By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Proteins. According to news reporting out of Beijing, People's Republic of China, by NewsRx editors, research stated, "The origin of eukaryotic histone modification enzymes still remains obscure. Prototypic KMT4/Dot1 from Archaea targets chromatin proteins (Sul7d and Cren7) and shows increased activity on Sul7d, but not Cren7, in the presence of DNA."
Our news journalists obtained a quote from the research from China Agricultural University, "Promiscuous aKMT4 could be regulated by chromatin environment. This study supports the prokaryotic origin model of eukaryotic histone methyltransferases and sheds light on chromatin dynamics in Archaea. Histone methylation is one of the major epigenetic modifications even in early diverging unicellular eukaryotes. We show that a widespread lysine methyltransferase from Archaea (aKMT4), bears striking structural and functional resemblance to the core of distantly related eukaryotic KMT4/Dot1. aKMT4 methylates a set of various proteins, including the chromatin proteins Sul7d and Cren7, and RNA exosome components. Csl4-and Rrp4-exosome complexes are methylated in different patterns. aKMT4 can self-methylate intramolecularly and compete with other proteins for the methyl group. Automethylation is inhibited by suitable substrates or DNA in a concentration-dependent manner. The automethylated enzyme shows relatively compromised activity. aKMT4-8A mutant with abrogated automethylation shows a more than 150% increase in methylation of substrates, suggesting a possible mechanism to regulate methyltransferase activity. More interestingly, methylation of Sul7d, but not Cren7, by aKMT4 is significantly enhanced by DNA. MS/MS and kinetic analysis further suggest that aKMT4 methylates Sul7d in the chromatin context. These data provide a clue to the possible regulation of aKMT4 activity by the local chromatin environment, albeit as a promiscuous enzyme required for extensive and variegated lysine methylation in Sulfolobus."
According to the news editors, the research concluded: "This study supports the prokaryotic origin model of eukaryotic histone modification enzymes and sheds light on regulation of archaeal chromatin."
For more information on this research see: A prototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns. Journal of Biological Chemistry, 2013;288(19):13728-40. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
Our news journalists report that additional information may be obtained by contacting Y. Niu, State Key Laboratory of Agro-Biotechnology and Ministry of Agriculture Key Laboratory of Soil Microbiology, College of Biological Sciences, China Agricultural University, Beijing 100193, People's Taiwan. Additional authors for this research include Y. Xia, S. Wang, J. Li, C. Niu, X. Li, Y. Zhao, H. Xiong, Z. Li, H. Lou and Q. Cao (see also Proteins).
Keywords for this news article include: Asia, Lysine, Beijing, Genetics, Histones, Peptides, Chromatin, Nucleoproteins, Basic Amino Acids, Methyltransferases, Diamino Amino Acids, Enzymes and Coenzymes, Essential Amino Acids, People's Republic of China, One Carbon Group Transferases.
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