TY - JOUR
T1 - Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin
AU - Peters, Antoine H.F.M.
AU - Kubicek, Stefan
AU - Mechtler, Karl
AU - O'Sullivan, Roderick J.
AU - Derijck, Alwin A.H.A.
AU - Perez-Burgos, Laura
AU - Kohlmaier, Alexander
AU - Opravil, Susanne
AU - Tachibana, Makoto
AU - Shinkai, Yoichi
AU - Martens, Joost H.A.
AU - Jenuwein, Thomas
N1 - Funding Information: We are indebted to Judd Rice and David Allis for the synergies in characterizing the histone H3-K9 mono-di-tri-specific methylation antibodies. We thank Gunter Reuter and Stephen Jacobsen for allowing us to cite work prior to its publication. We particularly acknowledge Mathias Madalinski for peptide synthesis and Ines Steinmacher and Richard Imre for excellent technical assistance with mass spectrometry. Research in the laboratory of T.J. is supported by the IMP through Boehringer Ingelheim and by grants from the Vienna Economy Promotion Fund, the European Union (EU-network HPRN-CT 2000-00078), and the Austrian GEN-AU initiative which is financed by the Austrian Ministry of Education, Science and Culture.
PY - 2003/12
Y1 - 2003/12
N2 - Methylation of position-specific lysine residues in histone N termini is a central modification for regulating epigenetic transitions in chromatin. Each methylatable lysine residue can exist in a mono-, di-, or trimethylated state, thereby extending the indexing potential of this particular modification. Here, we examine all possible methylation states for histone H3 lysine 9 (H3-K9) and lysine 27 (H3-K27) in mammalian chromatin. Using highly specific antibodies together with quantitative mass spectrometry, we demonstrate that pericentric heterochromatin is selectively enriched for H3-K27 monomethylation and H3-K9 trimethylation. This heterochromatic methylation profile is dependent on the Suv39h histone methyltransferases (HMTases) but independent of the euchromatic G9a HMTase. In Suv39h double null cells, pericentric heterochromatin is converted to alternative methylation imprints and accumulates H3-K27 trimethylation and H3-K9 monomethylation. Our data underscore the selective presence of distinct histone lysine methylation states in partitioning chromosomal subdomains but also reveal a surprising plasticity in propagating methylation patterns in eukaryotic chromatin.
AB - Methylation of position-specific lysine residues in histone N termini is a central modification for regulating epigenetic transitions in chromatin. Each methylatable lysine residue can exist in a mono-, di-, or trimethylated state, thereby extending the indexing potential of this particular modification. Here, we examine all possible methylation states for histone H3 lysine 9 (H3-K9) and lysine 27 (H3-K27) in mammalian chromatin. Using highly specific antibodies together with quantitative mass spectrometry, we demonstrate that pericentric heterochromatin is selectively enriched for H3-K27 monomethylation and H3-K9 trimethylation. This heterochromatic methylation profile is dependent on the Suv39h histone methyltransferases (HMTases) but independent of the euchromatic G9a HMTase. In Suv39h double null cells, pericentric heterochromatin is converted to alternative methylation imprints and accumulates H3-K27 trimethylation and H3-K9 monomethylation. Our data underscore the selective presence of distinct histone lysine methylation states in partitioning chromosomal subdomains but also reveal a surprising plasticity in propagating methylation patterns in eukaryotic chromatin.
UR - http://www.scopus.com/inward/record.url?scp=9144268924&partnerID=8YFLogxK
U2 - https://doi.org/10.1016/S1097-2765(03)00477-5
DO - https://doi.org/10.1016/S1097-2765(03)00477-5
M3 - Article
C2 - 14690609
SN - 1097-2765
VL - 12
SP - 1577
EP - 1589
JO - Molecular Cell
JF - Molecular Cell
IS - 6
ER -