Expanding the Reader Landscape of Histone Acylation

Abid Khan; Joseph B Bridgers; Brian D Strahl

doi:10.1016/j.str.2017.03.010

Expanding the Reader Landscape of Histone Acylation

Structure. 2017 Apr 4;25(4):571-573. doi: 10.1016/j.str.2017.03.010.

Authors

Abid Khan¹, Joseph B Bridgers¹, Brian D Strahl²

Affiliations

¹ Department of Biochemistry and Biophysics, The University of North Carolina, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
² Department of Biochemistry and Biophysics, The University of North Carolina, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA. Electronic address: [email protected].

Abstract

In this issue of Structure,Klein et al. (2017) expand our understanding of what reader domains bind to by showing that MORF, a double PHD domain containing lysine acetyltransferase, is a preferential reader of histone lysine acylation.

Publication types

Comment

MeSH terms

Acylation
Histone Acetyltransferases / chemistry
Histones / chemistry*
Lysine*

Substances

Histones
Histone Acetyltransferases
Lysine

Abstract

Publication types

MeSH terms

Substances

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