Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3.

Research output: Contribution to journal › Journal article › Research › peer-review

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Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3. / Lindroth, Anders M; Shultis, David; Jasencakova, Zusana; Fuchs, Jörg; Johnson, Lianna; Schubert, Daniel; Patnaik, Debasis; Pradhan, Sriharsa; Goodrich, Justin; Schubert, Ingo; Jenuwein, Thomas; Khorasanizadeh, Sepideh; Jacobsen, Steven E.

In: EMBO Journal, Vol. 23, No. 21, 2004, p. 4286-96.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Lindroth, AM, Shultis, D, Jasencakova, Z, Fuchs, J, Johnson, L, Schubert, D, Patnaik, D, Pradhan, S, Goodrich, J, Schubert, I, Jenuwein, T, Khorasanizadeh, S & Jacobsen, SE 2004, 'Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3.', EMBO Journal, vol. 23, no. 21, pp. 4286-96. https://doi.org/10.1038/sj.emboj.7600430

APA

Lindroth, A. M., Shultis, D., Jasencakova, Z., Fuchs, J., Johnson, L., Schubert, D., Patnaik, D., Pradhan, S., Goodrich, J., Schubert, I., Jenuwein, T., Khorasanizadeh, S., & Jacobsen, S. E. (2004). Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3. EMBO Journal, 23(21), 4286-96. https://doi.org/10.1038/sj.emboj.7600430

Vancouver

Lindroth AM, Shultis D, Jasencakova Z, Fuchs J, Johnson L, Schubert D et al. Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3. EMBO Journal. 2004;23(21):4286-96. https://doi.org/10.1038/sj.emboj.7600430

Author

Lindroth, Anders M ; Shultis, David ; Jasencakova, Zusana ; Fuchs, Jörg ; Johnson, Lianna ; Schubert, Daniel ; Patnaik, Debasis ; Pradhan, Sriharsa ; Goodrich, Justin ; Schubert, Ingo ; Jenuwein, Thomas ; Khorasanizadeh, Sepideh ; Jacobsen, Steven E. / Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3. In: EMBO Journal. 2004 ; Vol. 23, No. 21. pp. 4286-96.

Bibtex

@article{52359450518b11dd8d9f000ea68e967b,
title = "Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3.",
abstract = "Both DNA methylation and post-translational histone modifications contribute to gene silencing, but the mechanistic relationship between these epigenetic marks is unclear. Mutations in two Arabidopsis genes, the KRYPTONITE (KYP) histone H3 lysine 9 (H3K9) methyltransferase and the CHROMOMETHYLASE3 (CMT3) DNA methyltransferase, cause a reduction of CNG DNA methylation, suggesting that H3K9 methylation controls CNG DNA methylation. Here we show that the chromodomain of CMT3 can directly interact with the N-terminal tail of histone H3, but only when it is simultaneously methylated at both the H3K9 and H3K27 positions. Furthermore, using chromatin immunoprecipitation analysis and immunohistolocalization experiments, we found that H3K27 methylation colocalizes with H3K9 methylation at CMT3-controlled loci. The H3K27 methylation present at heterochromatin was not affected by mutations in KYP or in several Arabidopsis PcG related genes including the Enhancer of Zeste homologs, suggesting that a novel pathway controls heterochromatic H3K27 methylation. Our results suggest a model in which H3K9 methylation by KYP, and H3K27 methylation by an unknown enzyme provide a combinatorial histone code for the recruitment of CMT3 to silent loci.",
author = "Lindroth, {Anders M} and David Shultis and Zusana Jasencakova and J{\"o}rg Fuchs and Lianna Johnson and Daniel Schubert and Debasis Patnaik and Sriharsa Pradhan and Justin Goodrich and Ingo Schubert and Thomas Jenuwein and Sepideh Khorasanizadeh and Jacobsen, {Steven E}",
note = "Keywords: Amino Acid Sequence; Animals; Arabidopsis; Arabidopsis Proteins; Chromosomal Proteins, Non-Histone; Epigenesis, Genetic; Gene Expression Regulation, Plant; Gene Silencing; Histone-Lysine N-Methyltransferase; Histones; Humans; Lysine; Methylation; Methyltransferases; Models, Genetic; Molecular Sequence Data; Protein Binding; Sequence Alignment; Site-Specific DNA Methyltransferase (Cytosine-Specific)",
year = "2004",
doi = "10.1038/sj.emboj.7600430",
language = "English",
volume = "23",
pages = "4286--96",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "21",

}

RIS

TY - JOUR

T1 - Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3.

AU - Lindroth, Anders M

AU - Shultis, David

AU - Jasencakova, Zusana

AU - Fuchs, Jörg

AU - Johnson, Lianna

AU - Schubert, Daniel

AU - Patnaik, Debasis

AU - Pradhan, Sriharsa

AU - Goodrich, Justin

AU - Schubert, Ingo

AU - Jenuwein, Thomas

AU - Khorasanizadeh, Sepideh

AU - Jacobsen, Steven E

N1 - Keywords: Amino Acid Sequence; Animals; Arabidopsis; Arabidopsis Proteins; Chromosomal Proteins, Non-Histone; Epigenesis, Genetic; Gene Expression Regulation, Plant; Gene Silencing; Histone-Lysine N-Methyltransferase; Histones; Humans; Lysine; Methylation; Methyltransferases; Models, Genetic; Molecular Sequence Data; Protein Binding; Sequence Alignment; Site-Specific DNA Methyltransferase (Cytosine-Specific)

PY - 2004

Y1 - 2004

N2 - Both DNA methylation and post-translational histone modifications contribute to gene silencing, but the mechanistic relationship between these epigenetic marks is unclear. Mutations in two Arabidopsis genes, the KRYPTONITE (KYP) histone H3 lysine 9 (H3K9) methyltransferase and the CHROMOMETHYLASE3 (CMT3) DNA methyltransferase, cause a reduction of CNG DNA methylation, suggesting that H3K9 methylation controls CNG DNA methylation. Here we show that the chromodomain of CMT3 can directly interact with the N-terminal tail of histone H3, but only when it is simultaneously methylated at both the H3K9 and H3K27 positions. Furthermore, using chromatin immunoprecipitation analysis and immunohistolocalization experiments, we found that H3K27 methylation colocalizes with H3K9 methylation at CMT3-controlled loci. The H3K27 methylation present at heterochromatin was not affected by mutations in KYP or in several Arabidopsis PcG related genes including the Enhancer of Zeste homologs, suggesting that a novel pathway controls heterochromatic H3K27 methylation. Our results suggest a model in which H3K9 methylation by KYP, and H3K27 methylation by an unknown enzyme provide a combinatorial histone code for the recruitment of CMT3 to silent loci.

AB - Both DNA methylation and post-translational histone modifications contribute to gene silencing, but the mechanistic relationship between these epigenetic marks is unclear. Mutations in two Arabidopsis genes, the KRYPTONITE (KYP) histone H3 lysine 9 (H3K9) methyltransferase and the CHROMOMETHYLASE3 (CMT3) DNA methyltransferase, cause a reduction of CNG DNA methylation, suggesting that H3K9 methylation controls CNG DNA methylation. Here we show that the chromodomain of CMT3 can directly interact with the N-terminal tail of histone H3, but only when it is simultaneously methylated at both the H3K9 and H3K27 positions. Furthermore, using chromatin immunoprecipitation analysis and immunohistolocalization experiments, we found that H3K27 methylation colocalizes with H3K9 methylation at CMT3-controlled loci. The H3K27 methylation present at heterochromatin was not affected by mutations in KYP or in several Arabidopsis PcG related genes including the Enhancer of Zeste homologs, suggesting that a novel pathway controls heterochromatic H3K27 methylation. Our results suggest a model in which H3K9 methylation by KYP, and H3K27 methylation by an unknown enzyme provide a combinatorial histone code for the recruitment of CMT3 to silent loci.

U2 - 10.1038/sj.emboj.7600430

DO - 10.1038/sj.emboj.7600430

M3 - Journal article

C2 - 15457214

VL - 23

SP - 4286

EP - 4296

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 21

ER -

ID: 5014103