13072_2016_66_MOESM1_ESM.pdf (594.72 kB)

MOESM1 of Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3

Download (594.72 kB)
journal contribution
posted 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.

Funding

Leukemia and Lymphoma Society

History