Repression of Transposable Elements by Histone Biotinylation

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The Journal of Nutrition Symposium: Nutrients and Epigenetic Regulation of Gene Expression Repression of Transposable Elements by Histone Biotinylation

Transposable elements constitute .40% of the human genome; transposition of these elements increases genome instability and cancer risk. Epigenetic mechanisms are important for transcriptional repression of retrotransposons, thereby preventing transposition events. Binding of biotin to histones, mediated by holocarboxylase synthetase (HCS), is a novel histone mark that plays a role in gene regu...

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Histone biotinylation in Candida albicans.

Candida albicans is an opportunistic fungal pathogen in humans. It is a polymorphic fungus: it can live as yeasts, hyphae, or pseudohyphae. Biotin is required for cell growth and fatty acid metabolism because it is used as a cofactor for carboxylases such as acetyl-CoA carboxylase, and pyruvate carboxylase. In addition, we have discovered that biotin is used to modify histones in C. albicans. B...

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Holocarboxylase Synthetase-dependent Biotinylation of Histone H4

Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysine (K) residues in histones H3 and H4. Histone biotinylation marks play important roles in the repression of genes and retrotransposons. Preliminary studies suggest that K16 in histone H4 is a target for biotinylation by HCS. Here we tested the hypothesis that H4K16bio is a real histone mark in human chromatin, and that H4K...

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A novel, enigmatic histone modification: biotinylation of histones by holocarboxylase synthetase.

Holocarboxylase synthetase catalyzes the covalent binding of biotin to histones in humans and other eukaryotes. Eleven biotinylation sites have been identified in histones H2A, H3, and H4. K12-biotinylated histone H4 is enriched in heterochromatin, repeat regions, and plays a role in gene repression. About 30% of the histone H4 molecules are biotinylated at K12 in histone H4 in human fibroblast...

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Topological repression of gene activity by a transposable element.

The ebgA (evolved beta-galactosidase) gene of Escherichia coli was isolated as part of a 9.6-kilobase (kb) sequence cloned into plasmid pBR322. The position of the ebgA gene within that 9.6-kilobase sequence was identified by insertional inactivation by means of the transposon gamma-delta. In addition to the gamma-delta insertions that inactivate ebgA by disrupting the coding sequence, seven ad...

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ژورنال

عنوان ژورنال: The Journal of Nutrition

سال: 2009

ISSN: 0022-3166,1541-6100

DOI: 10.3945/jn.109.111856