Fig. 5: Histone modifications modulate OCT4 binding to the nMATN1 nucleosome.
From: Histone modifications regulate pioneer transcription factor cooperativity
a, Structural model of human OCT4 (orange) bound to a nucleosome (grey) assembled with a 186-bp DNA fragment from the nMATN1 regulatory element. b, Surface model showing the electrostatic potential of the OCT4-POUS domain and the positively charged histone H3 tail. c, Representative native gel electrophoresis showing OCT4 binding to unmodified or nMATN1-H3K27ac nucleosomes (left). The coloured asterisks mark molecules bound to the nucleosome: 1-OCT4 is in red, 2-OCT4 is in blue, 3-OCT4 is in green and 4-OCT4 is in purple. Quantification of OCT4 binding to nMATN1-H3K27ac relative to unmodified nucleosomes (right), using bands marked with asterisks. Data shown are mean ± s.e.m. of four independent experiments; *P = 0.02 and **P = 0.008, one-sided Student’s t-test. d, Representative native gel electrophoresis showing OCT4 binding to unmodified or nMATN1-H3K27me3 nucleosomes (left). The coloured asterisks are as in panel c. Quantification of OCT4 binding to nMATN1-H3K27me3 relative to unmodified (right), using bands marked with asterisks. Data shown are mean ± s.e.m. of four independent experiments; ***P = 0.0007 (2-OCT4) and ***P = 0.0004 (3-OCT4), one-sided Student’s t-test.
