title: Camello, a novel family of Histone Acetyltransferases that acetylate histone H4 and is essential for zebrafish development.
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.
authors.affiliation: Center of Excellence in Epigenetics, Indian Institute of Science Education and Research, Pashan, Pune 411 021, India.
authors.forename: Krishanpal
authors.initials: K
authors.lastname: Karmodiya
authors.affiliation: 1] Center of Excellence in Epigenetics, Indian Institute of Science Education and Research, Pashan, Pune 411 021, India [2].
authors.forename: Krishanpal
authors.initials: K
authors.lastname: Anamika
authors.affiliation: Center of Excellence in Epigenetics, Indian Institute of Science Education and Research, Pashan, Pune 411 021, India.
authors.forename: Vijaykumar
authors.initials: V
authors.lastname: Muley
authors.affiliation: Center of Excellence in Epigenetics, Indian Institute of Science Education and Research, Pashan, Pune 411 021, India.
authors.forename: Saurabh J
authors.initials: SJ
authors.lastname: Pradhan
authors.affiliation: Center of Excellence in Epigenetics, Indian Institute of Science Education and Research, Pashan, Pune 411 021, India.
authors.forename: Yoshita
authors.initials: Y
authors.lastname: Bhide
authors.affiliation: Center of Excellence in Epigenetics, Indian Institute of Science Education and Research, Pashan, Pune 411 021, India.
authors.forename: Sanjeev
authors.initials: S
authors.lastname: Galande
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D019521:Body Patterning / Q000235:genetics*; D045744:Cell Line, Tumor; D055785:Gene Knockdown Techniques; D006367:HeLa Cells; D051548:Histone Acetyltransferases / Q000235:genetics* / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D060172:Morpholinos / Q000235:genetics; D011499:Protein Processing, Post-Translational; D016415:Sequence Alignment; D015027:Zebrafish / Q000196:embryology*; D016335:Zinc Fingers / Q000235:genetics
chemical_list: D006657:Histones; D060172:Morpholinos; D051548:Histone Acetyltransferases; D008239:Lysine