The SAM domain of polyhomeotic, RAE28, and scm mediates specific interactions through conserved residues.

@article{Kyba1998TheSD,
  title={The SAM domain of polyhomeotic, RAE28, and scm mediates specific interactions through conserved residues.},
  author={Michael Kyba and Hugh W Brock},
  journal={Developmental genetics},
  year={1998},
  volume={22 1},
  pages={74-84}
}
The SAM (sterile alpha motif) domain is a 65- to 70-amino acid sequence found in many diverse proteins whose functions range from signal transduction to transcriptional repression. We show that the SAM domain of the Drosophila Polycomb group protein, polyhomeotic (ph), is capable of binding to itself in vitro. We test a number of near relatives of the ph SAM domain from fruit fly, mouse, and yeast and show that all are capable of self-binding. Heterologous interactions are seen among a subset… CONTINUE READING
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