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Volumn 733, Issue 1-2, 2012, Pages 58-60

Biotin requirements for DNA damage prevention

Author keywords

Biotin; Epigenetics; Genome stability; Human; Requirements

Indexed keywords

BINDING PROTEIN; BIOTIN; HISTONE H3; HISTONE METHYLTRANSFERASE; HOLOCARBOXYLASE SYNTHETASE; METHYLATED CYTOSINE BINDING PROTEIN 2; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 84860553658     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2011.08.001     Document Type: Review
Times cited : (28)

References (40)
  • 2
    • 0035853728 scopus 로고    scopus 로고
    • Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase, Influence of the N-terminus on biotinylation and identification of a minimum functional protein
    • Campeau E., Gravel R.A. Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase, Influence of the N-terminus on biotinylation and identification of a minimum functional protein. J. Biol. Chem. 2001, 276:12310-12316.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12310-12316
    • Campeau, E.1    Gravel, R.A.2
  • 3
    • 0003114965 scopus 로고    scopus 로고
    • Disorders of biotin metabolism
    • McGraw-Hill, New York, NY, C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.)
    • Wolf B. Disorders of biotin metabolism. The Metabolic and Molecular Bases of Inherited Disease 2001, 3935-3962. McGraw-Hill, New York, NY. C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
    • (2001) The Metabolic and Molecular Bases of Inherited Disease , pp. 3935-3962
    • Wolf, B.1
  • 5
    • 0025987716 scopus 로고
    • Biotinidase deficiency
    • Medical Book Publishers, Chicago, IL, L. Barness, F. Oski (Eds.)
    • Wolf B., Heard G.S. Biotinidase deficiency. Advances in Pediatrics 1991, 1-21. Medical Book Publishers, Chicago, IL. L. Barness, F. Oski (Eds.).
    • (1991) Advances in Pediatrics , pp. 1-21
    • Wolf, B.1    Heard, G.S.2
  • 6
    • 0034797338 scopus 로고    scopus 로고
    • Biotinylation of histones in human cells: effects of cell proliferation
    • Stanley J.S., Griffin J.B., Zempleni J. Biotinylation of histones in human cells: effects of cell proliferation. Eur. J. Biochem. 2001, 268:5424-5429.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5424-5429
    • Stanley, J.S.1    Griffin, J.B.2    Zempleni, J.3
  • 9
    • 33645053801 scopus 로고    scopus 로고
    • Lysine residues in N- and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase
    • Chew Y.C, Camporeale G., Kothapalli N., Sarath G., Zempleni J. Lysine residues in N- and C-terminal regions of human histone H2A are targets for biotinylation by biotinidase. J. Nutr. Biochem. 2006, 17:225-233.
    • (2006) J. Nutr. Biochem. , vol.17 , pp. 225-233
    • Chew, Y.C.1    Camporeale, G.2    Kothapalli, N.3    Sarath, G.4    Zempleni, J.5
  • 10
    • 43249096338 scopus 로고    scopus 로고
    • Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3
    • Kobza K., Sarath G., Zempleni J. Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3. BMB Rep. 2008, 41:310-315.
    • (2008) BMB Rep. , vol.41 , pp. 310-315
    • Kobza, K.1    Sarath, G.2    Zempleni, J.3
  • 11
    • 79954572835 scopus 로고    scopus 로고
    • Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18
    • Bao B., Pestinger V.H.Y.I., Borgstahl G.E.O., Kolar C., Zempleni J. Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18. J. Nutr. Biochem. 2011, 22:470-475.
    • (2011) J. Nutr. Biochem. , vol.22 , pp. 470-475
    • Bao, B.1    Pestinger, V.H.Y.I.2    Borgstahl, G.E.O.3    Kolar, C.4    Zempleni, J.5
  • 13
    • 79952533709 scopus 로고    scopus 로고
    • Novel histone biotinylation marks are enriched in repeat regions and participate in repression of transcriptionally competent genes
    • Pestinger V., Wijeratne S.S.K., Rodriguez-Melendez R., Zempleni J. Novel histone biotinylation marks are enriched in repeat regions and participate in repression of transcriptionally competent genes. J. Nutr. Biochem. 2011, 22:328-333.
    • (2011) J. Nutr. Biochem. , vol.22 , pp. 328-333
    • Pestinger, V.1    Wijeratne, S.S.K.2    Rodriguez-Melendez, R.3    Zempleni, J.4
  • 14
    • 41549161253 scopus 로고    scopus 로고
    • Biotin deficiency affects the proliferation of human embryonic palatal mesenchymal cells in culture
    • Takechi R., Taniguchi A., Ebara S., Fukui T., Watanabe T. Biotin deficiency affects the proliferation of human embryonic palatal mesenchymal cells in culture. J. Nutr. 2008, 138:680-684.
    • (2008) J. Nutr. , vol.138 , pp. 680-684
    • Takechi, R.1    Taniguchi, A.2    Ebara, S.3    Fukui, T.4    Watanabe, T.5
  • 15
    • 84874557973 scopus 로고    scopus 로고
    • Physiology, regulation, and pathogenesis of nitrogen metabolism in opportunistic fungal pathogen Candida albicans, Ph.D. Thesis [advisor: K. Nickerson]. School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE, 2009 [ISBN 9781109224726].
    • S. Ghosh, Physiology, regulation, and pathogenesis of nitrogen metabolism in opportunistic fungal pathogen Candida albicans, Ph.D. Thesis [advisor: K. Nickerson]. School of Biological Sciences, University of Nebraska-Lincoln, Lincoln, NE, 2009 [ISBN 9781109224726].
    • Ghosh, S.1
  • 18
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal
    • Kim M.Y., Zhang T., Kraus W.L. Poly(ADP-ribosyl)ation by PARP-1: 'PAR-laying' NAD+ into a nuclear signal. Genes Dev. 2005, 19:1951-1967.
    • (2005) Genes Dev. , vol.19 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 19
    • 77649270133 scopus 로고    scopus 로고
    • K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts
    • Wijeratne S.S., Camporeale G., Zempleni J. K12-biotinylated histone H4 is enriched in telomeric repeats from human lung IMR-90 fibroblasts. J. Nutr. Biochem. 2010, 21:310-316.
    • (2010) J. Nutr. Biochem. , vol.21 , pp. 310-316
    • Wijeratne, S.S.1    Camporeale, G.2    Zempleni, J.3
  • 22
    • 0003673876 scopus 로고
    • National Academy Press, Washington, DC, National Research Council
    • National Research Council Recommended Dietary Allowances 1989, National Academy Press, Washington, DC.
    • (1989) Recommended Dietary Allowances
  • 23
    • 33751079894 scopus 로고    scopus 로고
    • Drosophila holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan and heat tolerance
    • Camporeale G., Giordano E., Rendina R., Zempleni J., Eissenberg J.C. Drosophila holocarboxylase synthetase is a chromosomal protein required for normal histone biotinylation, gene transcription patterns, lifespan and heat tolerance. J. Nutr. 2006, 136:2735-2742.
    • (2006) J. Nutr. , vol.136 , pp. 2735-2742
    • Camporeale, G.1    Giordano, E.2    Rendina, R.3    Zempleni, J.4    Eissenberg, J.C.5
  • 25
    • 43249125904 scopus 로고    scopus 로고
    • Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus
    • Gralla M., Camporeale G., Zempleni J. Holocarboxylase synthetase regulates expression of biotin transporters by chromatin remodeling events at the SMVT locus. J. Nutr. Biochem. 2008, 19:400-408.
    • (2008) J. Nutr. Biochem. , vol.19 , pp. 400-408
    • Gralla, M.1    Camporeale, G.2    Zempleni, J.3
  • 26
    • 25444442591 scopus 로고    scopus 로고
    • Mutations in the holocarboxylase synthetase gene HLCS
    • Suzuki Y., Yang X., Aoki Y., Kure S., Matsubara Y. Mutations in the holocarboxylase synthetase gene HLCS. Hum. Mutat. 2005, 26:285-290.
    • (2005) Hum. Mutat. , vol.26 , pp. 285-290
    • Suzuki, Y.1    Yang, X.2    Aoki, Y.3    Kure, S.4    Matsubara, Y.5
  • 27
    • 84874577447 scopus 로고    scopus 로고
    • National Center for Biotechnology Information, Online Mendelian Inheritance in Man. Available from: (accessed 18.7.08).
    • National Center for Biotechnology Information, Online Mendelian Inheritance in Man. Available from: (accessed 18.7.08). http://www.ncbi.nlm.nih.gov/sites/entrez%3Fdb=omim.
  • 28
    • 0033060116 scopus 로고    scopus 로고
    • Prenatal diagnosis and treatment of holocarboxylase synthetase deficiency
    • Thuy L.P., Belmont J., Nyhan W.L. Prenatal diagnosis and treatment of holocarboxylase synthetase deficiency. Prenat. Diagn. 1999, 19:108-112.
    • (1999) Prenat. Diagn. , vol.19 , pp. 108-112
    • Thuy, L.P.1    Belmont, J.2    Nyhan, W.L.3
  • 29
    • 84874579597 scopus 로고    scopus 로고
    • UniProt, UniProtKB. Available from: (accessed 26.3.10).
    • UniProt, UniProtKB. Available from: (accessed 26.3.10). http://www.uniprot.org/uniprot/P50747.
  • 30
    • 84874574540 scopus 로고    scopus 로고
    • Metastasis promoting genes and proteins. Available from: (accessed 26.3.10).
    • J. Massague and P. Bos, Metastasis promoting genes and proteins. Available from: (accessed 26.3.10). http://www.faqs.org/patents/app/20100029748.
    • Massague, J.1    Bos, P.2
  • 31
    • 84874578637 scopus 로고    scopus 로고
    • Institute for Biomedical Technologies, Genes-to-system breast cancer database. Available from: (accessed 26.3.10).
    • Institute for Biomedical Technologies, Genes-to-system breast cancer database. Available from: (accessed 26.3.10). http://www.itb.cnr.it/breastcancer/php/showMostCorrelated.php%3Fid=6664.
  • 32
    • 84874562491 scopus 로고    scopus 로고
    • Epigenetic synergies between methylation of cytosines and biotinylation of histones in gene repression, Experimental Biology 2011, Washington, DC, 2011. [abstract].
    • J. Xue and J. Zempleni, Epigenetic synergies between methylation of cytosines and biotinylation of histones in gene repression, Experimental Biology 2011, Washington, DC, 2011. [abstract].
    • Xue, J.1    Zempleni, J.2
  • 34
    • 50449088155 scopus 로고    scopus 로고
    • A common sequence motif associated with recombination hot spots and genome instability in humans
    • Myers S., Freeman C., Auton A., Donnelly P., McVean G. A common sequence motif associated with recombination hot spots and genome instability in humans. Nat. Genet. 2008, 40:1124-1129.
    • (2008) Nat. Genet. , vol.40 , pp. 1124-1129
    • Myers, S.1    Freeman, C.2    Auton, A.3    Donnelly, P.4    McVean, G.5
  • 35
    • 0024590325 scopus 로고
    • Species and strain differences in teratogenic effects of biotin deficiency in rodents
    • Watanabe T., Endo A. Species and strain differences in teratogenic effects of biotin deficiency in rodents. J. Nutr. 1989, 119:255-261.
    • (1989) J. Nutr. , vol.119 , pp. 255-261
    • Watanabe, T.1    Endo, A.2
  • 36
    • 0025108841 scopus 로고
    • Teratogenic effects of maternal biotin deficiency in mouse embryos examined at midgestation
    • Watanabe T., Endo A. Teratogenic effects of maternal biotin deficiency in mouse embryos examined at midgestation. Teratology 1990, 42:295-300.
    • (1990) Teratology , vol.42 , pp. 295-300
    • Watanabe, T.1    Endo, A.2
  • 38
    • 21344433635 scopus 로고    scopus 로고
    • Marginal biotin deficiency is teratogenic in mice and perhaps humans: a review of biotin deficiency during human pregnancy and effects of biotin deficiency on gene expression and enzyme activities in mouse dam and fetus
    • Mock D.M. Marginal biotin deficiency is teratogenic in mice and perhaps humans: a review of biotin deficiency during human pregnancy and effects of biotin deficiency on gene expression and enzyme activities in mouse dam and fetus. J. Nutr. Biochem. 2005, 16:435-437.
    • (2005) J. Nutr. Biochem. , vol.16 , pp. 435-437
    • Mock, D.M.1
  • 39
    • 4444240734 scopus 로고    scopus 로고
    • Biotin supplementation increases expression of the cytochrome P450 1B1 gene in Jurkat cells, increasing the occurrence of single-stranded DNA breaks
    • Rodriguez-Melendez R., Griffin J.B., Zempleni J. Biotin supplementation increases expression of the cytochrome P450 1B1 gene in Jurkat cells, increasing the occurrence of single-stranded DNA breaks. J. Nutr. 2004, 134:2222-2228.
    • (2004) J. Nutr. , vol.134 , pp. 2222-2228
    • Rodriguez-Melendez, R.1    Griffin, J.B.2    Zempleni, J.3
  • 40
    • 19844378446 scopus 로고    scopus 로고
    • Low intake of calcium, folate, nicotinic acid, vitamin E, retinol, beta-carotene and high intake of pantothenic acid, biotin and riboflavin are significantly associated with increased genome instability - results from a dietary intake and micronucleus index survey in South Australia
    • Fenech M., Baghurst P., Luderer W., Turner J., Record S., Ceppi M., Bonassi S. Low intake of calcium, folate, nicotinic acid, vitamin E, retinol, beta-carotene and high intake of pantothenic acid, biotin and riboflavin are significantly associated with increased genome instability - results from a dietary intake and micronucleus index survey in South Australia. Carcinogenesis 2005, 26:991-999.
    • (2005) Carcinogenesis , vol.26 , pp. 991-999
    • Fenech, M.1    Baghurst, P.2    Luderer, W.3    Turner, J.4    Record, S.5    Ceppi, M.6    Bonassi, S.7


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