The SAM domain of Polyhomeotic, RAE28, and Scm mediates specific interactions through conserved residues

Michael Kyba, Hugh W. Brock

Research output: Contribution to journalArticle

63 Scopus citations

Abstract

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 fruitfly, mouse, and yeast and show that all are capable of self-binding. Heterologous interactions are seen among a subset of SAM domains, including ph, Scm, and RAE28. Several conserved amino acid residues were mutated in the ph SAM domain, and the effects on self-binding and heterologous association were demonstrated. 133, 141, and 162 are shown to be important determinants of the binding interface, while W1 and G50 are likely essential for the structure of the domain.

Original languageEnglish (US)
Pages (from-to)74-84
Number of pages11
JournalDevelopmental Genetics
Volume22
Issue number1
DOIs
StatePublished - Mar 25 1998

Keywords

  • Chromatin
  • Polycomb group
  • SAM domain

Fingerprint Dive into the research topics of 'The SAM domain of Polyhomeotic, RAE28, and Scm mediates specific interactions through conserved residues'. Together they form a unique fingerprint.

  • Cite this