메뉴 건너뛰기




Volumn 23, Issue 2, 2013, Pages 331-340

PUB-NChIP-"in vivo biotinylation" approach to study chromatin in proximity to a protein of interest

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2AZ; RAD18 PROTEIN;

EID: 84873387462     PISSN: 10889051     EISSN: 15495469     Source Type: Journal    
DOI: 10.1101/gr.134874.111     Document Type: Article
Times cited : (23)

References (44)
  • 1
    • 37249031844 scopus 로고    scopus 로고
    • Msc1 acts through histone h2a.z to promote chromosome stability in schizosaccharomyces pombe
    • Ahmed S, Dul B, Qiu X, Walworth NC. 2007. Msc1 acts through histone H2A.Z to promote chromosome stability in Schizosaccharomyces pombe. Genetics 177: 1487-1497.
    • (2007) Genetics , vol.177 , pp. 1487-1497
    • Ahmed, S.1    Dul, B.2    Qiu, X.3    Walworth, N.C.4
  • 2
    • 79959947909 scopus 로고    scopus 로고
    • Chromatin response to dna double-strand break damage
    • Bao Y. 2011. Chromatin response to DNA double-strand break damage. Epigenomics 3: 307-321.
    • (2011) Epigenomics , vol.3 , pp. 307-321
    • Bao, Y.1
  • 3
    • 1242316281 scopus 로고    scopus 로고
    • Chip-chip: Considerations for the design, analysis, and application of genome-wide chromatin immunoprecipitation experiments
    • Buck MJ, Lieb JD. 2004. ChIP-chip: Considerations for the design, analysis, and application of genome-wide chromatin immunoprecipitation experiments. Genomics 83: 349-360.
    • (2004) Genomics , vol.83 , pp. 349-360
    • Buck, M.J.1    Lieb, J.D.2
  • 4
    • 0035336967 scopus 로고    scopus 로고
    • Histone h2a variants and the inactive x chromosome: Identification of a second macroh2a variant
    • Chadwick BP, Willard HF. 2001a. Histone H2A variants and the inactive X chromosome: Identification of a second macroH2A variant. Hum Mol Genet 10: 1101-1113.
    • (2001) Hum Mol Genet , vol.10 , pp. 1101-1113
    • Chadwick, B.P.1    Willard, H.F.2
  • 5
    • 0035931749 scopus 로고    scopus 로고
    • A novel chromatin protein, distantly related to histone h2a, is largely excluded from the inactive x chromosome
    • Chadwick BP, Willard HF. 2001b. A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. J Cell Biol 152: 375-384.
    • (2001) J Cell Biol , vol.152 , pp. 375-384
    • Chadwick, B.P.1    Willard, H.F.2
  • 6
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroh2a1 is concentrated in the inactive x chromosome of female mammals
    • Costanzi C, Pehrson Jr. 1998. Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393: 599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 7
    • 47749105733 scopus 로고    scopus 로고
    • Protein-protein interaction detection in vitro and in cells by proximity biotinylation
    • Fernandez-Suarez M, Chen TS, Ting AY. 2008. Protein-protein interaction detection in vitro and in cells by proximity biotinylation. J Am Chem Soc 130: 9251-9253.
    • (2008) J Am Chem Soc , vol.130 , pp. 9251-9253
    • Fernandez-Suarez, M.1    Chen, T.S.2    Ting, A.Y.3
  • 9
    • 33747831899 scopus 로고    scopus 로고
    • Damid: Mapping of in vivo protein-genome interactions using tethered dna adenine methyltransferase
    • Greil F, Moorman C, van Steensel B. 2006. DamID: Mapping of in vivo protein-genome interactions using tethered DNA adenine methyltransferase. Methods Enzymol 410: 342-359.
    • (2006) Methods Enzymol , vol.410 , pp. 342-359
    • Greil, F.1    Moorman, C.2    Van Steensel, B.3
  • 13
  • 14
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. 2001. Translating the histone code. Science 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 15
    • 59649124496 scopus 로고    scopus 로고
    • Chromosome-wide rad51 spreading and sumo-h2a.z-dependent chromosome fixation in response to a persistent dna double-strand break
    • KalocsayM, Hiller NJ, Jentsch S. 2009. Chromosome-wide Rad51 spreading and SUMO-H2A.Z-dependent chromosome fixation in response to a persistent DNA double-strand break. Mol Cell 33: 335-343.
    • (2009) Mol Cell , vol.33 , pp. 335-343
    • Kalocsay, M.1    Hiller, N.J.2    Jentsch, S.3
  • 16
    • 2442417331 scopus 로고    scopus 로고
    • Interaction of human dna polymerase h with monoubiquitinated pcna: A possible mechanism for the polymerase switch in response to dna damage
    • Kannouche PL, Wing J, Lehmann AR. 2004. Interaction of human DNA polymerase h with monoubiquitinated PCNA: A possible mechanism for the polymerase switch in response to DNA damage. Mol Cell 14: 491-500.
    • (2004) Mol Cell , vol.14 , pp. 491-500
    • Kannouche, P.L.1    Wing, J.2    Lehmann, A.R.3
  • 17
    • 79955012081 scopus 로고    scopus 로고
    • Drosophila histone h2a variant (h2av) controls poly(adp-ribose) polymerase 1 (parp1) activation in chromatin
    • Kotova E, Lodhi N, Jarnik M, Pinnola AD, Ji Y, Tulin AV. 2011. Drosophila histone H2A variant (H2Av) controls poly(ADP-ribose) polymerase 1 (PARP1) activation in chromatin. Proc Natl Acad Sci 108: 6205-6210.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 6205-6210
    • Kotova, E.1    Lodhi, N.2    Jarnik, M.3    Pinnola, A.D.4    Ji, Y.5    Tulin, A.V.6
  • 20
    • 66149100528 scopus 로고    scopus 로고
    • A novel proteomics approach for the discovery of chromatin-associated protein networks
    • Lambert JP, Mitchell L, Rudner A, Baetz K, Figeys D. 2009. A novel proteomics approach for the discovery of chromatin-associated protein networks. Mol Cell Proteomics 8: 870-882.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 870-882
    • Lambert, J.P.1    Mitchell, L.2    Rudner, A.3    Baetz, K.4    Figeys, D.5
  • 21
    • 0036712095 scopus 로고    scopus 로고
    • Dna double-strand breakinduced phosphorylation of drosophila histone variant h2av helps prevent radiation-induced apoptosis
    • Madigan JP, Chotkowski HL, Glaser RL. 2002. DNA double-strand breakinduced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis. Nucleic Acids Res 30: 3698-3705.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3698-3705
    • Madigan, J.P.1    Chotkowski, H.L.2    Glaser, R.L.3
  • 22
    • 34249066085 scopus 로고    scopus 로고
    • Pcna, the maestro of the replication fork
    • Moldovan GL, Pfander B, Jentsch S. 2007. PCNA, the maestro of the replication fork. Cell 129: 665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 23
    • 77957889181 scopus 로고    scopus 로고
    • The swr1 histone replacement complex causes genetic instability and genomewide transcription misregulation in the absence of h2a.z
    • doi: 10.1371/journal.pone.0012143
    • Morillo-Huesca M, Clemente-Ruiz M, Andujar E, Prado F. 2010. The SWR1 histone replacement complex causes genetic instability and genomewide transcription misregulation in the absence of H2A.Z. PLoS ONE 5: e12143. doi: 10.1371/journal.pone.0012143.
    • (2010) PLoS ONE , vol.5
    • Morillo-Huesca, M.1    Clemente-Ruiz, M.2    Andujar, E.3    Prado, F.4
  • 25
    • 0041668072 scopus 로고    scopus 로고
    • Immunoprecipitation of native chromatin: Nchip
    • O'Neill LP, Turner BM. 2003. Immunoprecipitation of native chromatin: NChIP. Methods 31: 76-82.
    • (2003) Methods , vol.31 , pp. 76-82
    • O'Neill, L.P.1    Turner, B.M.2
  • 26
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, silac, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 27
    • 77951160864 scopus 로고    scopus 로고
    • A native chromatin purification system for epigenomic profiling in caenorhabditis elegans
    • doi: 10.1093/nar/gkp1090
    • Ooi SL, Henikoff JG, Henikoff S. 2010. A native chromatin purification system for epigenomic profiling in Caenorhabditis elegans. Nucleic Acids Res 38: e26. doi: 10.1093/nar/gkp1090.
    • (2010) Nucleic Acids Res , vol.38
    • Ooi, S.L.1    Henikoff, J.G.2    Henikoff, S.3
  • 28
    • 0034161329 scopus 로고    scopus 로고
    • Mapping chromosomal proteins in vivo by formaldehydecrosslinked-chromatin immunoprecipitation
    • Orlando V. 2000. Mapping chromosomal proteins in vivo by formaldehydecrosslinked-chromatin immunoprecipitation. Trends Biochem Sci 25: 99-104.
    • (2000) Trends Biochem Sci , vol.25 , pp. 99-104
    • Orlando, V.1
  • 29
    • 70349312354 scopus 로고    scopus 로고
    • Chip-seq: Advantages and challenges of a maturing technology
    • Park PJ. 2009. ChIP-seq: Advantages and challenges of a maturing technology. Nat Rev Genet 10: 669-680.
    • (2009) Nat Rev Genet , vol.10 , pp. 669-680
    • Park, P.J.1
  • 30
    • 1642272372 scopus 로고    scopus 로고
    • Shotgun annotation of histone modifications: A new approach for streamlined characterization of proteins by top down mass spectrometry
    • Pesavento JJ, Kim YB, Taylor GK, Kelleher NL. 2004. Shotgun annotation of histone modifications: A new approach for streamlined characterization of proteins by top down mass spectrometry. J Am Chem Soc 126: 3386-3387.
    • (2004) J Am Chem Soc , vol.126 , pp. 3386-3387
    • Pesavento, J.J.1    Kim, Y.B.2    Taylor, G.K.3    Kelleher, N.L.4
  • 31
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis dna polymerases: Specificity of structure and function
    • Prakash S, Johnson RE, Prakash L. 2005. Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function. Annu Rev Biochem 74: 317-353.
    • (2005) Annu Rev Biochem , vol.74 , pp. 317-353
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 32
    • 1042288539 scopus 로고    scopus 로고
    • Use of chromatin immunoprecipitation assays in genome-wide location analysis of mammalian transcription factors
    • Ren B, Dynlacht BD. 2004. Use of chromatin immunoprecipitation assays in genome-wide location analysis of mammalian transcription factors. Methods Enzymol 376: 304-315.
    • (2004) Methods Enzymol , vol.376 , pp. 304-315
    • Ren, B.1    Dynlacht, B.D.2
  • 36
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68: 850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 37
    • 65249153567 scopus 로고    scopus 로고
    • Regulation of gene expression and cellular proliferation by histone h2a.z
    • Svotelis A, Gevry N, Gaudreau L. 2009. Regulation of gene expression and cellular proliferation by histone H2A.Z. Biochem Cell Biol 87: 179-188.
    • (2009) Biochem Cell Biol , vol.87 , pp. 179-188
    • Svotelis, A.1    Gevry, N.2    Gaudreau, L.3
  • 38
    • 0024284552 scopus 로고
    • Drosophila has a single copy of the gene encoding a highly conserved histone h2a variant of the h2a.f/z type
    • van Daal A, White EM, Gorovsky MA, Elgin SC. 1988. Drosophila has a single copy of the gene encoding a highly conserved histone H2A variant of the H2A.F/Z type. Nucleic Acids Res 16: 7487-7497.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7487-7497
    • Van Daal, A.1    White, E.M.2    Gorovsky, M.A.3    Elgin, S.C.4
  • 39
    • 0003903126 scopus 로고
    • Springer-Verlag, New York
    • Van Holde KE. 1989. Chromatin. Springer-Verlag, New York.
    • (1989) Chromatin
    • Van Holde, K.E.1
  • 40
    • 0034007256 scopus 로고    scopus 로고
    • Identification of in vivo dna targets of chromatin proteins using tethered dam methyltransferase
    • van Steensel B, Henikoff S. 2000. Identification of in vivo DNA targets of chromatin proteins using tethered dam methyltransferase. Nat Biotechnol 18: 424-428.
    • (2000) Nat Biotechnol , vol.18 , pp. 424-428
    • Van Steensel, B.1    Henikoff, S.2
  • 41
    • 33745842279 scopus 로고    scopus 로고
    • Analysis of human histone h2az deposition in vivo argues against its direct role in epigenetic templating mechanisms
    • Viens A,Mechold U, Brouillard F,Gilbert C, Leclerc P,OgryzkoV. 2006. Analysis of human histone H2AZ deposition in vivo argues against its direct role in epigenetic templating mechanisms.Mol Cell Biol 26: 5325-5335.
    • (2006) Mol Cell Biol , vol.26 , pp. 5325-5335
    • Viens, A.1    Mechold, U.2    Brouillard, F.3    Gilbert, C.4    Leclerc, P.5    Ogryzko, V.6
  • 43
    • 0036024955 scopus 로고    scopus 로고
    • Identification of unknown target genes of human transcription factors using chromatin immunoprecipitation
    • Weinmann AS, FarnhamPJ. 2002. Identification of unknown target genes of human transcription factors using chromatin immunoprecipitation. Methods 26: 37-47.
    • (2002) Methods , vol.26 , pp. 37-47
    • Weinmann, A.S.1    Farnham, P.J.2
  • 44
    • 0347123341 scopus 로고    scopus 로고
    • Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry
    • Zhang L, Freitas MA, Wickham J, Parthun MR, Klisovic MI, Marcucci G, Byrd JC. 2004. Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry. J Am Soc Mass Spectrom 15: 77-86.
    • (2004) J Am Soc Mass Spectrom , vol.15 , pp. 77-86
    • Zhang, L.1    Freitas, M.A.2    Wickham, J.3    Parthun, M.R.4    Klisovic, M.I.5    Marcucci, G.6    Byrd, J.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.