Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Nature ◽  
2001 ◽  
Vol 410 (6824) ◽  
pp. 120-124 ◽  
Author(s):  
Andrew J. Bannister ◽  
Philip Zegerman ◽  
Janet F. Partridge ◽  
Eric A. Miska ◽  
Jean O. Thomas ◽  
...  
Keyword(s):  
Histone H3 ◽  
Selective Recognition ◽  
Chromo Domain ◽  
Methylated Lysine

scholarly journals Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3

2001 ◽  
Vol 20 (18) ◽  
pp. 5232-5241 ◽  
Author(s):  
Steven A. Jacobs ◽  
Sean D. Taverna ◽  
Yinong Zhang ◽  
Scott D. Briggs ◽  
Jinmei Li ◽  
...  
Keyword(s):  
Histone H3 ◽  
Chromo Domain ◽  
N Terminus

Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

Nature ◽  
2004 ◽  
Vol 432 (7015) ◽  
pp. 406-411 ◽  
Author(s):  
Yentram Huyen ◽  
Omar Zgheib ◽  
Richard A. DiTullio Jr ◽  
Vassilis G. Gorgoulis ◽  
Panayotis Zacharatos ◽  
...  
Keyword(s):  
Histone H3 ◽  
Double Strand Breaks ◽  
Dna Double Strand Breaks ◽  
Strand Breaks ◽  
Methylated Lysine

scholarly journals KDM4B: A Nail for Every Hammer?

Genes ◽  
2019 ◽  
Vol 10 (2) ◽  
pp. 134 ◽  
Author(s):  
Cailin Wilson ◽  
Adam J. Krieg
Keyword(s):  
Dna Damage ◽  
Cancer Progression ◽  
Histone H3 ◽  
Gene Repression ◽  
Epigenetic Changes ◽  
Histone Demethylases ◽  
Cellular Environment ◽  
Reversible Modification ◽  
Nuclear Processes ◽  
Methylated Lysine

Epigenetic changes are well-established contributors to cancer progression and normal developmental processes. The reversible modification of histones plays a central role in regulating the nuclear processes of gene transcription, DNA replication, and DNA repair. The KDM4 family of Jumonj domain histone demethylases specifically target di- and tri-methylated lysine 9 on histone H3 (H3K9me3), removing a modification central to defining heterochromatin and gene repression. KDM4 enzymes are generally over-expressed in cancers, making them compelling targets for study and therapeutic inhibition. One of these family members, KDM4B, is especially interesting due to its regulation by multiple cellular stimuli, including DNA damage, steroid hormones, and hypoxia. In this review, we discuss what is known about the regulation of KDM4B in response to the cellular environment, and how this context-dependent expression may be translated into specific biological consequences in cancer and reproductive biology.

scholarly journals Structure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3

2006 ◽  
Vol 34 (22) ◽  
pp. 6621-6628 ◽  
Author(s):  
Peng Zhang ◽  
Jiamu Du ◽  
Bingfa Sun ◽  
Xianchi Dong ◽  
Guoliang Xu ◽  
...  
Keyword(s):  
Histone H3 ◽  
Chromo Domain

scholarly journals Simultaneous Mutation of Methylated Lysine Residues in Histone H3 Causes Enhanced Gene Silencing, Cell Cycle Defects, and Cell Lethality in Saccharomyces cerevisiae

2007 ◽  
Vol 27 (19) ◽  
pp. 6832-6841 ◽  
Author(s):  
Yi Jin ◽  
Amy M. Rodriguez ◽  
Julie D. Stanton ◽  
Ana A. Kitazono ◽  
John J. Wyrick
Keyword(s):  
Cell Cycle ◽  
Histone H3 ◽  
Mitotic Cell ◽  
Histone Methyltransferase ◽  
Lethal Phenotype ◽  
Genome Wide ◽  
Lysine Residues ◽  
Sir Complex ◽  
Genomic Regions ◽  
Methylated Lysine

ABSTRACT The methylation of specific lysine residues in histone H3 is integral to transcription regulation; however, little is known about how combinations of methylated lysine residues act in concert to regulate genome-wide transcription. We have systematically mutated methylated histone lysine residues in yeast and found that the triple mutation of H3K4, H3K36, and H3K79 to arginine (H3 K4,36,79R) is lethal. The histone H3 K4,36,79R mutant causes a mitotic cell cycle delay and a progressive transcription defect that initiates in telomere regions and then spreads into the chromosome. This effect is mediated by the silent information regulator (SIR) silencing complex, as we observe increased binding of the SIR complex to genomic regions adjacent to yeast telomeres in the H3 K4,36,79R mutant and deletion of SIR2, SIR3, or SIR4 rescues the lethal phenotype. Curiously, a yeast strain in which the histone methyltransferase genes are simultaneously deleted is viable. Indeed, deletion of the histone methyltransferase genes can suppress the H3 K4,36,79R lethal phenotype. These and other data suggest that the cause of lethality may in part be due to the association of histone methyltransferase enzymes with a histone substrate that cannot be methylated.

scholarly journals Time makes histone H3 modifications drift

2021 ◽  
Author(s):  
Roman Hillje ◽  
Lucilla Luzi ◽  
Stefano Amatori ◽  
Mirco Fanelli ◽  
Pier Giuseppe Pelicci ◽  
...  
Keyword(s):  
Caloric Restriction ◽  
Histone Modifications ◽  
Histone H3 ◽  
Transcription Start ◽  
Transcription Start Sites ◽  
Genome Wide ◽  
Restriction Diet ◽  
Intergenic Regions ◽  
Genomic Regions ◽  
Methylated Lysine

Abstract To disclose the epigenetic drift of time passing, we determined the genome-wide distributions of mono- and tri-methylated lysine 4 and acetylated and tri-methylated lysine 27 of histone H3 in the livers of healthy 3, 6 and 12 months old C57BL/6 mice. The comparison of different age profiles of histone H3 marks revealed global redistribution of histone H3 modifications with time, in particular in intergenic regions and near transcription start sites, as well as altered correlation between the profiles of different histone modifications. Moreover, feeding mice with caloric restriction diet, a treatment known to retard aging, preserved younger state of histone H3 in these genomic regions.

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