ArticleMolecular genetics and metabolism2011
Biotinylation is a natural, albeit rare, modification of human histones.
Article in Molecular genetics and metabolism, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 66 citations in OpenAlex.
- Pregnancy and lactation alter biomarkers of biotin metabolism in women consuming a controlled diet.The Journal of nutrition · 2014Trial
- Histone modifications: Unveiling the epigenetic enigma of degenerative skeletal diseases.Journal of orthopaedic translation · 2025Review
- Post-Translational Modifications of Proteins Orchestrate All Hallmarks of Cancer.Life (Basel, Switzerland) · 2025Review
- Substrate and Functional Diversity of Protein Lysine Post-translational Modifications.Genomics, proteomics & bioinformatics · 2024Review
- Biotin attenuates heat shock factor 4b transcriptional activity by lysine 444 biotinylation.Biochemistry and biophysics reports · 2022Article
- Selective modulation of cell surface proteins during vaccinia infection: A resource for identifying viral immune evasion strategies.PLoS pathogens · 2022Article
- Article
- The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape.Genes · 2021Review
- Transposable Elements and Stress in Vertebrates: An Overview.International journal of molecular sciences · 2021Review
- Biotin rescues mitochondrial dysfunction and neurotoxicity in a tauopathy model.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mapping the Proteome of the Synaptic Cleft through Proximity Labeling Reveals New Cleft Proteins.Proteomes · 2018Article
- Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins.Chemical communications (Cambridge, England) · 2016Article
- Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation.The Journal of biological chemistry · 2016Article
- An assessment of molecular pathways of obesity susceptible to nutrient, toxicant and genetically induced epigenetic perturbation.The Journal of nutritional biochemistry · 2016Review
- Histone H2A.Z deregulation in prostate cancer. Cause or effect?Cancer metastasis reviews · 2014Review
- 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
- Nuclear receptors and epigenetic regulation: opportunities for nutritional targeting and disease prevention.Advances in nutrition (Bethesda, Md.) · 2014Review
- Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolism.Nutrition reviews · 2014Review
- Lysine biotinylation and methionine oxidation in the heat shock protein HSP60 synergize in the elimination of reactive oxygen species in human cell cultures.The Journal of nutritional biochemistry · 2014Article
- Epigenetic synergies between biotin and folate in the regulation of pro-inflammatory cytokines and repeats.Scandinavian journal of immunology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Previous studies suggest that histones H3 and H4 are posttranslationally modified by binding of the vitamin biotin, catalyzed by holocarboxylase synthetase (HCS). Albeit a rare epigenetic mark, biotinylated histones were repeatedly shown to be enriched in repeat regions and repressed loci, participating in the maintenance of genome stability and gene regulation. Recently, a team of investigators failed to detect biotinylated histones and proposed that biotinylation is not a natural modification of histones, but rather an assay artifact. Here, we describe the results of experiments, including the comparison of various analytical protocols, antibodies, cell lines, classes of histones, and radiotracers. These studies provide unambiguous evidence that biotinylation is a natural, albeit rare, histone modification. Less than 0.001% of human histones H3 and H4 are biotinylated, raising concerns that the abundance might too low to elicit biological effects in vivo. We integrated information from this study, previous studies, and ongoing research efforts to present a new working model in which biological effects are caused by a role of HCS in multiprotein complexes in chromatin. In this model, docking of HCS in chromatin causes the occasional binding of biotin to histones as a tracer for HCS binding sites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.