Equitable Value: Promoting Economic Mobility and Social Justice through Postsecondary Education

While structural racism has been part of the United States since before its founding, continued racial and gender violence alongside the coronavirus pandemic have exacerbated racial inequities across the country. The disproportionate impact of these events on people of color has catalyzed nationwide activism leading to renewed conversations about who has true access to opportunity in this country. Against this backdrop, the Postsecondary Value Commission leveraged diverse voices and experiences to interrogate the role that postsecondary education can—and should—play in promoting opportunity, paving an equitable path to economic mobility, and dismantling centuries of racist, classist, and sexist attitudes and policies. To be clear: overall, postsecondary education offers individuals the opportunity to earn a better living and build a better life for themselves and their families, while also fostering a healthier, more democratic society. Yet, troubling disparities in access to these opportunities exist by race, ethnicity, socioeconomic status, and gender

Additional file 1 of De novo methylation of histone H3K23 by the methyltransferases EHMT1/GLP and EHMT2/G9a

Additional file 1: Figure S1. EHMT1/GLP and EHMT2/G9a de novo methylate H3K18, H3K23, and H3K27, in vitro. (A) Annotated spectra, ions counts and mass error tables for the mass spectrometry analysis of EHMT1/GLP and EHMT2/G9a in vitro HMT reactions (B) Western blot panel of EHMT1/GLP and EHMT2/G9a in vitro HMT reactions for various H3K18 and H3K27 methylation states. H3K4me3 and H3K36me3 were included as negative controls. 50B11 whole cell lysate was used to validate that antibodies for H3K27me1/2, H3K4me3, and H3K36me3, were functional given these modifications were not detected by western blotting in EHMT1/GLP and EHMT2/G9a in vitro HMT reactions. Figure S2. Pharmacologic inhibition of EHMT1/GLP and EHMT2/G9a decreases H3K18 and H3K27 methylation in vitro. (A) UNC0642 dose titration with recombinant SetDB1 and Suv39h2, as measured by the MTase-Glo assay. (B) Western blotting panel showing production and inhibition of various H3K18 and H3K27 methylation states by EHMT1/GLP and EHMT2/G9a. Unlike H3K27me3, H3K27me1 and H3K27me2 were undetectable in this in vitro assay. Figure S3. Pharmacologic inhibition of EHMT1/GLP and EHMT2/G9a decrease H3K18 and H3K27 methylation in vivo. (A) Western blot panel of H3K9, H3K18, H3K23 and H3K27 methylation states in MC38 cells treated with DMSO or UNC0642. (B) Western blot panel of H3K18 and H3K27 methylation states of 50B11 cells treated with DMSO or UNC0642 (C)Western blot panel of H3K18 and H3K27 methylation states of HEK293 cells treated with DMSO or UNC0642. Figure S4. H3K9M, but not H3K23M, decrease H3K23me3 in vivo. (A) MC38 and (B) 50B11 cells lines were transduced with lentivirus carrying plasmids encoding various lysine (K) to methionine (M) mutations at specific residues (e.g. (, 23, 27, etc.) to evaluate their corresponding effect on various histone H3 methylation state in vivo. Figure S5. Genetic ablation of GLP, G9a or both perturbs H3K18 and H3K27 methylation in vivo. Western blot of H3K18 and H3K27 methylation states in mouse ESCs knocking down either EHMT1/GLP, EHMT2/G9a or both and their corresponding effect on H3K18 and h3K27 methylation states. Figure S6. Antibody validation via ELISA and peptide competition assays. Using a 96-well plate ELISA format, ELISAs and peptide competition assays were done to validate H3K9me1, H39me2, H3K9me3, H3K18me1, H3K18me2, H3K18me3, H3K23me1, H3K23me2 H3K23me3, H3K27me1, H3K27me2, and H3M27me3 antibodies for their target methylation state, cross-reactivity with other methylation states of the same epitope and cross-reactivity with methyl-lysines of a different epitope (e.g. K9 antibodies with K23-methyl peptides, etc.)