Formaldehyde-Induced Histone Modifications in Vitro

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• 作者：Kun Lu ; Gunnar Boysen ; Lina Gao ; Leonard B. Collins ; James A. Swenberg
• 刊名：Chemical Research in Toxicology
• 出版年：2008
• 出版时间：August 2008
• 年：2008
• 卷：21
• 期：8
• 页码：1586-1593
• 全文大小：372K
• 年卷期：v.21,no.8(August 2008)
• ISSN：1520-5010

文摘

Numerous experiments have demonstrated the genotoxic and mutagenic effects of formaldehyde, including DNA−protein cross-links (DPC). Histone was reported to be involved in the formation of DPC in which the ε-amino groups of lysine and exocyclic amino groups of DNA were thought to be cross-linked through multiple step reactions. Using mass spectrometry, the N-terminus of histone and lysine residues located in both the histone N-terminal tail and the globular fold domain were identified as binding sites for formaldehyde in the current study. The observation that only lysine residues without post-translational modification (PTM) can be attacked by formaldehyde indicates that PTM blocks the reaction between lysine and formaldehyde. Additionally, we found that formaldehyde-induced Schiff bases on lysine residues could inhibit the formation of PTM on histone, raising the possibility that formaldehyde might alter epigenetic regulation.