Literature DB >> 11992127

The SAM domain of polyhomeotic forms a helical polymer.

Chongwoo A Kim1, Mari Gingery, Rosemarie M Pilpa, James U Bowie.   

Abstract

The polycomb group (PcG) proteins are important in the maintenance of stable repression patterns during development. Several PcG members contain a protein protein interaction module called a SAM domain (also known as SPM, PNT and HLH). Here we report the high-resolution structure of the SAM domain of polyhomeotic (Ph). Ph-SAM forms a helical polymer structure, providing a likely mechanism for the extension of PcG complexes. The structure of the polymer resembles that formed by the SAM domain of another transcriptional repressor, TEL. The formation of these polymer structures by SAM domains in two divergent repressors suggests a conserved mode of repression involving a higher order chromatin structure.

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Year:  2002        PMID: 11992127     DOI: 10.1038/nsb802

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  81 in total

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6.  The growth-suppressive function of the polycomb group protein polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain.

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