R
Rui-Ming Xu
Researcher at Chinese Academy of Sciences
Publications - 102
Citations - 9645
Rui-Ming Xu is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Histone H3 & Histone. The author has an hindex of 48, co-authored 96 publications receiving 8661 citations. Previous affiliations of Rui-Ming Xu include University of Texas at Austin & Stony Brook University.
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Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27
Jinrong Min,Yi Zhang,Rui-Ming Xu +2 more
TL;DR: A 1.4-A-resolution structure of the chromodomain of Polycomb in complex with a hist one H3 peptide trimethylated at Lys 27 reveals a conserved mode of methyl-lysine binding and identifies Polycomb-specific interactions with histone H3, and proposes that self-association is functionally important for Polycomb.
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Cryo-em study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units
Feng Song,Ping Chen,Dapeng Sun,Mingzhu Wang,Liping Dong,Dan Liang,Rui-Ming Xu,Ping Zhu,Guohong Li +8 more
TL;DR: The 11-angstrom–resolution cryogenic electron microscopy (cryo-EM) structures of 30-nanometer chromatin fibers reconstituted in the presence of linker histone H1 and with different nucleosome repeat lengths provide mechanistic insights into how nucleosomes compact into higher-order Chromatin fibers.
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Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A
TL;DR: This study provides mechanistic insights into recognition of methylated histone tails by tudor domains and reveals the structural intricacy of methyl-lysine recognition by two closely spaced effector domains.
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Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
TL;DR: It is shown that Rad6-mediated ubiquitination of H2B lysine 123 is important for efficient methylation of lysin 79, but not lysines 36, of histone H3, and this study suggests that Rad 6 affects telomeric silencing, at least in part, by influencingmethylation of hist one H3.
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Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
TL;DR: Cells lacking Rtt109 or expressing rtt109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit increased sensitivity toward genotoxic agents, as well as elevated levels of spontaneous chromosome breaks.