Guiding COMPASS: Dpy-30 Positions SET1/MLL Epigenetic Signaling

David Dilworth; Cheryl H Arrowsmith

doi:10.1016/j.str.2018.11.010

Guiding COMPASS: Dpy-30 Positions SET1/MLL Epigenetic Signaling

Structure. 2018 Dec 4;26(12):1567-1570. doi: 10.1016/j.str.2018.11.010.

Authors

David Dilworth¹, Cheryl H Arrowsmith²

Affiliations

¹ Structural Genomics Consortium, University of Toronto, Toronto, ON, Canada.
² Structural Genomics Consortium, University of Toronto, Toronto, ON, Canada; Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, ON, Canada. Electronic address: [email protected].

PMID: 30517884
DOI: 10.1016/j.str.2018.11.010

Abstract

In this issue of Structure, Haddad et al. (2018) solve the high-resolution trimeric crystal structure of human COMPASS-like components Dpy-30 and Ash2L (2:1) to unravel an uncharacterized interaction surface required for competent H3K4 methylation in cells and clarify Dpy-30's role in the allosteric regulation of KMT2 enzymes.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

DNA-Binding Proteins
Epigenesis, Genetic
Histone-Lysine N-Methyltransferase*
Histones*
Humans
Methylation
Myeloid-Lymphoid Leukemia Protein
Nuclear Proteins
Protein Processing, Post-Translational
Transcription Factors

Substances

ASH2L protein, human
DNA-Binding Proteins
Histones
KMT2A protein, human
Nuclear Proteins
Transcription Factors
Myeloid-Lymphoid Leukemia Protein
Histone-Lysine N-Methyltransferase

Abstract

Publication types

MeSH terms

Substances

Grants and funding