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H1 histones: current perspectives and challenges
H1 and related linker histones are important both for maintenance of higher-order chromatin structure and for the regulation of gene expression. The biology of the linker histones is complex, as they are evolutionarily variable, exist in multiple isoforms and undergo a large variety of posttranslati...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3834806/ https://www.ncbi.nlm.nih.gov/pubmed/23945933 http://dx.doi.org/10.1093/nar/gkt700 |
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author | Harshman, Sean W. Young, Nicolas L. Parthun, Mark R. Freitas, Michael A. |
author_facet | Harshman, Sean W. Young, Nicolas L. Parthun, Mark R. Freitas, Michael A. |
author_sort | Harshman, Sean W. |
collection | PubMed |
description | H1 and related linker histones are important both for maintenance of higher-order chromatin structure and for the regulation of gene expression. The biology of the linker histones is complex, as they are evolutionarily variable, exist in multiple isoforms and undergo a large variety of posttranslational modifications in their long, unstructured, NH(2)- and COOH-terminal tails. We review recent progress in understanding the structure, genetics and posttranslational modifications of linker histones, with an emphasis on the dynamic interactions of these proteins with DNA and transcriptional regulators. We also discuss various experimental challenges to the study of H1 and related proteins, including limitations of immunological reagents and practical difficulties in the analysis of posttranslational modifications by mass spectrometry. |
format | Online Article Text |
id | pubmed-3834806 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-38348062013-11-21 H1 histones: current perspectives and challenges Harshman, Sean W. Young, Nicolas L. Parthun, Mark R. Freitas, Michael A. Nucleic Acids Res Survey and Summary H1 and related linker histones are important both for maintenance of higher-order chromatin structure and for the regulation of gene expression. The biology of the linker histones is complex, as they are evolutionarily variable, exist in multiple isoforms and undergo a large variety of posttranslational modifications in their long, unstructured, NH(2)- and COOH-terminal tails. We review recent progress in understanding the structure, genetics and posttranslational modifications of linker histones, with an emphasis on the dynamic interactions of these proteins with DNA and transcriptional regulators. We also discuss various experimental challenges to the study of H1 and related proteins, including limitations of immunological reagents and practical difficulties in the analysis of posttranslational modifications by mass spectrometry. Oxford University Press 2013-11 2013-08-14 /pmc/articles/PMC3834806/ /pubmed/23945933 http://dx.doi.org/10.1093/nar/gkt700 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Survey and Summary Harshman, Sean W. Young, Nicolas L. Parthun, Mark R. Freitas, Michael A. H1 histones: current perspectives and challenges |
title | H1 histones: current perspectives and challenges |
title_full | H1 histones: current perspectives and challenges |
title_fullStr | H1 histones: current perspectives and challenges |
title_full_unstemmed | H1 histones: current perspectives and challenges |
title_short | H1 histones: current perspectives and challenges |
title_sort | h1 histones: current perspectives and challenges |
topic | Survey and Summary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3834806/ https://www.ncbi.nlm.nih.gov/pubmed/23945933 http://dx.doi.org/10.1093/nar/gkt700 |
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