SAM: A novel motif in yeast sterile and drosophila polyhomeotic proteins

Authors

  • Christopher P. Ponting

    Corresponding author
    1. Fibrinolysis Research Unit, University of Oxford, The Old Observatory, Oxford OX1 3RH, United Kingdom
    • Fibrinolysis Research Unit, University of Oxford, The Old Observatory, South Parks Road, Oxford OX1 3RH, United Kingdom
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Abstract

Single copies of an ≈65–70 residue domain are shown to be present in the sequences of 14 eukaryotic proteins, including yeast byr2, STE11, ste4, and STE50, which are essential participants in sexual differentiation. This domain, named SAM (sterile alpha motif), appears to participate in other developmental processes because it is also present in Drosophila polyhomeotic gene product and related homologues, which are thought to regulate determination of segmental specification in early embryo-genesis. Its appearance in byr2 and STEI1, which are MEK kinases, and in proteins containing pleckstrin homology, src homology 3, and discs-large homologous region domains, suggests possible participation in signal transduction pathways.

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