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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Polyhomeotic stably associates with molecular chaperones Hsc4 and Droj2 in Drosophila Kc1 cells.

Polycomb group (PcG) proteins silence target loci in Drosophila. Although the mechanism of PcG-mediated silencing remains unknown, there is considerable evidence that PcG proteins act via multiple complexes. We have epitope-tagged Polyhomeotic Proximal, PHP, the major isoform of the proximal product of the polyhomeotic locus, at both termini (F-PHP-HA) and generated a stable Kc1 cell line in order to isolate F-PHP-HA-associated proteins. Using either column chromatography followed by immunoaffinity precipitation or a double immunoaffinity precipitation procedure, we observed multiple proteins that stably associate with F-PHP-HA. Sequencing the five major bands identified PHP-170 and PHP-140 isoforms, Polycomb, Heat shock cognate 4 (Hsc4), and a novel Drosophila J class chaperone we term Droj2. Mutations in both chaperone genes enhance homeotic transformations in PcG genes, suggesting that they have a role in silencing. We show by Western blotting that minor components of F-PHP-HA-associated proteins include TBP, TAF(II)42, TAF(II)85, and p55. However, unlike in PRC1, Psc, TAF(II)62, Modulo, dMI-2, or Rpd3/HDAC1 do not associate with F-PHP-HA. We discuss the role of chaperones and F-PHP-HA-associated proteins in PcG- mediated silencing and the evidence for different complexes containing Polyhomeotic in vivo.[1]


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