%0 Journal Article %1 Ruthenburg07 %A Ruthenburg, Alexander J %A Allis, C David %A Wysocka, Joanna %D 2007 %J Mol. Cell %K Amino_Acid_Sequence Animals Epigenesis,_Genetic Genes,_Developmental Histones,_chemistry/metabolism Homeodomain_Proteins,_chemistry/metabolism Humans Lysine,_metabolism Methylation Molecular_Sequence_Data %N 1 %P 15-30 %R 10.1016/j.molcel.2006.12.014 %T Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark. %U http://dx.doi.org/10.1016/j.molcel.2006.12.014 %V 25 %X Cells employ elaborate mechanisms to introduce structural and chemical variation into chromatin. Here, we focus on one such element of variation: methylation of lysine 4 in histone H3 (H3K4). We assess a growing body of literature, including treatment of how the mark is established, the patterns of methylation, and the functional consequences of this epigenetic signature. We discuss structural aspects of the H3K4 methyl recognition by the downstream effectors and propose a distinction between sequence-specific recruitment mechanisms and stabilization on chromatin through methyl-lysine recognition. Finally, we hypothesize how the unique properties of the polyvalent chromatin fiber and associated effectors may amplify small differences in methyl-lysine recognition, simultaneously allowing for a dynamic chromatin architecture.

@article{Ruthenburg07, abstract = {Cells employ elaborate mechanisms to introduce structural and chemical variation into chromatin. Here, we focus on one such element of variation: methylation of lysine 4 in histone H3 (H3K4). We assess a growing body of literature, including treatment of how the mark is established, the patterns of methylation, and the functional consequences of this epigenetic signature. We discuss structural aspects of the H3K4 methyl recognition by the downstream effectors and propose a distinction between sequence-specific recruitment mechanisms and stabilization on chromatin through methyl-lysine recognition. Finally, we hypothesize how the unique properties of the polyvalent chromatin fiber and associated effectors may amplify small differences in methyl-lysine recognition, simultaneously allowing for a dynamic chromatin architecture.}, added-at = {2010-01-26T20:35:53.000+0100}, author = {Ruthenburg, Alexander J and Allis, C David and Wysocka, Joanna}, biburl = {https://www.bibsonomy.org/bibtex/24df5d5f58ab8d67122f63c52a3eb5774/denilw}, doi = {10.1016/j.molcel.2006.12.014}, file = {article:../Histone modifications/Methylation of Lysine 4 on Histone H3%3A Intricacy of Writing and Reading a Single Epigenetic Mark.pdf:pdf}, institution = {Laboratory of Chromatin Biology, The Rockefeller University, New York, NY 10021, USA.}, interhash = {b6de513983c38f472d02626f134c4392}, intrahash = {4df5d5f58ab8d67122f63c52a3eb5774}, journal = {Mol. Cell}, keywords = {Amino_Acid_Sequence Animals Epigenesis,_Genetic Genes,_Developmental Histones,_chemistry/metabolism Homeodomain_Proteins,_chemistry/metabolism Humans Lysine,_metabolism Methylation Molecular_Sequence_Data}, month = Jan, number = 1, owner = {denilw}, pages = {15-30}, pii = {S1097-2765(06)00872-0}, pmid = {17218268}, timestamp = {2010-01-26T20:36:03.000+0100}, title = {Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark.}, url = {http://dx.doi.org/10.1016/j.molcel.2006.12.014}, volume = 25, year = 2007 }