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作 者:Yanjing Li Kexue Gei Tingting Li Run Cai Yong Chen
机构地区:[1]State Key Laboratory of Molecular Biology,National Center for Protein Science Shanghai,Shanghai Institute of Biochemistry and Cell Biology,Center for Excellence in Molecular Cell Science,Chinese Academyof Sciences,320 Yue Yang Road,Shanghai 200031,China [2]State Key Laboratory of Bioreactor Engineering,East China University of Science and Technology,Shanghai Collaborative Innovation Center for Biomanufacturing(SCICB),Meilong Road 130,Shanghai 200237,China
出 处:《Protein & Cell》2023年第3期165-179,共15页蛋白质与细胞(英文版)
基 金:supported by grants from the Strategic Priority Research Program of the Chinese Academy of Sciences(XDB37010303 to Y.C.);the National Natural Science Foundation of China(31670748,31970576 to Y.C.,and 32071195 and 31900934 to Y.L.);the Young Elite Scientist Sponsorship Program by Chinese Association for Science and Technology(YESS20170198 to Y.L.);the National Postdoctoral Program for Innovative Talents(Bx201700263 to Y.L.).
摘 要:Histone lysine methyltransferases(HKMTs)deposit methyl groups onto lysine residues on histones and play important roles in regulating chromatin structure and gene expression.The structures and functions of HKMTs have been extensively investigated in recent decades,significantly advancing our understanding of the dynamic regulation of histone methylation.Here,we review the recent progress in structural studies of representative HKMTs in complex with nucleosomes(H3K4,H3K27,H3K36,H3K79,and H4K20 methyltransferases),with emphasis on the molecular mechanisms of nucleosome recognition and trans-histone crosstalk by these HKMTs.These structural studies inform HKMTs'roles in tumorigenesis and provide the foundations for developing new therapeutic approachestargetingHKMTs incancers.
关 键 词:NUCLEOSOME cryo-EM structures histone methyltransferases epigenetics histone methylation TUMORIGENESIS
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