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

Yousef I. Hassan; Janos Zempleni

doi:10.1111/j.1753-4887.2008.00127.x

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

Yousef I. Hassan, Janos Zempleni

Research output: Contribution to journal › Review article › peer-review

47 Scopus citations

Abstract

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 telomeres. The abundance of biotinylated histones at distinct genomic loci depends on biotin availability. Decreased histone biotinylation decreases life span and stress resistance in Drosophila. Low enrichment of biotinylated histones at transposable elements impairs repression of these elements.

Original language	English (US)
Pages (from-to)	721-725
Number of pages	5
Journal	Nutrition Reviews
Volume	66
Issue number	12
DOIs	https://doi.org/10.1111/j.1753-4887.2008.00127.x
State	Published - Dec 2008

Keywords

Biotin
Chromatin
Epigenetics
Histones
Holocarboxylase synthetase

ASJC Scopus subject areas

Medicine (miscellaneous)
Nutrition and Dietetics

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10.1111/j.1753-4887.2008.00127.x

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abstract = "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 telomeres. The abundance of biotinylated histones at distinct genomic loci depends on biotin availability. Decreased histone biotinylation decreases life span and stress resistance in Drosophila. Low enrichment of biotinylated histones at transposable elements impairs repression of these elements.",

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AU - Hassan, Yousef I.

AU - Zempleni, Janos

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N2 - 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 telomeres. The abundance of biotinylated histones at distinct genomic loci depends on biotin availability. Decreased histone biotinylation decreases life span and stress resistance in Drosophila. Low enrichment of biotinylated histones at transposable elements impairs repression of these elements.

AB - 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 telomeres. The abundance of biotinylated histones at distinct genomic loci depends on biotin availability. Decreased histone biotinylation decreases life span and stress resistance in Drosophila. Low enrichment of biotinylated histones at transposable elements impairs repression of these elements.

KW - Biotin

KW - Chromatin

KW - Epigenetics

KW - Histones

KW - Holocarboxylase synthetase

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

Abstract

Keywords

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