Total kinetic analysis reveals how combinatorial methylation patterns are established on lysines 27 and 36 of histone H3

We have developed a targeted method to quantify all combinations of methylation on an H3 peptide containing lysines 27 and 36 (H3K27-K36). By using stable isotopes that separately label the histone backbone and its methylations, we tracked the rates of methylation and demethylation in myeloma cells...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2012-08, Vol.109 (34), p.13549-13554
Hauptverfasser:	Zheng, Yupeng, Sweet, Steve M. M, Popovic, Relja, Martinez-Garcia, Eva, Tipton, Jeremiah D, Thomas, Paul M, Licht, Jonathan D, Kelleher, Neil L
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Biochemistry - methods Biological Sciences Cell Line Cell lines Cells Chromatin Combinatorial Chemistry Techniques DNA methylation drugs Effective annual interest rates Enzyme kinetics Epigenetics Epigenomics Histone-Lysine N-Methyltransferase - chemistry Histone-Lysine N-Methyltransferase - genetics Histones Histones - chemistry Humans Isotopes Kinetics lysine Lysine - chemistry Mass Spectrometry - methods Mass spectroscopy Mathematical constants Methylation methyltransferases Methyltransferases - chemistry Molecules myeloma Proteins Repressor Proteins - chemistry Repressor Proteins - genetics stable isotopes
Online-Zugang:	Volltext
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