Nature News

Structural bases of nucleosome recognition and modification by MLL methyltransferases

1.

Ruthenburg, A.J., Allis, C.D. & Wysocka, J. Methylation of lysine Four on histone H3: complexity of writing and studying a single epigenetic signal. Mol. Cell 25, 15-30 (2007).

2

Shilatifard, A. The COMPASS household of histone H3K4 methylases: mechanisms regulating the event and pathogenesis of the illness. Annu. Rev. Biochem. 81, 65-95 (2012).

Three

Krivtsov, A.V. & Armstrong, S.A.MLL translocations, histone modifications, and leukemia stem cell improvement. Nat. Rev. Most cancers 7, 823-833 (2007).

Four

Rao, R.C. & Dou, Y. Diversified in most cancers: the KMT2 methyltransferase household (MLL). Nat. Rev. Most cancers 15, 334-346 (2015).

5

Lee, J. et al. The focused inactivation of MLL3 histone H3 – Lys-Four methyltransferase exercise in mice reveals key roles for MLL3 in adipogenesis. Proc. Natl Acad. Sci. USA 105, 19229-19324 (2008).

6

Ortega-Molina, A. et al. The histone lysine methyltransferase KMT2D helps a gene expression program that represses the event of B-cell lymphoma. Nat. Med. 21, 1199-1208 (2015).

7.

Dou, Y. et al. Regulation of the exercise of methyltransferase MLL1 H3K4 by its central parts. Nat. Struct. Mol. Biol. 13, 713-719 (2006).

eight

Patel, A., Dharmarajan, V., Vought, V.E. & Cosgrove, M.S. On the mechanism of a number of methylation of lysine by the core advanced of human blended lineage leukemia protein (MLL1). J. Biol. Chem. 284, 24242-24256 (2009).

9

Li, Y. et al. Structural foundation for the regulation of the exercise of methyltransferases of the MLL household. Nature 530, 447-452 (2016).

ten.

Solar, Z.-W. & Allis, C. D. The ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418, 104-108 (2002).

11

Fierz, B. et al. Histone H2B ubiquitylation disrupts native compaction and better order chromatin. Nat. Chem. Biol. 7, 113-119 (2011).

12

Kim, J. et al. The ubiquitylation of H2B coupled with RAD6-mediated transcription instantly stimulates the methylation of H3K4 in human cells. Cell 137, 459-471 (2009).

13

Mittal, A. et al. The construction of the β-propeller area of RbBP5 reveals a floor with potential websites for binding to the nucleic acid. Nucleic Acids Res. 46, 3802-3812 (2018).

14

Wilson, M.D. et al. Structural foundation of 53BP1 modified nucleosome recognition. Nature 536, 100-103 (2016).

15

Patel, A., Dharmarajan, V. & Cosgrove, M. S. Construction of WDR5 linked to leukemia protein-1 peptide of blended line. J. Biol. Chem. 283, 32158-32161 (2008).

16

Odho, Z., Southall, SM & Wilson, JR Characterization of a brand new WDR5 binding website that recruits RbBP5 by a conserved motif to boost the methylation of histone H3 lysine Four by Leukemia Protein 1 of blended line. J. Biol. Chem. 285, 32 967-32976 (2010).

17

Qu, Q. et al. Construction and conformational dynamics of a compound COMPASS histone H3K4 methyltransferase. Cell 174, 1117-1126.e12 (2018).

18

Hsu, P. L. et al. Crystalline construction of the COMPASS H3K4 methyltransferase catalytic module. Cell 174, 1106-1116.e9 (2018).

19

Takahashi, Y.H. et al. Structural evaluation of the COMPASS household of histone H3K4 methylases from yeast to people. Proc. Natl Acad. Sci. USA 108, 20526-20531 (2011).

20

Armache, Okay.J., Garlick, J.D., D. Canzio, D.Narlikar, G.J. and Kingston, R.E. Structural foundation of silence: the Sir3 BAH area advanced with a nucleosome at a decision of three.zero Å. Science 334, 977-982 (2011).

21

Jiao, L. & Liu, X. Structural bases of the histone H3K27 trimethylation by an lively repressive polycomb advanced 2. Science 350, aac4383 (2015).

22

Qiao, Q. et al. The construction of NSD1 reveals a self-regulating mechanism underlying the methylation of histone H3K36. J. Biol. Chem. 286, 8361-8368 (2011).

23

Zhang, X. et al. Structural foundation of the specificity of histone lysine methyltransferases to the product. Mol. Cell 12, 177-185 (2003).

24

Shinsky, S.A. and Cosgrove, M.S. Distinctive function of the WD-40 repetition protein subunit (WDR5) in blended lineage leukemia histone Three methyltransferase advanced (MLL3). J. Biol. Chem. 290, 25819-25833 (2015).

25

Worden, E.J., Hoffmann, N.A., Hicks, C.W. and Wolberger, C. Mechanism of cross-interaction between H2B ubiquitination and methylation of H3 by Dot1L. Cell 176, 1490-1501e12 (2019).

26

Anderson, C.J. et al. Structural foundation for ubiquitylated nucleosome recognition by Dot1L methyltransferase. Cell Studies 26, 1681-1690.e5 (2019).

27

Valencia-Sánchez, M.I. et al. Structural foundation of Dot1L stimulation by ubiquitination with histone H2B lysine 120. Mol. Cell 74, 1010-1019.e6 (2019).

28

Jang, S. et al. Structural foundation of recognition and destabilization of the nucleosome ubiquitinated by H2B histone by histone DOT1L H3 Lys79 methyltransferase. Genes Dev. 33, 620-625 (2019).

29

Yao, T. et al. Structural foundation of the crosstalk between histone H2B monoubiquitation and the methylation of 79 H3 lysine on the nucleosome. Cell Res. 29, 330-333 (2019).

30

Poepsel, S., Kasinath, V. & Nogales, E. Cryo-EM buildings of PRC2 are concurrently concerned with two functionally distinct nucleosomes. Nat. Struct. Mol. Biol. 25, 154-162 (2018).

31.

Dyer, P. N. et al. Reconstitution of nucleosomal particles from recombinant histones and DNA. Enzymol strategies. 375, 23-44 (2004).

32

Morgan, M.T. et al. Structural foundation of histone H2B ubiquitination by the SAGA DUB module. Science 351, 725-728 (2016).

33

Kastner, B. et al. GraFix: pattern preparation for single particle electron cryomicroscopy. Nat. Strategies 5, 53-55 (2008).

34

Grant, T. & Grigorieff, N. Measurement of optimum publicity for single-particle cryo-EM with assistance from a 2.6 Å reconstruction of VP6 rotavirus. eLife Four, e06980 (2015).

35

Zheng, S. Q. et al. MotionCor2: Anisotropic correction of beam-induced movement to enhance cryo-electron microscopy. Nat. Strategies 14, 331-332 (2017).

36

Zhang, Okay. Gctf: Actual-time willpower and correction by the FCT. J. Struct. Biol. 193, 1-12 (2016).

37

Zivanov, J. et al. New instruments for the automated willpower of the excessive decision cryo-EM construction in RELION-Three. eLife 7, e42166 (2018).

38

Bai, X.C., Rajendra E., Yang G., Shi, Y. and Scheres, S. H. W. Sampling of the conformational house of the catalytic subunit of human γ-secretase. eLife Four, e11182 (2015).

39

Scheres, S. H. W. and Chen, S. Prevention of overfitting within the willpower of cryo-EM Nat construction. Strategies 9, 853-854 (2012).

40

Kucukelbir, A., Sigworth, F.J. and Tagare, H.D. Quantify the native decision of cryo-EM density maps. Nat. Strategies 11, 63-65 (2014).

41

Pettersen, E.F. et al. UCSF Chimera – a visualization system for exploratory analysis and evaluation. J. Comput. Chem. 25, 1605-1612 (2004).

42

Emsley, P., Lohkamp, ​​B., Scott, W. G. and Cowtan, Okay. Traits and improvement of Coot. Acta Crystallogr. D 66, 486-501 (2010).

43

Adams, P.D. et al. PHENIX: a whole system based mostly on Python for an answer with a macromolecular construction. Acta Crystallogr. D 66, 213-221 (2010).

Leave a Reply

Your email address will not be published. Required fields are marked *