Orthologs of known SWI/SNF complex subunits in human, fly and yeast.

<p>Orthologs of known SWI/SNF complex subunits in human, fly and yeast.</p

Abundance of purified proteins^‡ in each TAP-tag preparation.

‡<p>Protein abundance is represented by the exponentially modified Protein Abundance Index <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834-Ishihama1" target="_blank">[96]</a>.</p>*<p>mRNA abundance was estimated from probe set fluorescence signal intensities, as recommended by Affymetrix (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834.s002" target="_blank">Data S2</a>).</p

Complex walking.

<p>(A) Silver-stained gels of the actual purified protein preparations that were analyzed by mass spectrometry. The respective TAP-tag fusion proteins are designated by black triangles. Size markers (Da) are indicated for every gel. Banding patterns differ because the gels were not all run under the same conditions. (B) Osprey interaction network <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834-Breitkreutz1" target="_blank">[131]</a> based on the mass spectrometry results obtained with the material shown in panel A. Blue name labels indicate the TAP-tag fusion employed here. The thickness of the lines reflect purification yield and are proportional to the emPAI values <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834-Ishihama1" target="_blank">[96]</a> shown on <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone-0033834-t001" target="_blank">Table 1</a>. The presence of orthologs in yeast and <i>Drosophila</i> genomes of the human factors that are displayed is indicated on <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone-0033834-t002" target="_blank">Table 2</a>.</p

SS18 and the animal-specific SWI/SNF subunits.

<p>(A) Domain organization of the human proteins DPF1,-2,-3; PHF10; SS18 and its paralog SS18l1/crest; and BCL7A,-B,-C. We note that while CG2682, the <i>Drosophila melanogaster</i> ortholog of DPF2 (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone-0033834-t002" target="_blank">Table 2</a>), lacks the C2H2 domain, this domain is present in the <i>Tribolium</i> ortholog D6WFQ9_TRICA <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834-Richards1" target="_blank">[125]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834-Punta1" target="_blank">[132]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0033834#pone.0033834-Hunter1" target="_blank">[133]</a>, suggesting conservation of this domain in protostome and in deuterostome animals (B) Co-immunoprecipitation of SS18-SSX1^MYC by antibodies directed against human BRM. (C) Co-immunoprecipitation of SS18^MYC by antibodies directed against DPF2 and BRD9.</p