Next Article in Journal
Oxidative Stress-Responsive Apoptosis Inducing Protein (ORAIP) Plays a Critical Role in High Glucose-Induced Apoptosis in Rat Cardiac Myocytes and Murine Pancreatic β-Cells
Previous Article in Journal
A Perspective on the Experimental Techniques for Studying Lamins
Article Menu

Export Article

Open AccessFeature PaperArticle
Cells 2017, 6(4), 34; doi:10.3390/cells6040034

Post-Translational Modification of Human Histone by Wide Tolerance of Acetylation

1
Cancer Research Center, Shandong University School of Medicine, Jinan 250012, China
2
Departments of Surgery, Urology, Neurology and Proteomics Laboratory, VA Boston Healthcare System, Boston University School of Medicine, Boston, MA 02130, USA
3
Department of Management Science, Shandong University School of Management, Jinan 250100, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Received: 13 September 2017 / Revised: 3 October 2017 / Accepted: 4 October 2017 / Published: 12 October 2017
View Full-Text   |   Download PDF [860 KB, uploaded 16 October 2017]   |  

Abstract

Histone acetylation adds an acetyl group on the lysine residue commonly found within the N-terminal tail protruding from the histone core of the nucleosome, and is important for chromosome structure and function in gene transcription and chromatin remodeling. Acetylation may also occur on other residues additional to lysine, but have not been thoroughly investigated at the proteomics level. Here we report a wide tolerance acetylation study mimicking the addition of 42 ± 0.5 Da delta mass modification on undefined amino acid residues of histones by shotgun proteomics using liquid chromatography–tandem mass spectrometry. A multi-blind spectral alignment algorithm with a wide peptide tolerance revealed frequent occurrence of 42 ± 0.5 Da modifications at lysine (K), serine (S) and threonine (T) residues in human histones from kidney tissues. Precision delta mass analysis identified acetylation (42.011 ± 0.004 Da) and trimethylation (42.047 ± 0.002 Da) modifications within the delta mass range. A specific antibody was produced to validate the acetylated T22 of human histone H3 (H3T22ac) by immune assays. Thus, we demonstrated that the wide tolerance acetylation approach identified histone acetylation as well as modification variants commonly associated with acetylation at undefined residues additional to lysine. View Full-Text
Keywords: post-translational modifications; mass spectrometry; human histones; acetylation; proteomics post-translational modifications; mass spectrometry; human histones; acetylation; proteomics
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Li, C.; Choi, H.-P.; Wang, X.; Wu, F.; Chen, X.; Lü, X.; Jing, R.; Ryu, H.; Wang, X.; Azadzoi, K.M.; Yang, J.-H. Post-Translational Modification of Human Histone by Wide Tolerance of Acetylation. Cells 2017, 6, 34.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Cells EISSN 2073-4409 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top