ZFIN ID: ZDB-PUB-140816-15
Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development
Karmodiya, K., Anamika, K., Muley, V., Pradhan, S.J., Bhide, Y., Galande, S.
Date: 2014
Source: Scientific Reports   4: 6076 (Journal)
Registered Authors:
Keywords: none
MeSH Terms:
  • Acetylation
  • Amino Acid Sequence
  • Animals
  • Body Patterning/genetics*
  • Cell Line, Tumor
  • Gene Knockdown Techniques
  • HeLa Cells
  • Histone Acetyltransferases/genetics*
  • Histone Acetyltransferases/metabolism*
  • Histones/metabolism*
  • Humans
  • Lysine/chemistry
  • Mice
  • Molecular Sequence Data
  • Morpholinos/genetics
  • Protein Processing, Post-Translational
  • Sequence Alignment
  • Zebrafish/embryology*
  • Zinc Fingers/genetics
PubMed: 25123547 Full text @ Sci. Rep.
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ABSTRACT
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.
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