Histone acetyltransferases and histone deacetyl transferases play crucial role during oogenesis and early embryo development.
HATs
HDACs
early embryo development
oogenesis
preimplantation embryos
Journal
Genesis (New York, N.Y. : 2000)
ISSN: 1526-968X
Titre abrégé: Genesis
Pays: United States
ID NLM: 100931242
Informations de publication
Date de publication:
09 2023
09 2023
Historique:
revised:
29
04
2023
received:
09
02
2023
accepted:
02
05
2023
medline:
21
9
2023
pubmed:
25
5
2023
entrez:
25
5
2023
Statut:
ppublish
Résumé
Dynamic epigenetic regulation is critical for proper oogenesis and early embryo development. During oogenesis, fully grown germinal vesicle oocytes develop to mature Metaphase II oocytes which are ready for fertilization. Fertilized oocyte proliferates mitotically until blastocyst formation and the process is called early embryo development. Throughout oogenesis and early embryo development, spatio-temporal gene expression takes place, and this dynamic gene expression is controlled with the aid of epigenetics. Epigenetic means that gene expression can be altered without changing DNA itself. Epigenome is regulated through DNA methylation and histone modifications. While DNA methylation generally ends up with repression of gene expression, histone modifications can result in expression or repression depending on type of modification, type of histone protein and its specific residue. One of the modifications is histone acetylation which generally ends up with gene expression. Histone acetylation occurs through the addition of acetyl group onto amino terminal of the core histone proteins by histone acetyltransferases (HATs). Contrarily, histone deacetylation is associated with repression of gene expression, and it is catalyzed by histone deacetylases (HDACs). This review article focuses on what is known about alterations in the expression of HATs and HDACs and emphasizes importance of HATs and HDACs during oogenesis and early embryo development.
Substances chimiques
Histones
0
Histone Acetyltransferases
EC 2.3.1.48
Transferases
EC 2.-
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e23518Informations de copyright
© 2023 Wiley Periodicals LLC.
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