Transcription-linked acetylation by Gcn5p of histones H3 and H4 at specific lysines
| Autor: | R. E. Sobel, J. E. Brownell, Richard G. Cook, S. Y. Roth, C D Allis, Tamara A. Ranalli, Diane G. Edmondson, Min Hao Kuo |
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| Rok vydání: | 1996 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Transcription Genetic Molecular Sequence Data Saccharomyces cerevisiae SAP30 complex mixtures Substrate Specificity Tetrahymena thermophila Fungal Proteins Histones Histone H4 Histone H3 Acetyltransferases Animals Histone code Amino Acid Sequence Histone Acetyltransferases Multidisciplinary biology Lysine Acetylation Histone acetyltransferase Recombinant Proteins DNA-Binding Proteins Biochemistry Histone methyltransferase biology.protein bacteria Cattle HAT1 Chickens Protein Kinases |
| Zdroj: | Nature. 383:269-272 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/383269a0 |
| Popis: | The yeast transcriptional adaptor, Gcn5p, is a catalytic subunit of a nuclear (type A) histone acetyltransferase linking histone acetylation to gene activation. Here we report that Gcn5p acetylates histones H3 and H4 non-randomly at specific lysines in the amino-terminal domains. Lysine 14 of H3 and lysines 8 and 16 of H4 are highly preferred acetylation sites for Gcn5p. We also demonstrate that lysine 9 is the preferred position of acetylation in newly synthesized yeast H3 in vivo. This finding, along with the fact that lysines 5 and 12 in H4 are predominant acetylation sites during chromatin assembly of many organisms, indicates that Gcn5p acetylates a distinct set of lysines that do not overlap with those sites characteristically used by type B histone acetyltransferases for histone deposition and chromatin assembly. |
| Databáze: | OpenAIRE |
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