Structure of H3K36-methylated nucleosome–PWWP complex reveals multivalent cross-gyre binding

Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we repo...

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Published in	Nature structural & molecular biology Vol. 27; no. 1; pp. 8 - 13
Main Authors	Wang, Haibo, Farnung, Lucas, Dienemann, Christian, Cramer, Patrick
Format	Journal Article
Language	English
Published	New York Nature Publishing Group US 01.01.2020 Nature Publishing Group
Subjects	101/28 631/337/100/1701 631/337/100/2285 631/535/1258/1259 82/83 Acetylation Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Binding Biochemistry Biological Microscopy Biomedical and Life Sciences Chromatin Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA methylation DNA repair Electron microscopy Genetic research Genomes Gyres Histones Histones - chemistry Histones - metabolism Humans Life Sciences Membrane Biology Methylation Models, Molecular Molecular structure Nucleosomes Nucleosomes - chemistry Nucleosomes - metabolism Observations Peptides Properties Protein Binding Protein Conformation Protein Domains Protein Structure Sequence Alignment Transcription Factors - chemistry Transcription Factors - metabolism Germany
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ISSN	1545-9993 1545-9985 1545-9985
DOI	10.1038/s41594-019-0345-4

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Abstract	Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2–Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair. The cryo-EM structure of the PWWP reader domain of the transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA.
AbstractList	Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair. Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2–Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair. The cryo-EM structure of the PWWP reader domain of the transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA. Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here we report the cryo-electron microscopy (cryo-EM) structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with a H3K36-methylated nucleosome at 3.2 Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair. Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2–Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair.The cryo-EM structure of the PWWP reader domain of the transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA. Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair.Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair.
Audience	Academic
Author	Wang, Haibo Dienemann, Christian Farnung, Lucas Cramer, Patrick
AuthorAffiliation	1 Max-Planck-Institute for Biophysical Chemistry, Department of Molecular Biology, Am Faßberg 11, 37077 Göttingen, Germany
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BackLink	https://www.ncbi.nlm.nih.gov/pubmed/31819277$$D View this record in MEDLINE/PubMed
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Snippet	Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies...
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SubjectTerms	101/28 631/337/100/1701 631/337/100/2285 631/535/1258/1259 82/83 Acetylation Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Binding Biochemistry Biological Microscopy Biomedical and Life Sciences Chromatin Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism DNA methylation DNA repair Electron microscopy Genetic research Genomes Gyres Histones Histones - chemistry Histones - metabolism Humans Life Sciences Membrane Biology Methylation Models, Molecular Molecular structure Nucleosomes Nucleosomes - chemistry Nucleosomes - metabolism Observations Peptides Properties Protein Binding Protein Conformation Protein Domains Protein Structure Sequence Alignment Transcription Factors - chemistry Transcription Factors - metabolism
Title	Structure of H3K36-methylated nucleosome–PWWP complex reveals multivalent cross-gyre binding
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