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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...

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Detalles Bibliográficos
Autores principales: Kim, Daesung, Blus, Bartlomiej J., Chandra, Vikas, Huang, Pengxiang, Rastinejad, Fraydoon, Khorasanizadeh, Sepideh
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
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.
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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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