DOI: 10.1016/s0960-9822(02)00901-6. Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain

Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain

10.1016/s0960-9822(02)00901-6

Crossref journal-article

Elsevier BV

Current Biology (78)

Bibliography

Feng, Q., Wang, H., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002). Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain. Current Biology, 12(12), 1052â1058.

Authors 7

Qin Feng (first)
Hengbin Wang (additional)
Huck Hui Ng (additional)
Hediye Erdjument-Bromage (additional)
Paul Tempst (additional)
Kevin Struhl (additional)
Yi Zhang (additional)

References 25 Referenced 707

10.1038/47412 / Nature / The language of covalent histone modifications by Strahl (2000)
10.1126/science.1063127 / Science / Translating the histone code by Jenuwein (2001)
10.1101/gad.927301 / Genes Dev. / Transcription regulation by histone methylation by Zhang (2001)
10.1016/S0959-437X(02)00287-3 / Curr. Opin. Genet. Dev. / Histone methylation in transcriptional control by Kouzarides (2002)
10.1038/35020506 / Nature / Regulation of chromatin structure by site-specific histone H3 methyltransferases by Rea (2000)
10.1101/gad.940201 / Genes Dev. / Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae by Briggs (2001)
10.1093/emboj/20.24.7137 / EMBO J. / The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4 by Roguev (2001)
10.1016/S1097-2765(01)00405-1 / Mol. Cell / Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase by Wang (2001)
10.1074/jbc.M101914200 / J. Biol. Chem. / SET-domain containing protein, G9a, is a novel lysine-preferring mammalian histone methylthansferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3 by Tachibana (2001)
10.1038/sj.onc.1204998 / Oncogene / Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor by Yang (2002)
10.1073/pnas.221596698 / Proc. Natl. Acad. Sci. USA / A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3 by Nagy (2002)
10.1016/S0960-9822(01)00652-2 / Curr. Biol. / Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism by Bryk (2002)
10.1101/gad.967202 / Genes Dev. / Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation by Nishioka (2002)
10.1128/MCB.22.5.1298-1306.2002 / Mol. Cell. Biol. / Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression by Strahl (2002)
10.1038/38444 / Nature / Crystal structure of the nucleosome core particle at 2.8 A resolution by Luger (1997)
10.1074/jbc.274.2.814 / J. Biol. Chem. / S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase by Niewmierzycka (1999)
10.1016/S0968-0004(01)01856-4 / Trends Biochem. Sci. / Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold by Dlakic (2001)
10.1101/gad.1001502 / Genes Dev. / Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association by Ng (2002)
10.1093/genetics/150.2.613 / Genetics / Identification of high-copy disruptors of telomeric silencing in Saccharomyces cerevisiae by Singer (1998)
10.1091/mbc.11.10.3601 / Mol. Biol. Cell / Role for the silencing protein Dot1 in meiotic checkpoint control by San-Segundo (2000)
10.1016/S0021-9258(19)45074-6 / J. Biol. Chem. / Studies of histone methylation during the HeLa S-3 cell cycle by Borun (1972)
10.1128/MCB.20.12.4188-4198.2000 / Mol. Cell. Biol. / Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms by Whitfield (2000)
{'key': '10.1016/S0960-9822(02)00901-6_BIB23', 'series-title': 'Current Protocols in Cell Biology', 'article-title': 'Determining cell cycle stage by flow cytometry', 'author': 'Darzynkiewicz', 'year': '1999'} / Current Protocols in Cell Biology / Determining cell cycle stage by flow cytometry by Darzynkiewicz (1999)
10.1016/S0092-8674(00)81758-4 / Cell / The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities by Zhang (1998)
10.1021/ac991071n / Anal. Chem. / Tuning of an electrospray ionization source for maximum peptide-ion transmission into a mass spectrometer by Geromanos (2000)

Dates

Type	When
Created	22 years, 10 months ago (Oct. 10, 2002, 7:40 p.m.)
Deposited	4 years, 2 months ago (May 26, 2021, 9:56 a.m.)
Indexed	2 weeks, 6 days ago (Aug. 2, 2025, 1:06 a.m.)
Issued	23 years, 2 months ago (June 1, 2002)
Published	23 years, 2 months ago (June 1, 2002)
Published Print	23 years, 2 months ago (June 1, 2002)

Funders 0

None

BibTeX

@article{Feng_2002, title={Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain}, volume={12}, ISSN={0960-9822}, url={http://dx.doi.org/10.1016/s0960-9822(02)00901-6}, DOI={10.1016/s0960-9822(02)00901-6}, number={12}, journal={Current Biology}, publisher={Elsevier BV}, author={Feng, Qin and Wang, Hengbin and Ng, Huck Hui and Erdjument-Bromage, Hediye and Tempst, Paul and Struhl, Kevin and Zhang, Yi}, year={2002}, month=jun, pages={1052–1058} }

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