Enzymol.

    (1978)
  • W.G. Crewther et al.

    The preparation and properties of large peptides from the helical regions of the low-sulfur proteins of wool

  • Cited by (0)

    View full text