AI Article Synopsis
- Over the last ten years, researchers have found various histone acyl post-translational modifications (acyl-PTMs), but their functions are still being explored.
- The study uses high-resolution mass spectrometry to accurately measure eight acyl-PTMs both in living organisms and through enzymatic tests, finding that specific histone acetyltransferases (HATs) work better with short-chain acyl-CoAs than larger ones.
- The research shows a strong correlation between acyl-CoA availability and acyl-PTM levels, indicating that both enzymatic actions and non-enzymatic processes influence the abundance of these histone modifications.
Article Abstract
Over the last decade, numerous histone acyl post-translational modifications (acyl-PTMs) have been discovered, of which the functional significance is still under intense study. Here, we use high-resolution mass spectrometry to accurately quantify eight acyl-PTMs in vivo and after in vitro enzymatic assays. We assess the ability of seven histone acetyltransferases (HATs) to catalyze acylations on histones in vitro using short-chain acyl-CoA donors, proving that they are less efficient towards larger acyl-CoAs. We also observe that acyl-CoAs can acylate histones through non-enzymatic mechanisms. Using integrated metabolomic and proteomic approaches, we achieve high correlation (R > 0.99) between the abundance of acyl-CoAs and their corresponding acyl-PTMs. Moreover, we observe a dose-dependent increase in histone acyl-PTM abundances in response to acyl-CoA supplementation in in nucleo reactions. This study represents a comprehensive profiling of scarcely investigated low-abundance histone marks, revealing that concentrations of acyl-CoAs affect histone acyl-PTM abundances by both enzymatic and non-enzymatic mechanisms.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5656686 | PMC |
| http://dx.doi.org/10.1038/s41467-017-01384-9 | DOI Listing |
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