A charge-suppressing strategy for probing protein methylation

Methylation of arginine and lysine (RK) residues play essential roles in epigenetics and the regulation of gene expression. However, research in this area is often hindered by the lack of effective tools for probing the protein methylation. Here, we present an antibody-free strategy to capture prote...

Full description

Saved in:
Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2016-01, Vol.52 (31), p.5474-5477
Main Authors: Ning, Zhibin, Star, Alexandra Therese, Mierzwa, Anna, Lanouette, Sylvain, Mayne, Janice, Couture, Jean-Francois, Figeys, Daniel
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Arginine - analysis
Chromatography, Ion Exchange
Exchange
Gene expression
Lysine
Lysine - analysis
Mass Spectrometry
Methylation
Peptides
Peptides - chemistry
Proteins
Proteins - chemistry
Residues
Strategy
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:Methylation of arginine and lysine (RK) residues play essential roles in epigenetics and the regulation of gene expression. However, research in this area is often hindered by the lack of effective tools for probing the protein methylation. Here, we present an antibody-free strategy to capture protein methylation on RK residues by using chemical reactions to eliminate the charges on un-modified RK residues and peptide N-termini. Peptides containing methylated RK residues remain positively charged and are then enriched by strong cation exchange chromatography, followed by high-resolution mass spectrometry identification.
ISSN:1359-7345
1364-548X
DOI:10.1039/c6cc00814c