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NTIS 바로가기Molecular and cellular biology, v.21 no.1, 2001년, pp.196 - 208
Fernández, Luis A. (Howard Hughes Medical Institute and Department of Microbiology and Immunology, University of California, San Francisco, California 94143) , Winkler, Michael (Howard Hughes Medical Institute and Department of Microbiology and Immunology, University of California, San Francisco, California 94143) , Grosschedl, Rudolf (Howard Hughes Medical Institute and Department of Microbiology and Immunology, University of California, San Francisco, California 94143)
ABSTRACT Nuclear matrix attachment regions (MARs), which flank the immunoglobulin μ heavy-chain enhancer on either side, are required for the activation of the distal variable-region (V H ) promoter in transgenic mice. Previously, we have shown that the MARs extend a local domain of chromatin acc...
Current protocols in molecular biology. Ausubel F. M. 1993
Bannister, Andrew J., Kouzarides, Tony. The CBP co-activator is a histone acetyltransferase. Nature, vol.384, no.6610, 641-643.
Beckmann, H, Su, L K, Kadesch, T. TFE3: a helix-loop-helix protein that activates transcription through the immunoglobulin enhancer muE3 motif.. Genes & development, vol.4, no.2, 167-179.
Belmont, Andrew S, Dietzel, Steffen, Nye, Anne C, Strukov, Yuri G, Tumbar, Tudorita. Large-scale chromatin structure and function. Current opinion in cell biology, vol.11, no.3, 307-311.
Bhattacharya, Sanjoy K., Ramchandani, Shyam, Cervoni, Nadia, Szyf, Moshe. A mammalian protein with specific demethylase activity for mCpG DNA. Nature, vol.397, no.6720, 579-583.
Blackwood, Elizabeth M., Kadonaga, James T.. Going the Distance: A Current View of Enhancer Action. Science, vol.281, no.5373, 60-63.
Bode, J, Kohwi, Y, Dickinson, L, Joh, T, Klehr, D, Mielke, C, Kohwi-Shigematsu, T. Biological significance of unwinding capability of nuclear matrix-associating DNAs. Science, vol.255, no.5041, 195-197.
Brehm, Alexander, Miska, Eric A., McCance, Dennis J., Reid, Juliet L., Bannister, Andrew J., Kouzarides, Tony. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature, vol.391, no.6667, 597-601.
Brown, Christine E, Lechner, Thomas, Howe, LeAnn, Workman, Jerry L. The many HATs of transcription coactivators. Trends in biochemical sciences, vol.25, no.1, 15-19.
Brownell, James E, Zhou, Jianxin, Ranalli, Tamara, Kobayashi, Ryuji, Edmondson, Diane G, Roth, Sharon Y, Allis, C.David. Tetrahymena Histone Acetyltransferase A: A Homolog to Yeast Gcn5p Linking Histone Acetylation to Gene Activation. Cell, vol.84, no.6, 843-851.
Chen, Hongwu, Lin, Richard J, Schiltz, R.Louis, Chakravarti, Debabrata, Nash, Alyssa, Nagy, Laszlo, Privalsky, Martin L, Nakatani, Yoshihiro, Evans, Ronald M. Nuclear Receptor Coactivator ACTR Is a Novel Histone Acetyltransferase and Forms a Multimeric Activation Complex with P/CAF and CBP/p300. Cell, vol.90, no.3, 569-580.
Chomczynski, Piotr, Sacchi, Nicoletta. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical biochemistry, vol.162, no.1, 156-159.
Cirillo, Lisa Ann, Zaret, Kenneth S. An Early Developmental Transcription Factor Complex that Is More Stable on Nucleosome Core Particles Than on Free DNA. Molecular cell, vol.4, no.6, 961-969.
Cockerill, P.N., Yuen, M.H., Garrard, W.T.. The enhancer of the immunoglobulin heavy chain locus is flanked by presumptive chromosomal loop anchorage elements.. The Journal of biological chemistry, vol.262, no.11, 5394-5397.
Trends Genet. Crane-Robinson C. 477 14 1998 10.1016/S0168-9525(98)01621-7
Curr. Opin. Genet. Dev. Dillon N. 260 4 1994 10.1016/S0959-437X(05)80053-X
Ephrussi, A, Church, GM, Tonegawa, S, Gilbert, W. B lineage--specific interactions of an immunoglobulin enhancer with cellular factors in vivo. Science, vol.227, no.4683, 134-140.
Ernst, Patricia, Smale, Stephen T.. Combinatorial regulation of transcription II: the immunoglobulin μ heavy chain gene. Immunity, vol.2, no.5, 427-438.
Felsenfeld, G, Boyes, J, Chung, J, Clark, D, Studitsky, V. Chromatin structure and gene expression.. Proceedings of the National Academy of Sciences of the United States of America, vol.93, no.18, 9384-9388.
Forrester, WC, van Genderen, C, Jenuwein, T, Grosschedl, R. Dependence of enhancer-mediated transcription of the immunoglobulin mu gene on nuclear matrix attachment regions. Science, vol.265, no.5176, 1221-1225.
Garrity, P A, Wold, B J. Effects of different DNA polymerases in ligation-mediated PCR: enhanced genomic sequencing and in vivo footprinting.. Proceedings of the National Academy of Sciences of the United States of America, vol.89, no.3, 1021-1025.
Grosveld, F.. Activation by locus control regions?. Current opinion in genetics & development, vol.9, no.2, 152-157.
Grunstein, Michael. Histone acetylation in chromatin structure and transcription. Nature, vol.389, no.6649, 349-352.
Hart, Craig M, Laemmli, Ulrich K. Facilitation of chromatin dynamics by SARs. Current opinion in genetics & development, vol.8, no.5, 519-525.
Hebbes, T.R., Clayton, A.L., Thorne, A.W., Crane-Robinson, C.. Core histone hyperacetylation co-maps with generalized DNase I sensitivity in the chicken beta-globin chromosomal domain.. The EMBO journal, vol.13, no.8, 1823-1830.
Herrera, Julio E., West, Katherine L., Schiltz, R. Louis, Nakatani, Yoshihiro, Bustin, Michael. Histone H1 Is a Specific Repressor of Core Histone Acetylation in Chromatin. Molecular and cellular biology, vol.20, no.2, 523-529.
Herrscher, R F, Kaplan, M H, Lelsz, D L, Das, C, Scheuermann, R, Tucker, P W. The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family.. Genes & development, vol.9, no.24, 3067-3082.
Jenuwein, T, Grosschedl, R. Complex pattern of immunoglobulin mu gene expression in normal and transgenic mice: nonoverlapping regulatory sequences govern distinct tissue specificities.. Genes & development, vol.5, no.6, 932-943.
Jenuwein, T, Forrester, W C, Qiu, R G, Grosschedl, R. The immunoglobulin mu enhancer core establishes local factor access in nuclear chromatin independent of transcriptional stimulation.. Genes & development, vol.7, no.10, 2016-2032.
Jenuwein, Thomas, Forrester, William C., Fernández-Herrero, Luis A., Laible, Götz, Dull, Maude, Grosschedl, Rudolf. Extension of chromatin accessibility by nuclear matrix attachment regions. Nature, vol.385, no.6613, 269-272.
Jones, Peter L., Veenstra, Gert Jan C., Wade, Paul A., Vermaak, Danielle, Kass, Stefan U., Landsberger, Nicoletta, Strouboulis, John, Wolffe, Alan P.. Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription. Nature genetics, vol.19, no.2, 187-191.
J. Immunol. Kashiwamura S. 337 145 1990 10.4049/jimmunol.145.1.337
10.1002/(SICI)1520-6408(1998)22:1<65::AID-DVG7>3.0.CO;2-5
Kioussis, Dimitris, Festenstein, Richard. Locus control regions: overcoming heterochromatin-induced gene inactivation in mammals. Current opinion in genetics & development, vol.7, no.5, 614-619.
Kirillov, Andrei, Kistler, Barbara, Mostoslavsky, Raul, Cedar, Howard, Wirth, Thomas, Bergman, Yehudit. A role for nuclear NF-κB in B-cell-specific demethylation of the Igκ locus. Nature genetics, vol.13, no.4, 435-441.
Klehr, D., Maass, K., Bode, Juergen. Scaffold-attached regions from the human interferon .beta. domain can be used to enhance the stable expression of genes under the control of various promoters. Biochemistry, vol.30, no.5, 1264-1270.
Kuo, M H, Zhou, J, Jambeck, P, Churchill, M E, Allis, C D. Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo.. Genes & development, vol.12, no.5, 627-639.
Laemmli, U.K., Kas, E., Poljak, L., Adachi, Y.. Scaffold-associated regions: cis-acting determinants of chromatin structural loops and functional domains. Current opinion in genetics & development, vol.2, no.2, 275-285.
Lennon, Gregory G., Perry, Robert P.. Cμ-containing transcripts initiate heterogeneously within the IgH enhancer region and contain a novel 5′-nontranslatable exon. Nature, vol.318, no.6045, 475-478.
Ling, X, Harkness, T A, Schultz, M C, Fisher-Adams, G, Grunstein, M. Yeast histone H3 and H4 amino termini are important for nucleosome assembly in vivo and in vitro: redundant and position-independent functions in assembly but not in gene regulation.. Genes & development, vol.10, no.6, 686-699.
Luger, Karolin, Richmond, Timothy J. The histone tails of the nucleosome. Current opinion in genetics & development, vol.8, no.2, 140-146.
Luger, Karolin, Mäder, Armin W., Richmond, Robin K., Sargent, David F., Richmond, Timothy J.. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature, vol.389, no.6648, 251-260.
McMurry, Michelle Taylor, Krangel, Michael S.. A Role for Histone Acetylation in the Developmental Regulation of V(D)J Recombination. Science, vol.287, no.5452, 495-498.
Misteli, Tom, Spector, David L. The cellular organization of gene expression. Current opinion in cell biology, vol.10, no.3, 323-331.
Nan, Xinsheng, Campoy, F.Javier, Bird, Adrian. MeCP2 Is a Transcriptional Repressor with Abundant Binding Sites in Genomic Chromatin. Cell, vol.88, no.4, 471-481.
Nan, Xinsheng, Ng, Huck-Hui, Johnson, Colin A., Laherty, Carol D., Turner, Bryan M., Eisenman, Robert N., Bird, Adrian. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature, vol.393, no.6683, 386-389.
Nelsen, B, Tian, G, Erman, B, Gregoire, J, Maki, R, Graves, B, Sen, R. Regulation of lymphoid-specific immunoglobulin mu heavy chain gene enhancer by ETS-domain proteins. Science, vol.261, no.5117, 82-86.
Ng, Huck-Hui, Jeppesen, Peter, Bird, Adrian. Active Repression of Methylated Genes by the Chromosomal Protein MBD1. Molecular and cellular biology, vol.20, no.4, 1394-1406.
Nikolajczyk, Barbara S, Sanchez, J.Aquiles, Sen, Ranjan. ETS Protein–Dependent Accessibility Changes at the Immunoglobulin μ Heavy Chain Enhancer. Immunity, vol.11, no.1, 11-20.
Mol. Cell. Biol. Nikolajczyk B. S. 3527 17 1997 10.1128/MCB.17.7.3527
O'Neill, L. P., Turner, B. M.. Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner.. The EMBO journal, vol.14, no.16, 3946-3957.
Orlando, Valerio, Strutt, Helen, Paro, Renato. Analysis of Chromatin Structure byin VivoFormaldehyde Cross-Linking. Methods, vol.11, no.2, 205-214.
Parekh, Bhavin S, Maniatis, Tom. Virus Infection Leads to Localized Hyperacetylation of Histones H3 and H4 at the IFN-β Promoter. Molecular cell, vol.3, no.1, 125-129.
Pederson, T.. Thinking about a nuclear matrix. Journal of molecular biology, vol.277, no.2, 147-159.
Mol. Cell. Biol. Phi-Van L. 2302 10 1990
Pikaart, Michael J., Recillas-Targa, Félix, Felsenfeld, Gary. Loss of transcriptional activity of a transgene is accompanied by DNA methylation and histone deacetylation and is prevented by insulators. Genes & development, vol.12, no.18, 2852-2862.
Pogo, B G, Allfrey, V G, Mirsky, A E. RNA synthesis and histone acetylation during the course of gene activation in lymphocytes.. Proceedings of the National Academy of Sciences of the United States of America, vol.55, no.4, 805-812.
Ptashne, Mark, Gann, Alexander. Transcriptional activation by recruitment. Nature, vol.386, no.6625, 569-577.
Mol. Cell. Biol. Reitman M. 3990 13 1993
A quantitative assay for transformation of bone marrow cells by Abelson murine leukemia virus. The Journal of experimental medicine, vol.143, no.6, 1453-1463.
Sauter, Patrick, Matthias, Patrick. Coactivator OBF-1 Makes Selective Contacts with Both the POU-Specific Domain and the POU Homeodomain and Acts as a Molecular Clamp on DNA. Molecular and cellular biology, vol.18, no.12, 7397-7409.
Genes Dev. Scheuermann R. 1255 3 1989 10.1101/gad.3.8.1255
Schübeler, Dirk, Francastel, Claire, Cimbora, Daniel M., Reik, Andreas, Martin, David I.K., Groudine, Mark. Nuclear localization and histone acetylation: a pathway for chromatin opening and transcriptional activation of the human β-globin locus. Genes & development, vol.14, no.8, 940-950.
Sealy, L, Chalkley, R. DNA associated with hyperacetylated histone is preferentially digested by DNase I.. Nucleic acids research, vol.5, no.6, 1863-1876.
Sen, R., Baltimore, D.. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell, vol.46, no.5, 705-716.
Sheridan, Philip L., Mayall, Timothy P., Verdin, Eric, Jones, Katherine A.. Histone acetyltransferases regulate HIV-1 enhancer activity in vitro. Genes & development, vol.11, no.24, 3327-3340.
Struhl, K. Histone acetylation and transcriptional regulatory mechanisms.. Genes & development, vol.12, no.5, 599-606.
Mol. Cell. Biol. Su L. 2619 10 1990
van Holde, K, Zlatanova, J. What determines the folding of the chromatin fiber?. Proceedings of the National Academy of Sciences of the United States of America, vol.93, no.20, 10548-10555.
Varga-Weisz, Patrick D, Becker, Peter B. Chromatin-remodeling factors: machines that regulate?. Current opinion in cell biology, vol.10, no.3, 346-353.
Vettese-Dadey, M., Grant, P. A., Hebbes, T. R., Crane- Robinson, C., Allis, C. D., Workman, J. L.. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.. The EMBO journal, vol.15, no.10, 2508-2518.
Vidali, G, Boffa, L C, Bradbury, E M, Allfrey, V G. Butyrate suppression of histone deacetylation leads to accumulation of multiacetylated forms of histones H3 and H4 and increased DNase I sensitivity of the associated DNA sequences.. Proceedings of the National Academy of Sciences of the United States of America, vol.75, no.5, 2239-2243.
Vitolo, Joseph M., Thiriet, Christophe, Hayes, Jeffrey J.. The H3-H4 N-Terminal Tail Domains Are the Primary Mediators of Transcription Factor IIIA Access to 5S DNA within a Nucleosome. Molecular and cellular biology, vol.20, no.6, 2167-2175.
Wade, Paul A., Wolffe, Alan P.. Transcriptional regulation: SWItching circuitry. Current biology : CB, vol.9, no.6, R221-R224.
Wang, Zhiyong, Goldstein, Adrian, Zong, Rui-Ting, Lin, Danjun, Neufeld, Ellis J., Scheuermann, Richard H., Tucker, Philip W.. Cux/CDP Homeoprotein Is a Component of NF-μNR and Represses the Immunoglobulin Heavy Chain Intronic Enhancer by Antagonizing the Bright Transcription Activator. Molecular and cellular biology, vol.19, no.1, 284-295.
Wasylyk, C., Wasylyk, B.. The immunoglobulin heavy-chain B-lymphocyte enhancer efficiently stimulates transcription in non-lymphoid cells.. The EMBO journal, vol.5, no.3, 553-560.
Weitzel, Joachim M., Buhrmester, Hartmut, Strätling, Wolf H.. Chicken MAR-Binding Protein ARBP Is Homologous to Rat Methyl-CpG-Binding Protein MeCP2. Molecular and cellular biology, vol.17, no.9, 5656-5666.
Yamamoto, Hitomi, Kihara-Negishi, Fumiko, Yamada, Toshiyuki, Hashimoto, Yoshiyuki, Oikawa, Tsuneyuki. Physical and functional interactions between the transcription factor PU.1 and the coactivator CBP. Oncogene, vol.18, no.7, 1495-1501.
Zhao, K., Käs, E., Gonzalez, E., Laemmli, U.K.. SAR-dependent mobilization of histone H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin.. The EMBO journal, vol.12, no.8, 3237-3247.
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