The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification
Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sa...
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| Format: | Article |
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Oxford Journals
2014
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| Online Access: | https://eprints.nottingham.ac.uk/2594/ |
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| author | Dreveny, Ingrid Deeves, Sian E. Fulton, Joel Yue, Baigong Messmer, Marie Bhattacharya, Amit Collins, Hilary M. Heery, David M. |
| author_facet | Dreveny, Ingrid Deeves, Sian E. Fulton, Joel Yue, Baigong Messmer, Marie Bhattacharya, Amit Collins, Hilary M. Heery, David M. |
| author_sort | Dreveny, Ingrid |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sampling H3 and H4 modification status, we show that the DPF cooperates with the MYST domain to promote H3K9 and H3K14 acetylation, although not if H3K4 is trimethylated. Four crystal structures of an extended DPF alone and in complex with unmodified or acetylated forms of the H3 tail reveal the molecular basis of crosstalk between H3K4me3 and H3K14ac. We show for the first time that MOZ DPF induces α-helical conformation of H3K4-T11, revealing a unique mode of H3 recognition. The helical structure facilitates sampling of H3K4 methylation status, and proffers H3K9 and other residues for modification. Additionally, we show that a conserved double glycine hinge flanking the H3 tail helix is required for a conformational change enabling docking of H3K14ac with the DPF. In summary, our data provide the first observations of extensive helical structure in a histone tail, revealing the inherent ability of the H3 tail to adopt alternate conformations in complex with chromatin regulators. |
| first_indexed | 2025-11-14T18:18:47Z |
| format | Article |
| id | nottingham-2594 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T18:18:47Z |
| publishDate | 2014 |
| publisher | Oxford Journals |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-25942020-05-04T20:16:30Z https://eprints.nottingham.ac.uk/2594/ The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification Dreveny, Ingrid Deeves, Sian E. Fulton, Joel Yue, Baigong Messmer, Marie Bhattacharya, Amit Collins, Hilary M. Heery, David M. Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sampling H3 and H4 modification status, we show that the DPF cooperates with the MYST domain to promote H3K9 and H3K14 acetylation, although not if H3K4 is trimethylated. Four crystal structures of an extended DPF alone and in complex with unmodified or acetylated forms of the H3 tail reveal the molecular basis of crosstalk between H3K4me3 and H3K14ac. We show for the first time that MOZ DPF induces α-helical conformation of H3K4-T11, revealing a unique mode of H3 recognition. The helical structure facilitates sampling of H3K4 methylation status, and proffers H3K9 and other residues for modification. Additionally, we show that a conserved double glycine hinge flanking the H3 tail helix is required for a conformational change enabling docking of H3K14ac with the DPF. In summary, our data provide the first observations of extensive helical structure in a histone tail, revealing the inherent ability of the H3 tail to adopt alternate conformations in complex with chromatin regulators. Oxford Journals 2014 Article PeerReviewed Dreveny, Ingrid, Deeves, Sian E., Fulton, Joel, Yue, Baigong, Messmer, Marie, Bhattacharya, Amit, Collins, Hilary M. and Heery, David M. (2014) The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Research, 42 (2). pp. 822-835. ISSN 0305-1048 http://nar.oxfordjournals.org/content/42/2/822.full doi:10.1093/nar/gkt931 doi:10.1093/nar/gkt931 |
| spellingShingle | Dreveny, Ingrid Deeves, Sian E. Fulton, Joel Yue, Baigong Messmer, Marie Bhattacharya, Amit Collins, Hilary M. Heery, David M. The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification |
| title | The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification |
| title_full | The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification |
| title_fullStr | The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification |
| title_full_unstemmed | The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification |
| title_short | The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification |
| title_sort | double phd finger domain of moz/myst3 induces α-helical structure of the histone h3 tail to facilitate acetylation and methylation sampling and modification |
| url | https://eprints.nottingham.ac.uk/2594/ https://eprints.nottingham.ac.uk/2594/ https://eprints.nottingham.ac.uk/2594/ |