A novel, enigmatic histone modification: biotinylation of histones by holocarboxylase synthetase
- 19 November 2008
- journal article
- review article
- Published by Oxford University Press (OUP) in Nutrition Reviews
- Vol. 66 (12), 721-725
- https://doi.org/10.1111/j.1753-4887.2008.00127.x
Abstract
Holocarboxylase synthetase catalyzes the covalent binding of biotin to histones in humans and other eukaryotes. Eleven biotinylation sites have beenKeywords
This publication has 47 references indexed in Scilit:
- Biotinylation of Histones Represses Transposable Elements in Human and Mouse Cells and Cell Lines and in Drosophila melanogaster3Journal of Nutrition, 2008
- Epigenetic regulation of chromatin structure and gene function by biotin: are biotin requirements being met?Nutrition Reviews, 2008
- Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locusThe Journal of Nutritional Biochemistry, 2008
- An avidin-based assay for histone debiotinylase activity in human cell nucleiThe Journal of Nutritional Biochemistry, 2007
- K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidaseThe FEBS Journal, 2005
- K8 and K12 are biotinylated in human histone H4European Journal of Biochemistry, 2004
- Reduced histone biotinylation in multiple carboxylase deficiency patients: a nuclear role for holocarboxylase synthetaseHuman Molecular Genetics, 2003
- Structure of human holocarboxylase synthetase gene and mutation spectrum of holocarboxylase synthetase deficiencyHuman Genetics, 2001
- Translating the Histone CodeScience, 2001
- Increase in histone poly(ADP-ribosylation) in mitogen-activated lymphoid cellsExperimental Cell Research, 1990