ArticleThe Journal of nutrition2006
Drosophila melanogaster holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan, and heat tolerance.
Article in The Journal of nutrition, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 81 citations in OpenAlex.
- Biotin Induces Inactive Chromosome X Reactivation and Corrects Physiopathological Alterations in Beta-Propeller-Protein-Associated Neurodegeneration.International journal of molecular sciences · 2025Article
- Rad6 Regulates Conidiation by Affecting the Biotin Metabolism inJournal of fungi (Basel, Switzerland) · 2024Article
- Review
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- Omics Insights into Animal Resilience and Stress Factors.Animals : an open access journal from MDPI · 2020Review
- Biotin rescues mitochondrial dysfunction and neurotoxicity in a tauopathy model.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A cross-talk between blood-cell neuroplasticity-related genes and environmental enrichment in working dogs.Scientific reports · 2019Article
- Resveratrol compounds inhibit human holocarboxylase synthetase and cause a lean phenotype in Drosophila melanogaster.The Journal of nutritional biochemistry · 2015Article
- A comprehensive view of the epigenetic landscape. Part II: Histone post-translational modification, nucleosome level, and chromatin regulation by ncRNAs.Neurotoxicity research · 2015Review
- β-Keto and β-hydroxyphosphonate analogs of biotin-5'-AMP are inhibitors of holocarboxylase synthetase.Bioorganic & medicinal chemistry letters · 2014Article
- Holocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeats.The Biochemical journal · 2014Article
- Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolism.Nutrition reviews · 2014Review
- Three promoters regulate the transcriptional activity of the human holocarboxylase synthetase gene.The Journal of nutritional biochemistry · 2013Article
- Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events.The Journal of nutritional biochemistry · 2013Article
- Holocarboxylase synthetase synergizes with methyl CpG binding protein 2 and DNA methyltransferase 1 in the transcriptional repression of long-terminal repeats.Epigenetics · 2013Article
- Article
- Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation.Archives of biochemistry and biophysics · 2013Article
- K16-biotinylated histone H4 is overrepresented in repeat regions and participates in the repression of transcriptionally competent genes in human Jurkat lymphoid cells.The Journal of nutritional biochemistry · 2012Article
- Whole transcriptome analysis of a reversible neurodegenerative process in Drosophila reveals potential neuroprotective genes.BMC genomics · 2012Article
- Cytosine methylation in miR-153 gene promoters increases the expression of holocarboxylase synthetase, thereby increasing the abundance of histone H4 biotinylation marks in HEK-293 human kidney cells.The Journal of nutritional biochemistry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Post-translational modifications of histones play important roles in chromatin structure and genomic stability. Distinct lysine residues in histones are targets for covalent binding of biotin, catalyzed by holocarboxylase synthetase (HCS) and biotinidase (BTD). Histone biotinylation has been implicated in heterochromatin structures, DNA repair, and mitotic chromosome condensation. To test whether HCS and BTD deficiency alters histone biotinylation and to characterize phenotypes associated with HCS and BTD deficiency, HCS- and BTD-deficient flies were generated by RNA interference (RNAi). Expression of HCS and BTD decreased by 65-90% in RNAi-treated flies, as judged by mRNA abundance, BTD activity, and abundance of HCS protein. Decreased expression of HCS and BTD caused decreased biotinylation of K9 and K18 in histone H3. This was associated with altered expression of 201 genes in HCS-deficient flies. Lifespan of HCS- and BTD-deficient flies decreased by up to 32% compared to wild-type controls. Heat tolerance decreased by up to 55% in HCS-deficient flies compared to controls, as judged by survival times; effects of BTD deficiency were minor. Consistent with this observation, HCS deficiency was associated with altered expression of 285 heat-responsive genes. HCS and BTD deficiency did not affect cold tolerance, suggesting stress-specific effects of chromatin remodeling by histone biotinylation. To our knowledge, this is the first study to provide evidence that HCS-dependent histone biotinylation affects gene function and phenotype, suggesting that the complex phenotypes of HCS- and BTD-deficiency disorders may reflect chromatin structure changes.
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