Cells, Vol. 6, Pages 34: Post-Translational Modification of Human Histone by Wide Tolerance of Acetylation

Cells, Vol. 6, Pages 34: Post-Translational Modification of Human Histone by Wide Tolerance of Acetylation

Cells doi: 10.3390/cells6040034

Authors: Cuiling Li Han-Pil Choi Xiaoyue Wang Fei Wu Xinjun Chen Xin Lü Ruirui Jing Hoon Ryu Xingyuan Wang Kazem Azadzoi Jing-Hua Yang

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.

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