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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1993-12-16
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pubmed:abstractText |
We describe major transitions in the type and modification of chromatin-associated proteins during the early development of Xenopus laevis. Histone H4 is stored in the diacetylated form in the egg and is progressively deacetylated during normal development. If histone deacetylases are inhibited with sodium butyrate, hyperacetylated histone H4 only accumulates after the mid-blastula transition. The type of linker histone in chromatin also changes during embryogenesis, from predominantly the B4 protein at the mid-blastula transition to predominantly histone H1 at the end of gastrulation. These transitions in chromatin composition correlate with major changes in the replicative and transcriptional activity of embryonic nuclei.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0012-1606
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
160
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
214-27
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:8224538-Acetylation,
pubmed-meshheading:8224538-Amino Acid Sequence,
pubmed-meshheading:8224538-Animals,
pubmed-meshheading:8224538-Base Sequence,
pubmed-meshheading:8224538-Blastocyst,
pubmed-meshheading:8224538-Butyric Acid,
pubmed-meshheading:8224538-Butyric Acids,
pubmed-meshheading:8224538-Chromatin,
pubmed-meshheading:8224538-Culture Techniques,
pubmed-meshheading:8224538-DNA,
pubmed-meshheading:8224538-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:8224538-Gastrula,
pubmed-meshheading:8224538-Histones,
pubmed-meshheading:8224538-Molecular Sequence Data,
pubmed-meshheading:8224538-Oocytes,
pubmed-meshheading:8224538-Sequence Homology, Amino Acid,
pubmed-meshheading:8224538-Transcription, Genetic,
pubmed-meshheading:8224538-Xenopus laevis
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pubmed:year |
1993
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pubmed:articleTitle |
Chromatin transitions during early Xenopus embryogenesis: changes in histone H4 acetylation and in linker histone type.
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pubmed:affiliation |
Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, NIH, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article
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