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Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins

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Abstract

Analysis of complementary DNA for human erythroid ankyrin indicates that the mature protein contains 1,880 amino acids comprising an N-terminal domain binding integral membrane proteins and tubulin, a central domain binding spectrin and vimentin, and an acidic C-terminal 'regulatory' domain containing an alternatively spliced sequence missing from ankyrin variant 2.2. The N-terminal domain is almost entirely composed of 22 tandem 33-amino-acid repeats. Similar repeats are found in yeast and invertebrate proteins involved in cell-cycle control and tissue differentiation.

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Authors and Affiliations

  1. Division of Hematology/Oncology, The Children's Hospital and Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts, 02115, USA

    Samuel E. Lux & Kathryn M. John

  2. Howard Hughes Medical Institute and Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, 27710, USA

    Vann Bennett

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  1. Samuel E. Lux
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  2. Kathryn M. John
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  3. Vann Bennett
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Lux, S., John, K. & Bennett, V. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature 344, 36–42 (1990). https://doi.org/10.1038/344036a0

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