Activation and regulation of H2B-Ubiquitin-dependent histone methyltransferases

被引：37

作者：

Worden, Evan J. ^{[1
]}

Wolberger, Cynthia ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Biophys & Biophys Chem, Baltimore, MD 21205 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2019年 / 59卷

关键词：

SET DOMAIN; STRUCTURAL BASIS; H3K79; METHYLATION; LYSINE METHYLATION; H3; H2B; UBIQUITINATION; RECOGNITION; NUCLEOSOME; COMPASS;

D O I：

10.1016/j.sbi.2019.05.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Covalent modifications of histone proteins regulate a wide variety of cellular processes. Methylation of histone H3K79 and H3K4 is associated with active transcription and is catalyzed by Dot1L and Set1, respectively. Both Doti L and Sett are activated by prior ubiquitination of histone H2B on K120 in a process termed 'histone crosstalk'. Recent structures of Dot1L bound to a ubiquitinated nucleosome revealed how Dot1L is activated by ubiquitin and how Dot1L distorts the nucleosome to access its substrate. Structures of Dot1L-interacting proteins have provided insight into how Dot1L is recruited to sites of active transcription. Cryo-EM and crystallographic studies of the complex of proteins associated with Sett (COMPASS), uncovered the architecture of COMPASS and how Sett is activated upon complex assembly.

引用

页码：98 / 106

页数：9

共 66 条

[1] Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin [J].

Altaf, Mohammed ;

Utley, Rhea T. ;

Lacoste, Nicolas ;

Tan, Song ;

Briggs, Scott D. ;

Cote, Jacques .

MOLECULAR CELL, 2007, 28 (06) :1002-1014

[2] Structural Basis for Recognition of Ubiquitylated Nucleosome by Dot1L Methyltransferase [J].

Anderson, Cathy J. ;

Baird, Matthew R. ;

Hsu, Allen ;

Barbour, Emily H. ;

Koyama, Yuka ;

Borgnia, Mario J. ;

McGinty, Robert K. .

CELL REPORTS, 2019, 26 (07) :1681-+

[3] Nucleosome Structure(s) and Stability: Variations on a Theme [J].

Andrews, Andrew J. ;

Luger, Karolin .

ANNUAL REVIEW OF BIOPHYSICS, VOL 40, 2011, 40 :99-117

[4] Structural rearrangements of the histone octamer translocate DNA [J].

Bilokapic, Silvija ;

Strauss, Mike ;

Halic, Mario .

NATURE COMMUNICATIONS, 2018, 9

[5] Histone octamer rearranges to adapt to DNA unwrapping [J].

Bilokapic, Silvija ;

Strauss, Mike ;

Halic, Mario .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2018, 25 (01) :101-+

[6] Gene silencing -: Trans-histone regulatory pathway in chromatin [J].

Briggs, SD ;

Xiao, TJ ;

Sun, ZW ;

Caldwell, JA ;

Shabanowitz, J ;

Hunt, DF ;

Allis, CD ;

Strahl, BD .

NATURE, 2002, 418 (6897) :498-498

[7] Strategy for "Detoxification" of a Cancer-Derived Histone Mutant Based on Mapping Its Interaction with the Methyltransferase PRC2 [J].

Brown, Zachary Z. ;

Mueller, Manuel M. ;

Jain, Siddhant U. ;

Allis, C. David ;

Lewis, Peter W. ;

Muir, Tom W. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2014, 136 (39) :13498-13501

[8]

BUSCH H, 1981, MOL CELL BIOCHEM, V40, P173

[9]

Chatterjee C, 2010, NAT CHEM BIOL, V6, P267, DOI [10.1038/nchembio.315, 10.1038/NCHEMBIO.315]

[10] Targeting DOT1L and HOX gene expression in MLL-rearranged leukemia and beyond [J].

Chen, Chun-Wei ;

Armstrong, Scott A. .

EXPERIMENTAL HEMATOLOGY, 2015, 43 (08) :673-684

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