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Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain
Human ASH2L is a trithorax group (TrxG) protein and a regulatory subunit of the SET1 family of lysine methyltransferases. Here we report that Ash2L binds DNA employing a Forkhead-like helix-wing-helix (HWH) domain. In vivo, Ash2L HWH domain is required for binding to the β-globin locus control regio...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3983046/ https://www.ncbi.nlm.nih.gov/pubmed/21642971 http://dx.doi.org/10.1038/nsmb.2093 |
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author | Sarvan, Sabina Avdic, Vanja Tremblay, Véronique Chaturvedi, Chandra-Prakash Zhang, Pamela Lanouette, Sylvain Blais, Alexandre Brunzelle, Joseph S. Brand, Marjorie Couture, Jean-François |
author_facet | Sarvan, Sabina Avdic, Vanja Tremblay, Véronique Chaturvedi, Chandra-Prakash Zhang, Pamela Lanouette, Sylvain Blais, Alexandre Brunzelle, Joseph S. Brand, Marjorie Couture, Jean-François |
author_sort | Sarvan, Sabina |
collection | PubMed |
description | Human ASH2L is a trithorax group (TrxG) protein and a regulatory subunit of the SET1 family of lysine methyltransferases. Here we report that Ash2L binds DNA employing a Forkhead-like helix-wing-helix (HWH) domain. In vivo, Ash2L HWH domain is required for binding to the β-globin locus control region (LCR), histone H3 Lys4 tri-methylation and maximal expression of the β-globin gene, validating the functional importance of Ash2L DNA binding activity. |
format | Online Article Text |
id | pubmed-3983046 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
record_format | MEDLINE/PubMed |
spelling | pubmed-39830462014-04-10 Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain Sarvan, Sabina Avdic, Vanja Tremblay, Véronique Chaturvedi, Chandra-Prakash Zhang, Pamela Lanouette, Sylvain Blais, Alexandre Brunzelle, Joseph S. Brand, Marjorie Couture, Jean-François Nat Struct Mol Biol Article Human ASH2L is a trithorax group (TrxG) protein and a regulatory subunit of the SET1 family of lysine methyltransferases. Here we report that Ash2L binds DNA employing a Forkhead-like helix-wing-helix (HWH) domain. In vivo, Ash2L HWH domain is required for binding to the β-globin locus control region (LCR), histone H3 Lys4 tri-methylation and maximal expression of the β-globin gene, validating the functional importance of Ash2L DNA binding activity. 2011-06-05 /pmc/articles/PMC3983046/ /pubmed/21642971 http://dx.doi.org/10.1038/nsmb.2093 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download 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 Sarvan, Sabina Avdic, Vanja Tremblay, Véronique Chaturvedi, Chandra-Prakash Zhang, Pamela Lanouette, Sylvain Blais, Alexandre Brunzelle, Joseph S. Brand, Marjorie Couture, Jean-François Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain |
title | Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain |
title_full | Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain |
title_fullStr | Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain |
title_full_unstemmed | Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain |
title_short | Crystal structure of the trithorax group protein Ash2L reveals a Forkhead-like DNA binding domain |
title_sort | crystal structure of the trithorax group protein ash2l reveals a forkhead-like dna binding domain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3983046/ https://www.ncbi.nlm.nih.gov/pubmed/21642971 http://dx.doi.org/10.1038/nsmb.2093 |
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