Cargando…
HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth
The dynamic architecture of chromatin is vital for proper cellular function, and is maintained by the concerted action of numerous nuclear proteins, including that of the linker histone H1 variants, the most abundant family of nucleosome-binding proteins. Here we show that the nuclear protein HP1BP3...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4344522/ https://www.ncbi.nlm.nih.gov/pubmed/25662603 http://dx.doi.org/10.1093/nar/gkv089 |
_version_ | 1782359428652072960 |
---|---|
author | Garfinkel, Benjamin P. Melamed-Book, Naomi Anuka, Eli Bustin, Michael Orly, Joseph |
author_facet | Garfinkel, Benjamin P. Melamed-Book, Naomi Anuka, Eli Bustin, Michael Orly, Joseph |
author_sort | Garfinkel, Benjamin P. |
collection | PubMed |
description | The dynamic architecture of chromatin is vital for proper cellular function, and is maintained by the concerted action of numerous nuclear proteins, including that of the linker histone H1 variants, the most abundant family of nucleosome-binding proteins. Here we show that the nuclear protein HP1BP3 is widely expressed in most vertebrate tissues and is evolutionarily and structurally related to the H1 family. HP1BP3 contains three globular domains and a highly positively charged C-terminal domain, resembling similar domains in H1. Fluorescence recovery after photobleaching (FRAP) studies indicate that like H1, binding of HP1BP3 to chromatin depends on both its C and N terminal regions and is affected by the cell cycle and post translational modifications. HP1BP3 contains functional motifs not found in H1 histones, including an acidic stretch and a consensus HP1-binding motif. Transcriptional profiling of HeLa cells lacking HP1BP3 showed altered expression of 383 genes, suggesting a role for HP1BP3 in modulation of gene expression. Significantly, Hp1bp3(−/−) mice present a dramatic phenotype with 60% of pups dying within 24 h of birth and the surviving animals exhibiting a lifelong 20% growth retardation. We suggest that HP1BP3 is a ubiquitous histone H1 like nuclear protein with distinct and non-redundant functions necessary for survival and growth. |
format | Online Article Text |
id | pubmed-4344522 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-43445222015-03-17 HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth Garfinkel, Benjamin P. Melamed-Book, Naomi Anuka, Eli Bustin, Michael Orly, Joseph Nucleic Acids Res Gene regulation, Chromatin and Epigenetics The dynamic architecture of chromatin is vital for proper cellular function, and is maintained by the concerted action of numerous nuclear proteins, including that of the linker histone H1 variants, the most abundant family of nucleosome-binding proteins. Here we show that the nuclear protein HP1BP3 is widely expressed in most vertebrate tissues and is evolutionarily and structurally related to the H1 family. HP1BP3 contains three globular domains and a highly positively charged C-terminal domain, resembling similar domains in H1. Fluorescence recovery after photobleaching (FRAP) studies indicate that like H1, binding of HP1BP3 to chromatin depends on both its C and N terminal regions and is affected by the cell cycle and post translational modifications. HP1BP3 contains functional motifs not found in H1 histones, including an acidic stretch and a consensus HP1-binding motif. Transcriptional profiling of HeLa cells lacking HP1BP3 showed altered expression of 383 genes, suggesting a role for HP1BP3 in modulation of gene expression. Significantly, Hp1bp3(−/−) mice present a dramatic phenotype with 60% of pups dying within 24 h of birth and the surviving animals exhibiting a lifelong 20% growth retardation. We suggest that HP1BP3 is a ubiquitous histone H1 like nuclear protein with distinct and non-redundant functions necessary for survival and growth. Oxford University Press 2015-02-27 2015-02-08 /pmc/articles/PMC4344522/ /pubmed/25662603 http://dx.doi.org/10.1093/nar/gkv089 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Gene regulation, Chromatin and Epigenetics Garfinkel, Benjamin P. Melamed-Book, Naomi Anuka, Eli Bustin, Michael Orly, Joseph HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth |
title | HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth |
title_full | HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth |
title_fullStr | HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth |
title_full_unstemmed | HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth |
title_short | HP1BP3 is a novel histone H1 related protein with essential roles in viability and growth |
title_sort | hp1bp3 is a novel histone h1 related protein with essential roles in viability and growth |
topic | Gene regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4344522/ https://www.ncbi.nlm.nih.gov/pubmed/25662603 http://dx.doi.org/10.1093/nar/gkv089 |
work_keys_str_mv | AT garfinkelbenjaminp hp1bp3isanovelhistoneh1relatedproteinwithessentialrolesinviabilityandgrowth AT melamedbooknaomi hp1bp3isanovelhistoneh1relatedproteinwithessentialrolesinviabilityandgrowth AT anukaeli hp1bp3isanovelhistoneh1relatedproteinwithessentialrolesinviabilityandgrowth AT bustinmichael hp1bp3isanovelhistoneh1relatedproteinwithessentialrolesinviabilityandgrowth AT orlyjoseph hp1bp3isanovelhistoneh1relatedproteinwithessentialrolesinviabilityandgrowth |