A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions

Aidan J. Peterson, Michael Kyba, Douglas Bornemann, Kelly Morgan, Hugh W. Brock, Jeffrey Simon

Research output: Contribution to journalArticlepeer-review

128 Scopus citations

Abstract

The Sex comb on midleg (Scm) and polyhomeotic (ph) proteins are members of the Polycomb group (PEG) of transcriptional repressors. PcG proteins maintain differential patterns of homeotic gene expression during development in Drosophila flies. The Scm and ph proteins share a homology domain with 38% identity over a length of 65 amino acids, termed the SPM domain, that is located at their respective C termini. Using the yeast two-hybrid system and in vitro protein-binding assays, we show that the SPM domain mediates direct interaction between Scm and ph. Binding studies with isolated SPM domains from Scm and ph show that the domain is sufficient for these protein interactions. These studies also show that the Scm-ph and Scm-Scm domain interactions are much stronger than the ph-ph domain interaction, indicating that the isolated domain has intrinsic binding specificity determinants. Analysis of site-directed point mutations identifies residues that are important for SPM domain function these binding properties, predicted α- helical secondary structure, and conservation of hydrophobic residues prompt comparisons of the SPM domain to the helix-loop-helix and leucine zipper domains used for homotypic and heterotypic protein interactions in other transcriptional regulators. In addition to in vitro studies, we show colocalization of the Scm and ph proteins at polytene chromosome sites in vivo. We discuss the possible roles of the SPM domain in the assembly or function of molecular complexes of PcG proteins.

Original languageEnglish (US)
Pages (from-to)6683-6692
Number of pages10
JournalMolecular and cellular biology
Volume17
Issue number11
DOIs
StatePublished - Nov 1997

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