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Journal of applied biological chemistry, v.57 no.4, 2014년, pp.379 - 386
강한철 (Department of metabolic engineering, National Academy of Agricultural Science, Rural Development Administration) , 김종범 (Department of metabolic engineering, National Academy of Agricultural Science, Rural Development Administration) , 노경희 (Department of metabolic engineering, National Academy of Agricultural Science, Rural Development Administration) , 김현욱 (Department of metabolic engineering, National Academy of Agricultural Science, Rural Development Administration) , 이경렬 (Department of metabolic engineering, National Academy of Agricultural Science, Rural Development Administration) , 김순희 (Department of metabolic engineering, National Academy of Agricultural Science, Rural Development Administration)
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Chromatin is an instructive DNA structure that can widely respond to external signals. An important change of chromatin is the modifications of histone for this regulation. There are accumulating lists of these modifications and the complexity of their action is gradually understood. It is evident t...
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| 핵심어 | 질문 | 논문에서 추출한 답변 |
|---|---|---|
| 크로마틴이란 무엇인가? | 크로마틴은 DNA 구조를 다시 결정해주는 것과 같은 존재로 각종 신호에 폭넓게 반응한다. 크로마틴의 중요한 변화는 이러한 조절을 위한 히스톤의 변이이다. | |
| 히스톤 변이는 chromatin을 재구성하는 효소들의 집합에 관여할 때 어떤 에너지를 사용하는가? | 히스톤 변이는 chromatin의 구조 조절에 관여하는 역할 이외에도 chromatin을 재구성하는 효소들의 집합에도 관여를 한다(Bannister와 Kouzarides, 2011). 이러한 경우에 효소들은 nucleosome을 재구성하기 위하여 ATP 를 분해시킨 에너지를 사용하게 된다. | |
| 히스톤의 변화의 역할은 무엇인가? | 이러한 변화들에 대한 지식이 점점 축적되고 있으며 이러한 반응의 복잡성이 점점 더 명확히 이해되고 있다. 히스톤의 변화가 대부분의 생명체의 반응에 있어서 DNA 의 발현 또는 억제를 통하여 중요한 역할을 한다는 사실이 명확해지고 있다. Nucleosome 의 표면은 각종 변화를 수용할 수 있다. |
Akasaka T, van Lohuizen M, van der Lugt N, and Mizutani-Koseki Y (2001) Mice doubly deficient for the Polycomb Group genes Mel18 and Bmi1 reveal synergy and requirement for maintenance but not initiation of Hox gene expression. Development 12, 1587-97.
Ang YS, Tsai SY, Lee DF, Monk J, Su J, and Ratnakumar K (2011) Wdr5 mediates self-renewal and reprogramming via the embryonic stem cell core transcriptional network. Cell 14, 183-97.
Bannister AJ and Kouzarides T (2011) Regulation of chromatin by histone modifications. Cell Research 21, 381-95.
Bedford MT and Clarke SG (2009) Protein arginine methylation in mammals; who, what and why. Mol Cell 3, 11-3.
Bilodeau S, Kagey MH, Frampton GM, Rahl PB, and Young RA (2009) SetDB1 contributes to repression of genes encoding developmental regulators and maintenance of ES cell state. Genes Dev 23, 2484-9.
Carninci P, Kasukawa T, Katayama S, and Gough J (2005) The transcriptional landscape of the mammalian genome. Science 30, 1559-63.
Castel SE and Martienssen RA (2013) RNA interference in the nucleus:roles for small RNAs in transcription, epigenetics and beyond. Nature Rev Genet 14,100-12.
Champagne KS and Kutateladze TG (2009) Structural insight into histone recognition by the ING PHD fingers. Curr Drug Targets 10, 432-41.
Chen Z, Zang J, and Whetstine J (2006) Structural insights into histone demethylation by JMJD2 members. Cell 125, 691-702.
Cohen-Armon M, Visochek L, and Rozensal D (2007) DNA independent PARP-1 activation by phosphorylated ERK2 increases Elk1 activity; a link to histone acetylation. Mol Cell 25, 297-308.
Cuthbert GL, Daujat S, Snowden AW, and Erdjument-Bromage H (2004) Histone deamination antagonizes arginine methylation. Cell 118, 545-53.
Dai J, Sultan S, Taylor SS, and Higgins JM (2005) The kinase haspin is required for mitotic histone H3 Thr 3 phosphorylation and normal metaphase chromosome alignment. Genes Dev 19, 472-88.
Dawson MA, Bannister AJ, and Gottgens DA (2009) JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin. Nature 461, 819-22.
Endoh M, Endo TA, Endoh T, Fujimura Y, and Ohara O (2008) Polycomb group proteins Ring1A/B are functionally linked to the core transcriptional regulatory circuitry to maintain ES cell identity. Development 135, 1513-24.
Fischle W, Tseng BS, Dormann HL, and Ueberheide BM (2005) Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature 438, 1116-22.
Gao Z, Zhang J, and Bonassio R (2012) PCGF homologs, CBX proteins, and RYBP define functionally distinct PRC1 family complexes. Mol Cell 45, 344-56.
Gehring M, Huh JH, Hsieh TF, Penterman J, and Choi Y (2006) DEMETER DNA glycosylase establishes MEDEA polycomb gene self-imprinting by allele-specific demethylation. Cell 124, 495-506.
Glaser S, Lubitz S, Loveland KL, Ohbo K, and Robb L (2009) The histone 3 lysine 4 methyltransferase, Mll2, is only required briefly in development and spermatogenesis. Epigenetics Chromatin 2, 5-11.
Golebiewska A, Atkinson SP, Lako M, and Armstrong L (2009) Epigenetic landscaping during hESC differentiation to neural cells. Stem Cells 27, 1298-308.
Hammoud SS, Nix DA, Zhang H, and Purwar J (2009) Distinctive chromatin in human sperm packages genes for embryo development. Nature 460, 473-8.
He J, Shen L, and Wan M (2013) Kdm2b maintains murine embryonic stem cell status by recruiting PRC1 complex to CpG islands of developmental genes. Nature Cell Biol 15, 373-84.
Hodawadekar SC and Marmorstein R (2007) Chemistry of acetyl transfer by histone modifying enzymes;structure, mechanism and implications for effector design. Oncogene 26, 5528-40.
Hong SH, Rampalli S, Lee JB, and McNicol J (2011) Cell fate potential of human pluripotent stem cells is encoded by histone modifications. Cell Stem Cell 9, 34-6.
Hsieh TF, Ibarra CA, Silva P, and Zemach A (2009) Genome-wide demethylation of Arabidopsis endosperm. Science 32, 1451-4.
Hu S, Xie Z, and Onishi A (2009) Profiling the human protein DNA interactome reveals ERK2 as a transcriptional repressor of interferon signaling. Cell 139, 610-22.
Huang Y, Fang J, Bedford MT, Zhang Y, and Xu RM (2006) Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312, 748-51.
Jiang H, Shukla A, Wang X, Chen WY, Bernstein BE, and Roeder RG (2011) Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains. Cell 144, 513-25.
Kim J, Daniel J, and Espejo A (2006) Tudor, MBT and chromodomains gauge the degree of lysine methylation. EMBO Rep 7, 397-403.
Krishnamoorthy T, Chen X, Govin J, and Cheung WL (2006). Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and is conserved in fly and mouse spermatogenesis. Genes Dev 20, 2580-92.
Kumar R and Rao DN (2013) Role of DNA methyltransferases in epigenetic regulation in bacteria. Subcell Biochem 61, 81-102.
Mercer TR, Dinger ME, Mariani J, and Kosik KS (2008) Noncoding RNAs in long-term memory formation. Neuroscientist 14, 434-45.
Metzger E, Wissmann M, Yin N, Muller JM, Schneider R, and Peters AH (2005) LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437, 436-9.
Morey L, Pascual G, and Cozutto L (2012) Nonoverlapping functions of the Polycomb group Cbx family of proteins in embryonic stem cells. Cell Stem Cell 10, 47-62.
Morgan HD, Dean W, Coker HA, Reik W, and Petersen-Mahrt SK (2004) Activation-induced cytidine deaminase deaminates 5-methylcytosine in DNA and is expressed in pluripotent tissues: implications for epigenetic reprogramming. J Biol Chem 279, 52353-60.
Nathan D, Ingvarsdottir K, Sterner DE, and Bylebyl GR (2006) Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive acting histone modifications. Genes Dev 20, 966-76.
Nelson CJ, Santos-Rosa H, and Kouzarides T (2006) Proline isomerization of histone H3 regulates lysine methylation and gene expression. Cell 126, 906-16.
Pasini D, Bracken A, Hansen J, Capillo M, and Helin K (2007) The polycomb group protein Suz12 is required for embryonic stem cell differentiation. Mol Cell Biol 27, 3769-79.
Pastor WA, Aravind L, and Rao A (2013) TETonic shift; biological roles of TET proteins in DNA demethylation and transcription. Nature Rev Mol Cell Biol 14, 341-56.
Peters AH, O'Carroll D, Scherthan H, and Mechtler K (2001) Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability. Cell 107, 323-37.
Popp C, Dean W, Feng S, and Cokus SJ (2010) Genome-wide erasure of DNA methylation in mouse primordial germ cells is affected by AID deficiency. Nature 463,1101-5.
Puschendorf M, Terranova R, Boutsma E, and Mao X (2008) PRC1 and Suv39h specify parental asymmetry at constitutive heterochromatin in early mouse embryos. Nat Genet 40, 411-20.
Rinn JL, Kertesz M, Wang JK, Squazzo SL, and Xu X (2007) Functional demarcation of active and silent chromatin domains in human HOX loci by noncoding RNAs. Cell 129, 1311-23.
Shen X, Liu Y, Hsu YJ, Fujiwara Y, and Kim J (2008) EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol Cell 32, 491-502.
Shilatifard A (2006) Chromatin modifications by methylation and ubiquitination; impli-cations in the regulation of gene expression. Annu Rev Biochem 75, 243-69.
Shimahara H, Hirano T, and Ohya K (2013) Nucleosome structural changes induced by binding of non-histone chromosomal proteins HMGN1 and HMGN2. FEBS 3,184-91
Shogren-Knaak M, Ishii H, Sun JM, and Pazin MJ (2006) Histone H4K16 acetylation controls chromatin structure and protein interactions. Science 311, 844-7.
Sims RJ, Chen CF, Santos-Rosa H, Kouzarides T, Patel SS, and Reinberg D (2005) Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains. J Biol Chem 280, 41789-92.
Skene PJ and Henikoff S (2013) Histone variants in pluripotency and disease. Development 140, 2513-24.
Sone M, Hayashi T, and Tarui H (2007) The mRNA-like noncoding RNA Gomafu constitutes a novel nuclear domain in a subset of neurons. J Cell Sci 120, 2498-506.
Steward MM, Lee JS, Donovan A, Wyatt M, Bernstein BE, and Shilatifard A (2006) Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes. Nat Struct Mol Biol 13, 852-54.
Tachibana M, Sugimoto K, Nozaki M, and Ueda J (2002) G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis. Genes Dev 16, 1779-91.
Tachibana M, Ueda J, Fukuda M, and Takeda N (2005) Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes Dev 19, 815-26.
Takihara Y, Tomotsune D, Shirai M, and Katoh-Fukui Y (1997) Targeted disruption of the mouse homologue of the Drosophila polyhomeotic gene leads to altered anteroposterior patterning and neural crest defects. Development 124, 3673-82.
Tavares L, Dimitrova E, and Webster J (2012) RYBP-PRC1 complexes mediate H2A ubiquity-lation at polycomb target sites independently of PRC2 and H3K27me3. Cell 148, 664-78.
Vaquero A, Scher, MB, Lee DH, and Sutton A (2006) SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes Dev 20, 1256-61.
Vermeulen M, Eberl HC, and Matarese F (2010) Quantitative interaction proteomics and genome-wide profiling of epigenetic histone marks and their readers. Cell 142, 967-80.
Walker E, Chang WY, Hunkapiller J, Cagney G, and Garcha K (2010) Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation. Cell Stem Cell 6, 153-66.
Wang Z, Zang C, and Rosenfeld JA (2008) Combinatorial patterns of histone acetylations and methylations in the human genome. Nat Genet 40, 897-903.
Wei Y, Mizzen CA, Cook RG, Gorovsky MA, and Allis CD (1998) Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Proc Natl Acad Sci USA 95, 7480-4.
Wu X, Johansen JV, and Helin K (2013) Fbxl10/Kdm2b recruits polycomb repressive complex 1 to CpG islands and regulates H2A ubiquitylation. Mol Cell 49, 1134-46.
Zachary DS and Alexander M (2013) DNA methylation; roles in mammalian development. Nat Rev Genet 14, 204-20.
Zhang Y and Reinberg D (2006) Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev 15, 2343-60.
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