Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation

John Faissal Haddad; Yidai Yang; Yoh hei Takahashi; Monika Joshi; Nidhi Chaudhary; Ashley R. Woodfin; Aissa Benyoucef; Sylvain Yeung; Joseph S. Brunzelle; Georgios Skiniotis; Marjorie Brand; Ali Shilatifard; Jean François Couture

doi:10.1016/j.str.2018.08.004

Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation

John Faissal Haddad, Yidai Yang, Yoh hei Takahashi, Monika Joshi, Nidhi Chaudhary, Ashley R. Woodfin, Aissa Benyoucef, Sylvain Yeung, Joseph S. Brunzelle, Georgios Skiniotis, Marjorie Brand, Ali Shilatifard, Jean François Couture^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Haddad et al. highlight that several interactions help in the formation of the Ash2L/Dpy-30 complex. The study also demonstrates that Dpy-30 couples its marginal ability to allosterically regulate KMT2 enzymes and chromatin recruitment activity to control epigenetic signaling in vivo.

Original language	English (US)
Pages (from-to)	1594-1603.e4
Journal	Structure
Volume	26
Issue number	12
DOIs	https://doi.org/10.1016/j.str.2018.08.004
State	Published - Dec 4 2018

Funding

J.F.H. received a scholarship from Ontario Graduate studies. J.-F.C. acknowledges a Canada Research Chair in structural biology and epigenetics and an Early Research Award from MEDI. J.-F.C. is supported by a Canadian Institutes of Health Research (CIHR) grant ( MOP-136816 and PJT-148533 ). This study was also supported by grants from CIHR to M.B. ( MOP-89834 ), NIH to A.S. ( R35CA197569 ). This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science user facility operated for the DOE Office of Science by Argonne National Laboratory under contract no. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (grant 085P1000817 ).

Keywords

H3K4 methylation
KMT2
MLL
SET1/COMPASS
allosteric regulation
chromatin
crystallography
histone
lysine methylation

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Access to Document

10.1016/j.str.2018.08.004

Cite this

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title = "Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation",

abstract = "Haddad et al. highlight that several interactions help in the formation of the Ash2L/Dpy-30 complex. The study also demonstrates that Dpy-30 couples its marginal ability to allosterically regulate KMT2 enzymes and chromatin recruitment activity to control epigenetic signaling in vivo.",

keywords = "H3K4 methylation, KMT2, MLL, SET1/COMPASS, allosteric regulation, chromatin, crystallography, histone, lysine methylation",

author = "Haddad, {John Faissal} and Yidai Yang and Takahashi, {Yoh hei} and Monika Joshi and Nidhi Chaudhary and Woodfin, {Ashley R.} and Aissa Benyoucef and Sylvain Yeung and Brunzelle, {Joseph S.} and Georgios Skiniotis and Marjorie Brand and Ali Shilatifard and Couture, {Jean Fran{\c c}ois}",

note = "Funding Information: J.F.H. received a scholarship from Ontario Graduate studies. J.-F.C. acknowledges a Canada Research Chair in structural biology and epigenetics and an Early Research Award from MEDI. J.-F.C. is supported by a Canadian Institutes of Health Research (CIHR) grant ( MOP-136816 and PJT-148533 ). This study was also supported by grants from CIHR to M.B. ( MOP-89834 ), NIH to A.S. ( R35CA197569 ). This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science user facility operated for the DOE Office of Science by Argonne National Laboratory under contract no. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (grant 085P1000817 ). Publisher Copyright: {\textcopyright} 2018 Elsevier Ltd",

year = "2018",

month = dec,

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doi = "10.1016/j.str.2018.08.004",

language = "English (US)",

volume = "26",

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AU - Haddad, John Faissal

AU - Yang, Yidai

AU - Takahashi, Yoh hei

AU - Joshi, Monika

AU - Chaudhary, Nidhi

AU - Woodfin, Ashley R.

AU - Benyoucef, Aissa

AU - Yeung, Sylvain

AU - Brunzelle, Joseph S.

AU - Skiniotis, Georgios

AU - Brand, Marjorie

AU - Shilatifard, Ali

AU - Couture, Jean François

N1 - Funding Information: J.F.H. received a scholarship from Ontario Graduate studies. J.-F.C. acknowledges a Canada Research Chair in structural biology and epigenetics and an Early Research Award from MEDI. J.-F.C. is supported by a Canadian Institutes of Health Research (CIHR) grant ( MOP-136816 and PJT-148533 ). This study was also supported by grants from CIHR to M.B. ( MOP-89834 ), NIH to A.S. ( R35CA197569 ). This research used resources of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science user facility operated for the DOE Office of Science by Argonne National Laboratory under contract no. DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (grant 085P1000817 ). Publisher Copyright: © 2018 Elsevier Ltd

PY - 2018/12/4

Y1 - 2018/12/4

N2 - Haddad et al. highlight that several interactions help in the formation of the Ash2L/Dpy-30 complex. The study also demonstrates that Dpy-30 couples its marginal ability to allosterically regulate KMT2 enzymes and chromatin recruitment activity to control epigenetic signaling in vivo.

AB - Haddad et al. highlight that several interactions help in the formation of the Ash2L/Dpy-30 complex. The study also demonstrates that Dpy-30 couples its marginal ability to allosterically regulate KMT2 enzymes and chromatin recruitment activity to control epigenetic signaling in vivo.

KW - H3K4 methylation

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KW - MLL

KW - SET1/COMPASS

KW - allosteric regulation

KW - chromatin

KW - crystallography

KW - histone

KW - lysine methylation

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Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation

Abstract

Funding

Keywords

ASJC Scopus subject areas

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Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30

Cite this

Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation

Abstract

Funding

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

Crystal structure of human Ash2L (SPRY domain and SDI motif) in complex with full length DPY-30

Cite this