Lee, Seongyeol Lee, Jieon Chae, Sehyun Moon, Yunwon Lee, Ho-Youl Park, Bongju Yang, Eun Gyeong Hwang, Daehee Park, Hyunsung 2024-01-20T00:03:08Z 2024-01-20T00:03:08Z 2021-09-03 2017-11-16 0305-1048 https://pubs.kist.re.kr/handle/201004/122053 Hypoxia increases both active and repressive histone methylation levels via decreased activity of histone demethylases. However, how such increases coordinately regulate induction or repression of hypoxia-responsive genes is largely unknown. Here, we profiled active and repressive histone tri-methylations (H3K4me3, H3K9me3, and H3K27me3) and analyzed gene expression profiles in human adipocyte-derived stem cells under hypoxia. We identified differentially expressed genes (DEGs) and differentially methylated genes (DMGs) by hypoxia and clustered the DEGs and DMGs into four major groups. We found that each group of DEGs was predominantly associated with alterations in only one type among the three histone tri-methylations. Moreover, the four groups of DEGs were associated with different TFs and localization patterns of their predominant types of H3K4me3, H3K9me3 and H3K27me3. Our results suggest that the association of altered gene expression with prominent single-type histone tri-methylations characterized by different localization patterns and with different sets of TFs contributes to regulation of particular sets of genes, which can serve as a model for coordinated epigenetic regulation of gene expression under hypoxia. English OXFORD UNIV PRESS CHROMATIN SIGNATURES STEM-CELLS HIF-ALPHA H3 LYS4 DEMETHYLASES INHIBITION BINDING O-2 TRIMETHYLATION PLURIPOTENT Multi-dimensional histone methylations for coordinated regulation of gene expression under hypoxia Article 10.1093/nar/gkx747 1 NUCLEIC ACIDS RESEARCH, v.45, no.20, pp.11643 - 11657 NUCLEIC ACIDS RESEARCH 45 20 11643 11657 scie scopus 000416164300020 2-s2.0-85038037055 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article CHROMATIN SIGNATURES STEM-CELLS HIF-ALPHA H3 LYS4 DEMETHYLASES INHIBITION BINDING O-2 TRIMETHYLATION PLURIPOTENT