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Methylation of p53 protein by KMT7/SET7 is the first reported KMT-mediated methylation occasion on a non-histone protein 18 Since that discovery, a number of KMTs, in addition to KDM1A, have been identified as p53 regulators that methylate or demethylate p53 protein, making p53 the most extensively studied non-histone protein present process lysine methylation 4 , 13 , sixteen , 18 , 162 Right here we use p53 as a model to debate the capabilities of lysine methylation of non-histone proteins.
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This household incorporates just one protein, SET7/9, which mono-methylates histone at H3K4 ninety two KMT7 was found to methylate, in addition to histone, numerous non-histone proteins, together with p53, [solicitor news](http://git.baige.me/efrainwinn043) DNA methyltransferase 1 (DNMT1), estrogen receptor alpha (ERα), nuclear issue kappaB (NFκB), and parts of the TATA binding protein (TBP) complex, TBP-associated components TAF10 and TAF7 ninety three The consensus recognition sequence in substrates for SET7-mediated lysine methylation, Ok/R-S/T-K (goal lysine is daring), is also acknowledged by the H3K4 demethylase KDM1A/LSD1, which is able to removing the methyl mark on most of those substrates 17 , 94 Subsequently KMT7/KDM1A has emerged as a traditional mannequin for dynamic lysine methylation of both histone and non-histone proteins.
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