Effect of biotin on phosphorylation, acetylation, methylation of rat liver histones

Petrelli, Fabio; Coderoni, S.; Moretti, Pierre; Paparelli, M

doi:10.1007/bf00775966

Cited by 27 publications

(10 citation statements)

References 26 publications

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“…In contrast, dimethylation of arginine residues enhances biotinylation of adjacent lysine residues (118). This is consistent with studies suggesting that histones in livers from biotin-deficient rats showed unusual patterns of phosphorylation, methylation, and acetylation compared with biotin-sufficient controls (99).…”

Section: Identification Of Biotinylation Sitessupporting

confidence: 90%

Uptake, Localization, and Noncarboxylase Roles of Biotin

2005

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Evidence is emerging that biotin participates in processes other than classical carboxylation reactions. Specifically, novel roles for biotin in cell signaling, gene expression, and chromatin structure have been identified in recent years. Human cells accumulate biotin by using both the sodium-dependent multivitamin transporter and monocarboxylate transporter 1. These transporters and other biotin-binding proteins partition biotin to compartments involved in biotin signaling: cytoplasm, mitochondria, and nuclei. The activity of cell signals such as biotinyl-AMP, Sp1 and Sp3, nuclear factor (NF)-kappaB, and receptor tyrosine kinases depends on biotin supply. Consistent with a role for biotin and its catabolites in modulating these cell signals, greater than 2000 biotin-dependent genes have been identified in various human tissues. Many biotin-dependent gene products play roles in signal transduction and localize to the cell nucleus, consistent with a role for biotin in cell signaling. Posttranscriptional events related to ribosomal activity and protein folding may further contribute to effects of biotin on gene expression. Finally, research has shown that biotinidase and holocarboxylase synthetase mediate covalent binding of biotin to histones (DNA-binding proteins), affecting chromatin structure; at least seven biotinylation sites have been identified in human histones. Biotinylation of histones appears to play a role in cell proliferation, gene silencing, and the cellular response to DNA repair. Roles for biotin in cell signaling and chromatin structure are consistent with the notion that biotin has a unique significance in cell biology.

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Section: Identification Of Biotinylation Sitessupporting

confidence: 90%

Uptake, Localization, and Noncarboxylase Roles of Biotin

2005

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“…As was demonstrated recently by Hymes and co-workers (55,56), human histones may be specifically biotinylated, in vivo, by the action of biotinidase functioning as a biotin transferase rather than as hydrolase. The packaging and regulatory properties of rat liver chromatin were shown be affected by a similar histone modification (59,60). Similarly, noncovalently associated biotinyl-AMP facilitates binding of the BirA aporepressor to the E. coli biotin operator (10,57,61).…”

Section: Discussionmentioning

confidence: 99%

Identification of the tRNA-binding Protein Arc1p as a Novel Target of in Vivo Biotinylation in Saccharomyces cerevisiae

Kim

Hoja

Stolz

et al. 2004

Journal of Biological Chemistry

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Biotin is an essential cofactor of cell metabolism serving as a protein-bound coenzyme in ATP-dependent carboxylation, in transcarboxylation, and certain decarboxylation reactions. The involvement of biotinylated proteins in other cellular functions has been suggested occasionally, but available data on this are limited. In the present study, a Saccharomyces cerevisiae protein was identified that reacts with streptavidin on Western blots and is not identical to one of the known biotinylated yeast proteins. After affinity purification on monomeric avidin, the biotinylated protein was identified as Arc1p. Using 14 C-labeled biotin, the cofactor was shown to be incorporated into Arc1p by covalent and alkalistable linkage. Similar to the known carboxylases, Arc1p biotinylation is mediated by the yeast biotin:protein ligase, Bpl1p. Mutational studies revealed that biotinylation occurs at lysine 86 within the N-terminal domain of Arc1p. In contrast to the known carboxylases, however, in vitro biotinylation of Arc1p is incomplete and increases with BPL1 overexpression. In accordance to this fact, Arc1p lacks the canonical consensus sequence of known biotin binding domains, and the bacterial biotin:protein ligase, BirA, is unable to use Arc1p as a substrate. Arc1p was shown previously to organize the association of MetRS and GluRS tRNA synthetases with their cognate tRNAs thereby increasing the substrate affinity and catalytic efficiency of these enzymes. Remarkably, not only biotinylated but also the biotinfree Arc1p obtained by replacement of lysine 86 with arginine were capable of restoring Arc1p function in both arc1⌬ and arc1⌬los1⌬ mutants, indicating that biotinylation of Arc1p is not essential for activity.

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“…134 In prostate cells, it has been demonstrated that hypoxia increases global DNA methylation and H3K9 histone acetylation. 136 Several dietary factors have been linked to increased histone acetylation (Table V), including biotin deficiency, 137 quercetin, 138 or caffeine. 136 Several dietary factors have been linked to increased histone acetylation (Table V), including biotin deficiency, 137 quercetin, 138 or caffeine.…”

Section: B Histone Modificationsmentioning

confidence: 99%