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Linker histone variants control chromatin dynamics during early embryogenesis.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2005 Apr 19; Vol. 102 (16), pp. 5697-702. Date of Electronic Publication: 2005 Apr 08. - Publication Year :
- 2005
-
Abstract
- Complex transitions in chromatin structure produce changes in genome function during development in metazoa. Linker histones, the last component of nucleosomes to be assembled into chromatin, comprise considerably divergent subtypes as compared with core histones. In all metazoa studied, their composition changes dramatically during early embryogenesis concomitant with zygotic gene activation, leading to distinct functional changes that are still poorly understood. Here, we show that early embryonic linker histone B4, which is maternally expressed, is functionally different from somatic histone H1 in influencing chromatin structure and dynamics. We developed a chromatin assembly system with nucleosome assembly protein-1 as a linker histone chaperone. This assay system revealed that maternal histone B4 allows chromatin to be remodeled by ATP-dependent chromatin remodeling factor, whereas somatic histone H1 prevents this remodeling. Structural analysis shows that histone B4 does not significantly restrict the accessibility of linker DNA. These findings define the functional significance of developmental changes in linker histone variants. We propose a model that holds that maternally expressed linker histones are key molecules specifying nuclear dynamics with respect to embryonic totipotency.
- Subjects :
- Animals
Cell Cycle Proteins
HeLa Cells
Histones genetics
Humans
Molecular Chaperones genetics
Molecular Chaperones metabolism
Nuclear Proteins
Nucleosome Assembly Protein 1
Proteins genetics
Proteins metabolism
Recombinant Proteins genetics
Recombinant Proteins metabolism
Xenopus Proteins genetics
Xenopus Proteins metabolism
Xenopus laevis embryology
Xenopus laevis metabolism
Chromatin metabolism
Embryonic Development genetics
Histones metabolism
Nucleic Acid Conformation
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 102
- Issue :
- 16
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 15821029
- Full Text :
- https://doi.org/10.1073/pnas.0409824102