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Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development
In this study, we have investigated genome-wide occurrence of Histone Acetyltransferases (HATs) in genomes of Mus musculus and Danio rerio on the basis of presence of HAT domain. Our study identified a group of proteins that lacks characteristic features of known HAT families, relatively smaller in...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4133703/ https://www.ncbi.nlm.nih.gov/pubmed/25123547 http://dx.doi.org/10.1038/srep06076 |
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author | Karmodiya, Krishanpal Anamika, Krishanpal Muley, Vijaykumar Pradhan, Saurabh J. Bhide, Yoshita Galande, Sanjeev |
author_facet | Karmodiya, Krishanpal Anamika, Krishanpal Muley, Vijaykumar Pradhan, Saurabh J. Bhide, Yoshita Galande, Sanjeev |
author_sort | Karmodiya, Krishanpal |
collection | PubMed |
description | In this study, we have investigated genome-wide occurrence of Histone Acetyltransferases (HATs) in genomes of Mus musculus and Danio rerio on the basis of presence of HAT domain. Our study identified a group of proteins that lacks characteristic features of known HAT families, relatively smaller in size and has no other associated domains. Most of the proteins in this unclassified group are Camello proteins, which are not yet known and classified as functional HATs. Our in vitro and in vivo analysis revealed that Camello family proteins are active HATs and exhibit specificity towards histone H4. Interestingly, Camello proteins are among the first identified HATs showing perinuclear localization. Moreover, Camello proteins are evolutionarily conserved in all chordates and are observed for the first time in cnidarians in phylogeny. Furthermore, knockdown of Camello protein (CMLO3) in zebrafish embryos exhibited defects in axis elongation and head formation. Thus, our study identified a novel family of active HATs that is specific for histone H4 acetylation, exhibits perinuclear localization and is essential for zebrafish development. |
format | Online Article Text |
id | pubmed-4133703 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-41337032014-08-18 Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development Karmodiya, Krishanpal Anamika, Krishanpal Muley, Vijaykumar Pradhan, Saurabh J. Bhide, Yoshita Galande, Sanjeev Sci Rep Article In this study, we have investigated genome-wide occurrence of Histone Acetyltransferases (HATs) in genomes of Mus musculus and Danio rerio on the basis of presence of HAT domain. Our study identified a group of proteins that lacks characteristic features of known HAT families, relatively smaller in size and has no other associated domains. Most of the proteins in this unclassified group are Camello proteins, which are not yet known and classified as functional HATs. Our in vitro and in vivo analysis revealed that Camello family proteins are active HATs and exhibit specificity towards histone H4. Interestingly, Camello proteins are among the first identified HATs showing perinuclear localization. Moreover, Camello proteins are evolutionarily conserved in all chordates and are observed for the first time in cnidarians in phylogeny. Furthermore, knockdown of Camello protein (CMLO3) in zebrafish embryos exhibited defects in axis elongation and head formation. Thus, our study identified a novel family of active HATs that is specific for histone H4 acetylation, exhibits perinuclear localization and is essential for zebrafish development. Nature Publishing Group 2014-08-15 /pmc/articles/PMC4133703/ /pubmed/25123547 http://dx.doi.org/10.1038/srep06076 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/ |
spellingShingle | Article Karmodiya, Krishanpal Anamika, Krishanpal Muley, Vijaykumar Pradhan, Saurabh J. Bhide, Yoshita Galande, Sanjeev Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development |
title | Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development |
title_full | Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development |
title_fullStr | Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development |
title_full_unstemmed | Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development |
title_short | Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development |
title_sort | camello, a novel family of histone acetyltransferases that acetylate histone h4 and is essential for zebrafish development |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4133703/ https://www.ncbi.nlm.nih.gov/pubmed/25123547 http://dx.doi.org/10.1038/srep06076 |
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