메뉴 건너뛰기




Volumn 5, Issue Se, 2016, Pages

Hemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; UBIQUITIN PROTEIN LIGASE; UHRF1 PROTEIN; UNCLASSIFIED DRUG; CCAAT ENHANCER BINDING PROTEIN; DNA; DNA (CYTOSINE 5) METHYLTRANSFERASE; DNA (CYTOSINE-5-)-METHYLTRANSFERASE 1; HISTONE; PROTEIN BINDING; UHRF1 PROTEIN, HUMAN;

EID: 84986203552     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.17101     Document Type: Article
Times cited : (107)

References (59)
  • 1
    • 53649097070 scopus 로고    scopus 로고
    • Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
    • Arita K, Ariyoshi M, Tochio H, Nakamura Y, Shirakawa M. 2008. Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism. Nature 455:818–821. doi: 10.1038/nature07249
    • (2008) Nature , vol.455 , pp. 818-821
    • Arita, K.1    Ariyoshi, M.2    Tochio, H.3    Nakamura, Y.4    Shirakawa, M.5
  • 4
    • 0021086610 scopus 로고
    • Two DNA methyltransferases from murine erythroleukemia cells: Purification, sequence specificity, and mode of interaction with DNA
    • Bestor TH, Ingram VM. 1983. Two DNA methyltransferases from murine erythroleukemia cells: purification, sequence specificity, and mode of interaction with DNA. PNAS 80:5559–5563. doi: 10.1073/pnas.80.18.5559
    • (1983) PNAS , vol.80 , pp. 5559-5563
    • Bestor, T.H.1    Ingram, V.M.2
  • 5
    • 84906952904 scopus 로고    scopus 로고
    • Polycomb repressive complex 2 and H3K27me3 cooperate with H3K9 methylation to maintain heterochromatin protein 1a at chromatin
    • Boros J, Arnoult N, Stroobant V, Collet JF, Decottignies A. 2014. Polycomb repressive complex 2 and H3K27me3 cooperate with H3K9 methylation to maintain heterochromatin protein 1a at chromatin. Molecular and Cellular Biology 34:3662–3674. doi: 10.1128/MCB.00205-14
    • (2014) Molecular and Cellular Biology , vol.34 , pp. 3662-3674
    • Boros, J.1    Arnoult, N.2    Stroobant, V.3    Collet, J.F.4    Decottignies, A.5
  • 6
    • 34648833002 scopus 로고    scopus 로고
    • UHRF1 plays a role in maintaining DNA methylation in mammalian cells
    • Bostick M, Kim JK, Estève PO, Clark A, Pradhan S, Jacobsen SE. 2007. UHRF1 plays a role in maintaining DNA methylation in mammalian cells. Science 317:1760–1764. doi: 10.1126/science.1147939
    • (2007) Science , vol.317 , pp. 1760-1764
    • Bostick, M.1    Kim, J.K.2    Estève, P.O.3    Clark, A.4    Pradhan, S.5    Jacobsen, S.E.6
  • 9
    • 34948848684 scopus 로고    scopus 로고
    • E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages
    • Christensen DE, Brzovic PS, Klevit RE. 2007. E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages. Nature Structural & Molecular Biology 14:941–948. doi: 10.1038/nsmb1295
    • (2007) Nature Structural & Molecular Biology , vol.14 , pp. 941-948
    • Christensen, D.E.1    Brzovic, P.S.2    Klevit, R.E.3
  • 10
    • 84920024622 scopus 로고    scopus 로고
    • Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal
    • DaRosa PA, Wang Z, Jiang X, Pruneda JN, Cong F, Klevit RE, Xu W. 2015. Allosteric activation of the RNF146 ubiquitin ligase by a poly(ADP-ribosyl)ation signal. Nature 517:223–226. doi: 10.1038/nature13826
    • (2015) Nature , vol.517 , pp. 223-226
    • Darosa, P.A.1    Wang, Z.2    Jiang, X.3    Pruneda, J.N.4    Cong, F.5    Klevit, R.E.6    Xu, W.7
  • 14
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. 2008. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134:995–1006. doi: 10.1016/j.cell.2008.07.022
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 18
    • 33644849860 scopus 로고    scopus 로고
    • Accuracy of DNA methylation pattern preservation by the Dnmt1 methyltransferase
    • Goyal R, Reinhardt R, Jeltsch A. 2006. Accuracy of DNA methylation pattern preservation by the Dnmt1 methyltransferase. Nucleic Acids Research 34:1182–1188. doi: 10.1093/nar/gkl002
    • (2006) Nucleic Acids Research , vol.34 , pp. 1182-1188
    • Goyal, R.1    Reinhardt, R.2    Jeltsch, A.3
  • 20
    • 53649089723 scopus 로고    scopus 로고
    • The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix
    • Hashimoto H, Horton JR, Zhang X, Bostick M, Jacobsen SE, Cheng X. 2008. The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix. Nature 455:826–829. doi: 10.1038/nature07280
    • (2008) Nature , vol.455 , pp. 826-829
    • Hashimoto, H.1    Horton, J.R.2    Zhang, X.3    Bostick, M.4    Jacobsen, S.E.5    Cheng, X.6
  • 21
    • 9144256125 scopus 로고    scopus 로고
    • The Dnmt1 DNA-(Cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites
    • Hermann A, Goyal R, Jeltsch A. 2004. The Dnmt1 DNA-(cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites. Journal of Biological Chemistry 279:48350–48359. doi: 10.1074/jbc.M403427200
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 48350-48359
    • Hermann, A.1    Goyal, R.2    Jeltsch, A.3
  • 22
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA. 1994. NMR View: A computer program for the visualization and analysis of NMR data. Journal of Biomolecular NMR 4:603–614. doi: 10.1007/BF00404272
    • (1994) Journal of Biomolecular NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 23
    • 54949129419 scopus 로고    scopus 로고
    • ProteoWizard: Open source software for rapid proteomics tools development
    • Kessner D, Chambers M, Burke R, Agus D, Mallick P. 2008. ProteoWizard: open source software for rapid proteomics tools development. Bioinformatics 24:2534–2536. doi: 10.1093/bioinformatics/btn323
    • (2008) Bioinformatics , vol.24 , pp. 2534-2536
    • Kessner, D.1    Chambers, M.2    Burke, R.3    Agus, D.4    Mallick, P.5
  • 25
    • 84925938228 scopus 로고    scopus 로고
    • UHRF1 is a sensor for DNA interstrand crosslinks and recruits FANCD2 to initiate the Fanconi anemia pathway
    • Liang CC, Zhan B, Yoshikawa Y, Haas W, Gygi SP, Cohn MA. 2015. UHRF1 is a sensor for DNA interstrand crosslinks and recruits FANCD2 to initiate the Fanconi anemia pathway. Cell Reports 10:1947–1956. doi: 10.1016/j.celrep.2015.02.053
    • (2015) Cell Reports , vol.10 , pp. 1947-1956
    • Liang, C.C.1    Zhan, B.2    Yoshikawa, Y.3    Haas, W.4    Gygi, S.P.5    Cohn, M.A.6
  • 26
    • 84865337735 scopus 로고    scopus 로고
    • Examining histone posttranslational modification patterns by high-resolution mass spectrometry
    • Lin S, Garcia BA. 2012. Examining histone posttranslational modification patterns by high-resolution mass spectrometry. Methods in Enzymology 512:3–28. doi: 10.1016/B978-0-12-391940-3.00001-9
    • (2012) Methods in Enzymology , vol.512 , pp. 3-28
    • Lin, S.1    Garcia, B.A.2
  • 27
    • 84875883306 scopus 로고    scopus 로고
    • UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9
    • Liu X, Gao Q, Li P, Zhao Q, Zhang J, Li J, Koseki H, Wong J. 2013. UHRF1 targets DNMT1 for DNA methylation through cooperative binding of hemi-methylated DNA and methylated H3K9. Nature Communications 4:1563. doi: 10.1038/ncomms2562
    • (2013) Nature Communications , vol.4
    • Liu, X.1    Gao, Q.2    Li, P.3    Zhao, Q.4    Zhang, J.5    Li, J.6    Koseki, H.7    Wong, J.8
  • 29
    • 84857411167 scopus 로고    scopus 로고
    • A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-Acylurea approach
    • Mahto SK, Howard CJ, Shimko JC, Ottesen JJ. 2011. A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-Acylurea approach. ChemBioChem 12:2488–2494. doi: 10.1002/cbic.201100472
    • (2011) Chembiochem , vol.12 , pp. 2488-2494
    • Mahto, S.K.1    Howard, C.J.2    Shimko, J.C.3    Ottesen, J.J.4
  • 31
    • 84959888769 scopus 로고    scopus 로고
    • USP7 enforces heterochromatinization of p53 target promoters by protecting SUV39H1 from MDM2-mediated degradation
    • Mungamuri SK, Qiao RF, Yao S, Manfredi JJ, Gu W, Aaronson SA. 2016. USP7 enforces heterochromatinization of p53 target promoters by protecting SUV39H1 from MDM2-mediated degradation. Cell Reports 14:2528–2537. doi: 10.1016/j.celrep.2016.02.049
    • (2016) Cell Reports , vol.14 , pp. 2528-2537
    • Mungamuri, S.K.1    Qiao, R.F.2    Yao, S.3    Manfredi, J.J.4    Gu, W.5    Aaronson, S.A.6
  • 34
    • 84961711865 scopus 로고    scopus 로고
    • Reading between the lines: "ADD"-ing histone and DNA methylation marks toward a new epigenetic "Sum"
    • Noh KM, Allis CD, Li H. 2016. Reading between the lines: "ADD"-ing histone and DNA methylation marks toward a new epigenetic "Sum". ACS Chemical Biology 11:554–563. doi: 10.1021/acschembio.5b00830
    • (2016) ACS Chemical Biology , vol.11 , pp. 554-563
    • Noh, K.M.1    Allis, C.D.2    Li, H.3
  • 35
    • 79952407243 scopus 로고    scopus 로고
    • Ubiquitin in motion: Structural studies of the ubiquitin-conjugating enzyme~ubiquitin conjugate
    • Pruneda JN, Stoll KE, Bolton LJ, Brzovic PS, Klevit RE. 2011. Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme~ubiquitin conjugate. Biochemistry 50:1624–1633. doi: 10.1021/bi101913m
    • (2011) Biochemistry , vol.50 , pp. 1624-1633
    • Pruneda, J.N.1    Stoll, K.E.2    Bolton, L.J.3    Brzovic, P.S.4    Klevit, R.E.5
  • 36
    • 79952407243 scopus 로고    scopus 로고
    • Ubiquitin in motion: Structural studies of the ubiquitin-conjugating enzyme~ubiquitin conjugate
    • Pruneda JN, Stoll KE, Bolton LJ, Brzovic PS, Klevit RE. 2011b. Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme~ubiquitin conjugate. Biochemistry 50:1624–1633. doi: 10.1021/bi101913m
    • (2011) Biochemistry , vol.50 , pp. 1624-1633
    • Pruneda, J.N.1    Stoll, K.E.2    Bolton, L.J.3    Brzovic, P.S.4    Klevit, R.E.5
  • 40
    • 0034814802 scopus 로고    scopus 로고
    • A novel single-molecule study to determine protein–protein association constants
    • Ratcliff GC, Erie DA. 2001. A novel single-molecule study to determine protein–protein association constants. Journal of the American Chemical Society 123:5632–5635. doi: 10.1021/ja005750n
    • (2001) Journal of the American Chemical Society , vol.123 , pp. 5632-5635
    • Ratcliff, G.C.1    Erie, D.A.2
  • 42
    • 84878838423 scopus 로고    scopus 로고
    • Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation
    • Rothbart SB, Dickson BM, Ong MS, Krajewski K, Houliston S, Kireev DB, Arrowsmith CH, Strahl BD. 2013. Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation. Genes & Development 27:1288–1298. doi: 10.1101/gad.220467.113
    • (2013) Genes & Development , vol.27 , pp. 1288-1298
    • Rothbart, S.B.1    Dickson, B.M.2    Ong, M.S.3    Krajewski, K.4    Houliston, S.5    Kireev, D.B.6    Arrowsmith, C.H.7    Strahl, B.D.8
  • 43
    • 84904541089 scopus 로고    scopus 로고
    • Interpreting the language of histone and DNA modifications
    • Rothbart SB, Strahl BD. 2014. Interpreting the language of histone and DNA modifications. Biochimica Et Biophysica Acta 1839:627–643. doi: 10.1016/j.bbagrm.2014.03.001
    • (2014) Biochimica Et Biophysica Acta , vol.1839 , pp. 627-643
    • Rothbart, S.B.1    Strahl, B.D.2
  • 46
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha A, Deshaies RJ. 2008. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Molecular Cell 32:21–31. doi: 10.1016/j.molcel.2008.08.021
    • (2008) Molecular Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 47
    • 81755162787 scopus 로고    scopus 로고
    • Twists and turns in ubiquitin-like protein conjugation cascades
    • Schulman BA. 2011. Twists and turns in ubiquitin-like protein conjugation cascades. Protein Science 20:1941–1954. doi: 10.1002/pro.750
    • (2011) Protein Science , vol.20 , pp. 1941-1954
    • Schulman, B.A.1
  • 49
    • 0038047672 scopus 로고    scopus 로고
    • A native peptide ligation strategy for deciphering nucleosomal histone modifications
    • Shogren-Knaak MA, Fry CJ, Peterson CL. 2003. A native peptide ligation strategy for deciphering nucleosomal histone modifications. Journal of Biological Chemistry 278:15744–15748. doi: 10.1074/jbc.M301445200
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 15744-15748
    • Shogren-Knaak, M.A.1    Fry, C.J.2    Peterson, C.L.3
  • 50
    • 84961775708 scopus 로고    scopus 로고
    • Reading the combinatorial histone language
    • Su Z, Denu JM. 2016. Reading the combinatorial histone language. ACS Chemical Biology 11:564–574. doi: 10.1021/acschembio.5b00864
    • (2016) ACS Chemical Biology , vol.11 , pp. 564-574
    • Su, Z.1    Denu, J.M.2
  • 52
    • 84934444524 scopus 로고    scopus 로고
    • Expression and purification of soluble His(6)-tagged TEV protease
    • Tropea JE, Cherry S, Waugh DS. 2009. Expression and purification of soluble His(6)-tagged TEV protease. Methods in Molecular Biology 498:297–307. doi: 10.1007/978-1-59745-196-3_19
    • (2009) Methods in Molecular Biology , vol.498 , pp. 297-307
    • Tropea, J.E.1    Cherry, S.2    Waugh, D.S.3
  • 53
    • 84940479138 scopus 로고    scopus 로고
    • Regulating the regulators: Recent revelations in the control of E3 ubiquitin ligases
    • Vittal V, Stewart MD, Brzovic PS, Klevit RE. 2015. Regulating the regulators: recent revelations in the control of E3 ubiquitin ligases. Journal of Biological Chemistry 290:21244–21251. doi: 10.1074/jbc.R115.675165
    • (2015) Journal of Biological Chemistry , vol.290 , pp. 21244-21251
    • Vittal, V.1    Stewart, M.D.2    Brzovic, P.S.3    Klevit, R.E.4
  • 54
    • 79551493745 scopus 로고    scopus 로고
    • E2s: Structurally economical and functionally replete
    • Wenzel DM, Stoll KE, Klevit RE. 2011. E2s: structurally economical and functionally replete. Biochemical Journal 433:31–42. doi: 10.1042/BJ20100985
    • (2011) Biochemical Journal , vol.433 , pp. 31-42
    • Wenzel, D.M.1    Stoll, K.E.2    Klevit, R.E.3
  • 59
    • 84957547988 scopus 로고    scopus 로고
    • Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation
    • Zhou L, Holt MT, Ohashi N, Zhao A, Müller MM, Wang B, Muir TW. 2016. Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation. Nature Communications 7:10589. doi: 10.1038/ncomms10589
    • (2016) Nature Communications , vol.7
    • Zhou, L.1    Holt, M.T.2    Ohashi, N.3    Zhao, A.4    Müller, M.M.5    Wang, B.6    Muir, T.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.