Histone H2AX Y142 phosphorylation is a low abundance modification

Hatimy, Abubakar A, Browne, Martin J G, Flaus, Andrew and Sweet, Steve M M (2015) Histone H2AX Y142 phosphorylation is a low abundance modification. International Journal of Mass Spectrometry, 391. pp. 139-145. ISSN 1387-3806

[img] PDF - Accepted Version
Restricted to SRO admin only until November 2017.

Download (923kB)
[img] PDF - Supplemental Material
Restricted to SRO admin only until November 2017.

Download (54kB)
[img] Microsoft Excel - Supplemental Material
Restricted to SRO admin only until November 2017.

Download (42kB)

Abstract

We employ targeted mass spectrometry to compare the levels of H2AX S139 phosphorylation (γH2AX) and Y142 phosphorylation. We use synthetic peptides to facilitate MS optimisation and estimate relative detection efficiencies for the different modifications. Despite phosphopeptide enrichment from large amounts of starting material, we are unable to detect endogenous H2AX Y142 phosphorylation, indicating that it is present in low abundance (<1%). We also calculate the relative levels of H2AX compared to other H2A isoforms and quantify the proportion of H2AX that is phosphorylated on S139 (γH2AX) after ionising radiation.

Item Type: Article
Schools and Departments: School of Life Sciences > Sussex Centre for Genome Damage and Stability
Depositing User: Steve Sweet
Date Deposited: 20 Jan 2016 07:43
Last Modified: 15 Aug 2017 07:07
URI: http://sro.sussex.ac.uk/id/eprint/59324

View download statistics for this item

📧 Request an update