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PMID: 15316069 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Dynamic alterations of specific histone modifications during early murine development.

Journal of cell science ·Vol. 117 ·No. Pt 19 ·2004-09-01 ·Pages 4449-59

Sarmento OF, Digilio LC, Wang Y, Perlin J, Herr JC, Allis CD, Coonrod SA

Abstract

In order to investigate whether covalent histone modifications may be involved in early embryonic reprogramming events, changes in global levels of a series of histone tail modifications were studied during oocyte maturation and pre-implantation mouse development using indirect immunofluorescence and scanning confocal microscopy. Results showed that histone modifications could be classified into two strikingly distinct categories. The first contains stable 'epigenetic' marks such as histone H3 lysine 9 methylation [Me(Lys9)H3], histone H3 lysine 4 methylation [Me(Lys4)H3] and histone H4/H2A serine 1 phosphorylation [Ph(Ser1)H4/H2A]. The second group contains dynamic and reversible marks and includes hyperacetylated histone H4, histone H3 arginine 17 methylation [Me(Arg17)H3] and histone H4 arginine 3 methylation [Me(Arg3)H4]). Our results also showed that removal of these marks in eggs and early embryos occurs during metaphase suggesting that the enzymes responsible for the loss of these modifications are probably cytoplasmic in nature. Finally, we provide data demonstrating that treatment of cellular histones with peptidylarginine deiminase (PAD) results in loss of staining for the histone H4 arginine 3 methyl mark, suggesting that PADs can reverse histone arginine methyl modifications.

MeSH Terms
Acetylation Animals Arginine/metabolism Embryo, Mammalian/metabolism Female Fluorescent Antibody Technique, Indirect Histones/metabolism Hydrolases/metabolism Lysine/metabolism Metaphase/physiology Methylation Mice Microscopy, Confocal Oocytes/growth & development,metabolism Phosphorylation Protein-Arginine Deiminases Serine/metabolism
Chemicals
Histones Serine Arginine Hydrolases Protein-Arginine Deiminases Lysine
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Sarmento Olga F
Department of Cell Biology, University of Virginia Health Science Center, PO Box 800732, Charlottesville, VA 22908, USA.
Digilio Laura C
Wang Yanming
Perlin Julie
Herr John C
Allis C David
Coonrod Scott A
Article Info
Journal
Journal of cell science
Abbr.
J Cell Sci
ISSN
0021-9533
Published
2004-09-01
Epub
2004-00-17
Pages
4449-59
Language
English
Region
England
NLM ID
0052457
Subset
IM
Grants
NICHD NIH HHS · HD38353 · United States
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