Doetsch, Martina Gluch, Angela Poznanović, Goran Bode, Juergen Vidaković, Melita Differences in the avidity of YY1 association examined for six potential binding motifs in <i>muPARP-1</i>. <p>Oligonucleotides containing the YY1 binding motif (BM1 to 5, 7) and a control (BM6) served as probes for EMSA. For each radioactive probe the binding reaction was performed either in the absence or presence of NIH3T3 nuclear extract. A third competition reactions contained a 200-fold molar excess of particular unlabeled oligonucleotides (BM 1–7) in order to illustrate the specificity of the protein:DNA interactions. A fourth reaction contained anti-YY1 antibody (H-414; Santa Cruz). Samples were run on an 8% polyacrylamide gel. Arrows indicate bands shifted by YY1/oligonucleotide binding alone (central lines in each group) whereas supershifts by the antibody are evident in the rightmost lanes for BM1, BM4 and BM7. Inset – Immunoblot analysis of NIH3T3 cell lysates revealed the presence of a degradation product (YY1*), as already reported <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0044125#pone.0044125-Klar3" target="_blank">[52]</a>.</p> avidity;yy1;examined;binding;motifs 2013-02-20
    https://plos.figshare.com/articles/figure/_Differences_in_the_avidity_of_YY1_association_examined_for_six_potential_binding_motifs_in_muPARP_1_/255470
10.1371/journal.pone.0044125.g003