MOESM1 of Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3
journal contributionposted on 30.04.2016, 05:00 by Sarah Hainer, Joseph Martens
Additional file 1: Fig. S1. Histone residue substitutions do not alter total protein levels. (a) Western analysis examining the effect of histone mutants on total histone H3, H2B, Spt6, Spt16, Pob3, Asf1-TAP, HA-Paf1, and Spt2-Myc protein levels. Strains expressing the indicated histone alleles (YS417, YS404, YS409, YS428, YS454, YS458, YS462, YS471, YS493, YS504, YS518, YS525) were grown to approximately 3 × 107 cells/mL in YPD at 30 °C. Proteins were extracted with trichloroacetic acid and subjected to Western analysis using anti-H3, anti-H2B, anti-Spt6, anti-Spt16, anti-Pob3, anti-PAP, anti-HA, anti-Myc, and anti-G6PDH (loading control). (b) Quantitation of Western analysis, where similar results were obtained for three independent experiments and WT was arbitrarily set to 1 and error bars represent the mean ± SEM of three biological replicate experiments.