Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers

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Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. / Vermeulen, Michiel; Eberl, H Christian; Matarese, Filomena; Marks, Hendrik; Denissov, Sergei; Butter, Falk; Lee, Kenneth K; Olsen, Jesper Velgaard; Hyman, Anthony A; Stunnenberg, Henk G; Mann, Matthias.

In: Cell, Vol. 142, No. 6, 17.09.2010, p. 967-80.

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

Harvard

Vermeulen, M, Eberl, HC, Matarese, F, Marks, H, Denissov, S, Butter, F, Lee, KK, Olsen, JV, Hyman, AA, Stunnenberg, HG & Mann, M 2010, 'Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers', Cell, vol. 142, no. 6, pp. 967-80. https://doi.org/10.1016/j.cell.2010.08.020

APA

Vermeulen, M., Eberl, H. C., Matarese, F., Marks, H., Denissov, S., Butter, F., Lee, K. K., Olsen, J. V., Hyman, A. A., Stunnenberg, H. G., & Mann, M. (2010). Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. Cell, 142(6), 967-80. https://doi.org/10.1016/j.cell.2010.08.020

Vancouver

Vermeulen M, Eberl HC, Matarese F, Marks H, Denissov S, Butter F et al. Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. Cell. 2010 Sep 17;142(6):967-80. https://doi.org/10.1016/j.cell.2010.08.020

Author

Vermeulen, Michiel ; Eberl, H Christian ; Matarese, Filomena ; Marks, Hendrik ; Denissov, Sergei ; Butter, Falk ; Lee, Kenneth K ; Olsen, Jesper Velgaard ; Hyman, Anthony A ; Stunnenberg, Henk G ; Mann, Matthias. / Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. In: Cell. 2010 ; Vol. 142, No. 6. pp. 967-80.

Bibtex

@article{1b56f0885e7f4ac3aadf3b0cae44918d,
title = "Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers",
abstract = "Trimethyl-lysine (me3) modifications on histones are the most stable epigenetic marks and they control chromatin-mediated regulation of gene expression. Here, we determine proteins that bind these marks by high-accuracy, quantitative mass spectrometry. These chromatin {"}readers{"} are assigned to complexes by interaction proteomics of full-length BAC-GFP-tagged proteins. ChIP-Seq profiling identifies their genomic binding sites, revealing functional properties. Among the main findings, the human SAGA complex binds to H3K4me3 via a double Tudor-domain in the C terminus of Sgf29, and the PWWP domain is identified as a putative H3K36me3 binding motif. The ORC complex, including LRWD1, binds to the three most prominent transcriptional repressive lysine methylation sites. Our data reveal a highly adapted interplay between chromatin marks and their associated protein complexes. Reading specific trimethyl-lysine sites by specialized complexes appears to be a widespread mechanism to mediate gene expression.",
keywords = "Chromatin, Epigenesis, Genetic, Gene Expression Regulation, Genome-Wide Association Study, Hela Cells, Histone Acetyltransferases, Histone Code, Humans, Lysine, Mass Spectrometry, Methylation, Proteomics",
author = "Michiel Vermeulen and Eberl, {H Christian} and Filomena Matarese and Hendrik Marks and Sergei Denissov and Falk Butter and Lee, {Kenneth K} and Olsen, {Jesper Velgaard} and Hyman, {Anthony A} and Stunnenberg, {Henk G} and Matthias Mann",
note = "Copyright {\textcopyright} 2010 Elsevier Inc. All rights reserved.",
year = "2010",
month = sep,
day = "17",
doi = "10.1016/j.cell.2010.08.020",
language = "English",
volume = "142",
pages = "967--80",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "6",

}

RIS

TY - JOUR

T1 - Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers

AU - Vermeulen, Michiel

AU - Eberl, H Christian

AU - Matarese, Filomena

AU - Marks, Hendrik

AU - Denissov, Sergei

AU - Butter, Falk

AU - Lee, Kenneth K

AU - Olsen, Jesper Velgaard

AU - Hyman, Anthony A

AU - Stunnenberg, Henk G

AU - Mann, Matthias

N1 - Copyright © 2010 Elsevier Inc. All rights reserved.

PY - 2010/9/17

Y1 - 2010/9/17

N2 - Trimethyl-lysine (me3) modifications on histones are the most stable epigenetic marks and they control chromatin-mediated regulation of gene expression. Here, we determine proteins that bind these marks by high-accuracy, quantitative mass spectrometry. These chromatin "readers" are assigned to complexes by interaction proteomics of full-length BAC-GFP-tagged proteins. ChIP-Seq profiling identifies their genomic binding sites, revealing functional properties. Among the main findings, the human SAGA complex binds to H3K4me3 via a double Tudor-domain in the C terminus of Sgf29, and the PWWP domain is identified as a putative H3K36me3 binding motif. The ORC complex, including LRWD1, binds to the three most prominent transcriptional repressive lysine methylation sites. Our data reveal a highly adapted interplay between chromatin marks and their associated protein complexes. Reading specific trimethyl-lysine sites by specialized complexes appears to be a widespread mechanism to mediate gene expression.

AB - Trimethyl-lysine (me3) modifications on histones are the most stable epigenetic marks and they control chromatin-mediated regulation of gene expression. Here, we determine proteins that bind these marks by high-accuracy, quantitative mass spectrometry. These chromatin "readers" are assigned to complexes by interaction proteomics of full-length BAC-GFP-tagged proteins. ChIP-Seq profiling identifies their genomic binding sites, revealing functional properties. Among the main findings, the human SAGA complex binds to H3K4me3 via a double Tudor-domain in the C terminus of Sgf29, and the PWWP domain is identified as a putative H3K36me3 binding motif. The ORC complex, including LRWD1, binds to the three most prominent transcriptional repressive lysine methylation sites. Our data reveal a highly adapted interplay between chromatin marks and their associated protein complexes. Reading specific trimethyl-lysine sites by specialized complexes appears to be a widespread mechanism to mediate gene expression.

KW - Chromatin

KW - Epigenesis, Genetic

KW - Gene Expression Regulation

KW - Genome-Wide Association Study

KW - Hela Cells

KW - Histone Acetyltransferases

KW - Histone Code

KW - Humans

KW - Lysine

KW - Mass Spectrometry

KW - Methylation

KW - Proteomics

U2 - 10.1016/j.cell.2010.08.020

DO - 10.1016/j.cell.2010.08.020

M3 - Journal article

C2 - 20850016

VL - 142

SP - 967

EP - 980

JO - Cell

JF - Cell

SN - 0092-8674

IS - 6

ER -

ID: 32355662