A nucleosome consists of two copies of the four histone proteins H2A, H2B, H3, and H4, those of which package DNA in the state of chromosome.  A major mechanism regulating the accessibility of chromatin for the purposes of transcription, replication, and DNA repair is through post-translational modification (PTM) of histones.  One of the most common PTMs is acetylation, and aberrant regulation of specific lysine acetylation could be correlated with human diseases.  Gcn5, one of the histone acetyltransferases, has been reported that catalyzes acetylation at multiple lysines.  In this study, we demonstrate mass spectrometry is capable of quantitatively monitoring acetylation at multiple lysine residues on histone H3 and establish an enzymatic kinetic model interpreting the sequence of lysine acetylation (K14 > K9 and K23 > K18) by Gcn5. The other goal of this research is to show this reliable analytical platform can be suitable for in vitro and in vivo studies without antibody selection and extra labeling work.

Kinetic modeling of Gcn5-mediated lysine acetylation on Histone H3 by mass spectrometry

244th National Meeting (2012)

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