메뉴 건너뛰기




Volumn 23, Issue 12, 2012, Pages 1559-1564

K16-biotinylated histone H4 is overrepresented in repeat regions and participates in the repression of transcriptionally competent genes in human Jurkat lymphoid cells

Author keywords

Biotin; Histone; Holocarboxylase synthetase; Human

Indexed keywords

BIOTIN; HISTONE H4; HISTONE H4K16; INTERLEUKIN 2; UNCLASSIFIED DRUG;

EID: 84869083957     PISSN: 09552863     EISSN: 18734847     Source Type: Journal    
DOI: 10.1016/j.jnutbio.2011.10.009     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0004050816 scopus 로고    scopus 로고
    • Academic Press, San Diego, CA
    • Wolffe A. Chromatin 1998, Academic Press, San Diego, CA. 3rd ed.
    • (1998) Chromatin
    • Wolffe, A.1
  • 2
    • 39549083972 scopus 로고    scopus 로고
    • Chromatin modifications and their mechanism of action
    • Cold Spring Harbor Press, Cold Spring Harbor, NY, C.D. Allis, T. Jenuwein, D. Reinberg (Eds.)
    • Kouzarides T., Berger S.L. Chromatin modifications and their mechanism of action. Epigenetics 2007, 191-209. Cold Spring Harbor Press, Cold Spring Harbor, NY. C.D. Allis, T. Jenuwein, D. Reinberg (Eds.).
    • (2007) Epigenetics , pp. 191-209
    • Kouzarides, T.1    Berger, S.L.2
  • 3
    • 0028858269 scopus 로고
    • Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency
    • Hymes J., Fleischhauer K., Wolf B. Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency. Biochem Mol Med 1995, 56:76-83.
    • (1995) Biochem Mol Med , vol.56 , pp. 76-83
    • Hymes, J.1    Fleischhauer, K.2    Wolf, B.3
  • 4
    • 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
  • 7
    • 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
  • 8
    • 33745660651 scopus 로고    scopus 로고
    • Biotinylation of K8 and K12 co-occurs with acetylation and mono-methylation in human histone H4
    • [abstract]
    • Chew Y.C., Raza A.S., Sarath G., Zempleni J. Biotinylation of K8 and K12 co-occurs with acetylation and mono-methylation in human histone H4. FASEB J 2006, 20:A610. [abstract].
    • (2006) FASEB J , vol.20
    • Chew, Y.C.1    Raza, A.S.2    Sarath, G.3    Zempleni, J.4
  • 9
    • 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
  • 11
    • 23844526831 scopus 로고    scopus 로고
    • K4, K9, and K18 in human histone H3 are targets for biotinylation by biotinidase
    • Kobza K., Camporeale G., Rueckert B., Kueh A., Griffin J.B., Sarath G., et al. K4, K9, and K18 in human histone H3 are targets for biotinylation by biotinidase. FEBS J 2005, 272:4249-4259.
    • (2005) FEBS J , vol.272 , pp. 4249-4259
    • Kobza, K.1    Camporeale, G.2    Rueckert, B.3    Kueh, A.4    Griffin, J.B.5    Sarath, G.6
  • 12
    • 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 Reports 2008, 41:310-315.
    • (2008) BMB Reports , vol.41 , pp. 310-315
    • Kobza, K.1    Sarath, G.2    Zempleni, J.3
  • 13
    • 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
  • 14
    • 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., Hy 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.2    Hy, I.3    Borgstahl, G.E.O.4    Kolar, C.5    Zempleni, J.6
  • 15
    • 57349181687 scopus 로고    scopus 로고
    • Biotinylation of histones represses transposable elements in human and mouse cells and cell lines, and in Drosophila melanogaster
    • Chew Y.C., West J.T., Kratzer S.J., Ilvarsonn A.M., Eissenberg J.C., Dave B.J., et al. Biotinylation of histones represses transposable elements in human and mouse cells and cell lines, and in Drosophila melanogaster. J Nutr 2008, 138:2316-2322.
    • (2008) J Nutr , vol.138 , pp. 2316-2322
    • Chew, Y.C.1    West, J.T.2    Kratzer, S.J.3    Ilvarsonn, A.M.4    Eissenberg, J.C.5    Dave, B.J.6
  • 16
    • 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
  • 17
    • 37049019244 scopus 로고    scopus 로고
    • Artifactual detection of biotin on histones by streptavidin
    • Bailey L.M., Ivanov R.A., Wallace J.C., Polyak S.W. Artifactual detection of biotin on histones by streptavidin. Anal Biochem 2008, 373:71-77.
    • (2008) Anal Biochem , vol.373 , pp. 71-77
    • Bailey, L.M.1    Ivanov, R.A.2    Wallace, J.C.3    Polyak, S.W.4
  • 18
    • 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
  • 19
    • 34247132738 scopus 로고    scopus 로고
    • K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells
    • Camporeale G., Oommen A.M., Griffin J.B., Sarath G., Zempleni J. K12-biotinylated histone H4 marks heterochromatin in human lymphoblastoma cells. J Nutr Biochem 2007, 18:760-768.
    • (2007) J Nutr Biochem , vol.18 , pp. 760-768
    • Camporeale, G.1    Oommen, A.M.2    Griffin, J.B.3    Sarath, G.4    Zempleni, J.5
  • 20
    • 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
  • 21
    • 0036246474 scopus 로고    scopus 로고
    • Biotin supply affects expression of biotin transporters, biotinylation of carboxylases, and metabolism of interleukin-2 in Jurkat cells
    • Manthey K.C., Griffin J.B., Zempleni J. Biotin supply affects expression of biotin transporters, biotinylation of carboxylases, and metabolism of interleukin-2 in Jurkat cells. J Nutr 2002, 132:887-892.
    • (2002) J Nutr , vol.132 , pp. 887-892
    • Manthey, K.C.1    Griffin, J.B.2    Zempleni, J.3
  • 22
    • 0028946447 scopus 로고
    • Biotin accounts for only half of the total avidin-binding substances in human serum
    • Mock D.M., Lankford G.L., Mock N.I. Biotin accounts for only half of the total avidin-binding substances in human serum. J Nutr 1995, 125:941-946.
    • (1995) J Nutr , vol.125 , pp. 941-946
    • Mock, D.M.1    Lankford, G.L.2    Mock, N.I.3
  • 23
    • 0035013946 scopus 로고    scopus 로고
    • In vivo biotin supplementation at a pharmacologic dose decreases proliferation rates of human peripheral blood mononuclear cells and cytokine release
    • Zempleni J., Helm R.M., Mock D.M. In vivo biotin supplementation at a pharmacologic dose decreases proliferation rates of human peripheral blood mononuclear cells and cytokine release. J Nutr 2001, 131:1479-1484.
    • (2001) J Nutr , vol.131 , pp. 1479-1484
    • Zempleni, J.1    Helm, R.M.2    Mock, D.M.3
  • 24
    • 44949138461 scopus 로고    scopus 로고
    • A rapid micro chromatin immunoprecipitation assay (microChIP)
    • Dahl J.A., Collas P. A rapid micro chromatin immunoprecipitation assay (microChIP). Nature Protocols 2008, 3:1032-1045.
    • (2008) Nature Protocols , vol.3 , pp. 1032-1045
    • Dahl, J.A.1    Collas, P.2
  • 25
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 27
    • 36248953882 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation: optimization, quantitative analysis and data normalization
    • Haring M., Offermann S., Danker T., Horst I., Peterhansel C., Stam M. Chromatin immunoprecipitation: optimization, quantitative analysis and data normalization. Plant methods 2007, 3:11.
    • (2007) Plant methods , vol.3 , pp. 11
    • Haring, M.1    Offermann, S.2    Danker, T.3    Horst, I.4    Peterhansel, C.5    Stam, M.6
  • 28
    • 0004044525 scopus 로고    scopus 로고
    • StatView Institute. SAS Publishing, Cary, NC
    • StatView Institute StatView Reference 1999, SAS Publishing, Cary, NC. 3rd ed.
    • (1999) StatView Reference
  • 30
    • 34247168395 scopus 로고    scopus 로고
    • Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases
    • Camporeale G., Zempleni J., Eissenberg J.C. Susceptibility to heat stress and aberrant gene expression patterns in holocarboxylase synthetase-deficient Drosophila melanogaster are caused by decreased biotinylation of histones, not of carboxylases. J Nutr 2007, 137:885-889.
    • (2007) J Nutr , vol.137 , pp. 885-889
    • Camporeale, G.1    Zempleni, J.2    Eissenberg, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.