Genetically Encoded Photoaffinity Histone Marks

Posttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analog...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the American Chemical Society 2017-05, Vol.139 (19), p.6522-6525
Main Authors: Xie, Xiao, Li, Xiao-Meng, Qin, Fangfei, Lin, Jianwei, Zhang, Gong, Zhao, Jingyi, Bao, Xiucong, Zhu, Rongfeng, Song, Haiping, Li, Xiang David, Chen, Peng R
Format: Article
Language:English
Subjects:
Genetic Code
Histones - chemistry
Histones - genetics
Histones - metabolism
Lysine - analogs & derivatives
Lysine - chemistry
Lysine - metabolism
Molecular Conformation
Photoaffinity Labels - chemistry
Photoaffinity Labels - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Posttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analogue that can be genetically and site-specifically incorporated into histone proteins. This, in conjunction with the genetically encoded photo-lysine as a “control probe”, enables the capture and identification of enzymatic machinery and/or effector proteins for histone lysine crotonylation.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.7b01431