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Corecognition of DNA and a methylated histone tail by MSL3 chromodomain
MSL3 resides in the MSL (male-specific-lethal) complex that upregulates transcription by spreading the H4K16 acetyl-mark. We discovered a DNA-dependent interaction of MSL3 chromodomain with the histone H4K20 monomethyl-mark. Structure of a ternary complex shows DNA minor groove accommodates the hist...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924628/ https://www.ncbi.nlm.nih.gov/pubmed/20657587 http://dx.doi.org/10.1038/nsmb.1856 |
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author | Kim, Daesung Blus, Bartlomiej J. Chandra, Vikas Huang, Pengxiang Rastinejad, Fraydoon Khorasanizadeh, Sepideh |
author_facet | Kim, Daesung Blus, Bartlomiej J. Chandra, Vikas Huang, Pengxiang Rastinejad, Fraydoon Khorasanizadeh, Sepideh |
author_sort | Kim, Daesung |
collection | PubMed |
description | MSL3 resides in the MSL (male-specific-lethal) complex that upregulates transcription by spreading the H4K16 acetyl-mark. We discovered a DNA-dependent interaction of MSL3 chromodomain with the histone H4K20 monomethyl-mark. Structure of a ternary complex shows DNA minor groove accommodates the histone H4 tail, and monomethyllysine inserts in a four-residue aromatic cage in MSL3. Histone H4K16 acetyl-mark antagonizes MSL3 binding, suggesting MSL function is regulated by a combination of post-translational modifications. |
format | Text |
id | pubmed-2924628 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
record_format | MEDLINE/PubMed |
spelling | pubmed-29246282011-02-01 Corecognition of DNA and a methylated histone tail by MSL3 chromodomain Kim, Daesung Blus, Bartlomiej J. Chandra, Vikas Huang, Pengxiang Rastinejad, Fraydoon Khorasanizadeh, Sepideh Nat Struct Mol Biol Article MSL3 resides in the MSL (male-specific-lethal) complex that upregulates transcription by spreading the H4K16 acetyl-mark. We discovered a DNA-dependent interaction of MSL3 chromodomain with the histone H4K20 monomethyl-mark. Structure of a ternary complex shows DNA minor groove accommodates the histone H4 tail, and monomethyllysine inserts in a four-residue aromatic cage in MSL3. Histone H4K16 acetyl-mark antagonizes MSL3 binding, suggesting MSL function is regulated by a combination of post-translational modifications. 2010-07-25 2010-08 /pmc/articles/PMC2924628/ /pubmed/20657587 http://dx.doi.org/10.1038/nsmb.1856 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Kim, Daesung Blus, Bartlomiej J. Chandra, Vikas Huang, Pengxiang Rastinejad, Fraydoon Khorasanizadeh, Sepideh Corecognition of DNA and a methylated histone tail by MSL3 chromodomain |
title | Corecognition of DNA and a methylated histone tail by MSL3 chromodomain |
title_full | Corecognition of DNA and a methylated histone tail by MSL3 chromodomain |
title_fullStr | Corecognition of DNA and a methylated histone tail by MSL3 chromodomain |
title_full_unstemmed | Corecognition of DNA and a methylated histone tail by MSL3 chromodomain |
title_short | Corecognition of DNA and a methylated histone tail by MSL3 chromodomain |
title_sort | corecognition of dna and a methylated histone tail by msl3 chromodomain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2924628/ https://www.ncbi.nlm.nih.gov/pubmed/20657587 http://dx.doi.org/10.1038/nsmb.1856 |
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