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PMID: 2448790 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Sequence of the human 40-kDa keratin reveals an unusual structure with very high sequence identity to the corresponding bovine keratin.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 85 ·No. 4 ·1988-02-00 ·Pages 1114-8

Eckert RL

Abstract

The complete amino acid and DNA sequences of the human 40-kDa keratin are reported. The DNA sequence encodes a protein of 44,098 Da, which is unique in that it lacks the terminal non-alpha-helical tail segment found in all other keratins. When the human 40-kDa keratin amino acid sequence is compared to the corresponding bovine keratin, the overall identity is 89%. The coil-forming regions are 89% identical and the head regions are 88% identical. This similarity is also evident in the DNA sequence of the coding region, the 5' upstream sequences, and the 3' noncoding sequences. The high degree of cross-species identity between bovine and human 40-kDa keratins suggests that there is strong evolutionary pressure to conserve the structure of this keratin. This in turn suggests an important and universal role for this intermediate filament subunit in all species.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cattle/genetics Humans Keratins/genetics Molecular Sequence Data Sequence Homology, Nucleic Acid Species Specificity
Chemicals
Keratins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Eckert R L
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
References (26)
26 references, click to expand
  1. A simple and very efficient method for generating cDNA libraries.
    Gene. 1983 Nov;25(2-3):263-9 PMID: 6198242
  2. Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits.
    J Biol Chem. 1985 Jun 10;260(11):7142-9 PMID: 2581964
  3. AUG is the only recognisable signal sequence in the 5' non-coding regions of eukaryotic mRNA.
    Nature. 1978 Jul 6;274(5666):84-7 PMID: 662001
  4. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I.
    J Mol Biol. 1977 Jun 15;113(1):237-51 PMID: 881736
  5. Efficient isolation of genes by using antibody probes.
    Proc Natl Acad Sci U S A. 1983 Mar;80(5):1194-8 PMID: 6219389
  6. A new method for sequencing DNA.
    Proc Natl Acad Sci U S A. 1977 Feb;74(2):560-4 PMID: 265521
  7. Coordinate control by vitamin A of keratin gene expression in human keratinocytes.
    J Biol Chem. 1985 Nov 15;260(26):14026-9 PMID: 2414289
  8. Complete sequence of a gene encoding a human type I keratin: sequences homologous to enhancer elements in the regulatory region of the gene.
    Proc Natl Acad Sci U S A. 1985 Mar;82(6):1609-13 PMID: 2580298
  9. The role of keratin subfamilies and keratin pairs in the formation of human epidermal intermediate filaments.
    J Cell Biol. 1986 May;102(5):1767-77 PMID: 2422179
  10. Amino acid sequence and gene organization of cytokeratin no. 19, an exceptional tail-less intermediate filament protein.
    EMBO J. 1986 Aug;5(8):1865-75 PMID: 2428612
  11. Structure of a gene for the human epidermal 67-kDa keratin.
    Proc Natl Acad Sci U S A. 1985 Apr;82(7):1896-900 PMID: 2580302
  12. Regulation of terminal differentiation of cultured human keratinocytes by vitamin A.
    Cell. 1981 Sep;25(3):617-25 PMID: 6169442
  13. New vectors for rapid sequencing of DNA fragments by chemical degradation.
    Gene. 1987;51(2-3):247-54 PMID: 3596245
  14. The molecular biology of intermediate filaments.
    Cell. 1985 Sep;42(2):411-20 PMID: 2411418
  15. Identification of two types of keratin polypeptides within the acidic cytokeratin subfamily I.
    J Mol Biol. 1984 Oct 25;179(2):257-81 PMID: 6209405
  16. A new small (40 kd) keratin filament protein made by some cultured human squamous cell carcinomas.
    Cell. 1981 Sep;25(3):627-35 PMID: 6169443
  17. Pair formation and promiscuity of cytokeratins: formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides.
    J Cell Biol. 1985 Nov;101(5 Pt 1):1826-41 PMID: 2414304
  18. Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins.
    Annu Rev Biochem. 1982;51:219-50 PMID: 6180679
  19. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins.
    EMBO J. 1982;1(12):1649-56 PMID: 6202512
  20. Empirical predictions of protein conformation.
    Annu Rev Biochem. 1978;47:251-76 PMID: 354496
  21. New M13 vectors for cloning.
    Methods Enzymol. 1983;101:20-78 PMID: 6310323
  22. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins.
    J Mol Biol. 1978 Mar 25;120(1):97-120 PMID: 642007
  23. The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells.
    Cell. 1982 Nov;31(1):11-24 PMID: 6186379
  24. Three tightly linked genes encoding human type I keratins: conservation of sequence in the 5'-untranslated leader and 5'-upstream regions of coexpressed keratin genes.
    Mol Cell Biol. 1986 Feb;6(2):539-48 PMID: 2431270
  25. Differentiation-related patterns of expression of proteins of intermediate-size filaments in tissues and cultured cells.
    Cold Spring Harb Symp Quant Biol. 1982;46 Pt 1:431-53 PMID: 7049531
  26. Cloning of cDNAs specifying vitamin A-responsive human keratins.
    Proc Natl Acad Sci U S A. 1984 Jul;81(14):4321-5 PMID: 6205395
Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.85.4.1114
Published
1988-02-00
Pages
1114-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC279716
Subset
IM
Databases
GENBANK
J03607
External Links
PubMed source DOI: 10.1073/pnas.85.4.1114 PMC Full Text View journal details
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