Recognition of the N-terminal histone H2A and H3 peptides by peptidylarginine deiminase IV.
Recognition of the N-terminal histone H2A and H3 peptides by peptidylarginine deiminase IV.
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DOI：
10.2174/092986609789055449
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发表时间：
2009-08
影响因子：
1.6
通讯作者：
Masatoshi Saiki;Mayumi Watase;Hironori Matsubayashi;Y. Hidaka
中科院分区：
文献类型：
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作者：
Masatoshi Saiki;Mayumi Watase;Hironori Matsubayashi;Y. Hidaka
肽精氨酸脱亚胺酶IV （PAD4）在多种蛋白质中催化精氨酸残基转化为瓜氨酸残基。特别是，PAD4对组蛋白亚基如H2A和H3的瓜氨酸化被认为与类风湿关节炎有关。然而，组蛋白H2A和H3的瓜氨酸化机制的细节尚不清楚。此外，n端乙酰化对组蛋白亚基在PAD4识别方面的影响尚未研究。为了进一步研究PAD4识别组蛋白H2A和H3亚基的机制，我们化学合成了一系列n端肽，并利用MALDI-TOF/MS鉴定了瓜氨酸化位点。组蛋白H2A的n端乙酰化对PAD4的体外识别没有显著影响，但H3肽的乙酰化对PAD4的体外识别有显著影响，导致Arg2残基上的瓜氨酸化为主。
Peptidylarginine deiminase IV (PAD4) catalyzes the conversion of an Arg residue to a citrulline residue in various proteins. In particular, citrullination of histone subunits, such as H2A and H3, by PAD4 is thought to be related to rheumatoid arthritis. However, the details of the citrullination mechanism of histone H2A and H3 are not yet well known. Moreover, the effects of N-terminal acetylation on histone subunits with respect to PAD4 recognition have not yet been studied. To further study the mechanism of PAD4 recognition of histone H2A and H3 subunits, a series of the N-terminal peptides was chemically synthesized and the citrullination sites were identified using MALDI-TOF/MS. N-terminal acetylation of histone H2A was not significant with respect to PAD4 recognition in vitro, but the acetylation of H3 peptide had a significant effect on PAD4 recognition in vitro, resulting in predominant citrullination at the Arg2 residue.