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Cells 2017, 6(4), 34;

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

Cancer Research Center, Shandong University School of Medicine, Jinan 250012, China
Departments of Surgery, Urology, Neurology and Proteomics Laboratory, VA Boston Healthcare System, Boston University School of Medicine, Boston, MA 02130, USA
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
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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

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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.

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