메뉴 건너뛰기




Volumn 40, Issue 20, 2012, Pages 10187-10202

Promoters active in interphase are bookmarked during mitosis by ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2B; HISTONE H3; PROTEIN H3K27ME3; PROTEIN H3K36ME3; PROTEIN H3K4ME3; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84869036520     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks820     Document Type: Article
Times cited : (7)

References (61)
  • 1
    • 0010115729 scopus 로고    scopus 로고
    • Ubiquitination of histone H3 in elongating spermatids of rat testes
    • Chen, H.Y., Sun, J.M., Zhang, Y., Davie, J.R. and Meistrich, M.L. (1998) Ubiquitination of histone H3 in elongating spermatids of rat testes. J. Biol. Chem., 273, 13165-13169.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13165-13169
    • Chen, H.Y.1    Sun, J.M.2    Zhang, Y.3    Davie, J.R.4    Meistrich, M.L.5
  • 2
    • 0034730745 scopus 로고    scopus 로고
    • Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila
    • Pham, A.D. and Sauer, F. (2000) Ubiquitin-activating/conjugating activity of TAFII250, a mediator of activation of gene expression in Drosophila. Science, 289, 2357-2360.
    • (2000) Science , vol.289 , pp. 2357-2360
    • Pham, A.D.1    Sauer, F.2
  • 3
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: Triggering gene activity
    • Weake, V.M. and Workman, J.L. (2008) Histone ubiquitination: triggering gene activity. Mol. Cell, 29, 653-663.
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 4
    • 34548777017 scopus 로고    scopus 로고
    • Monoubiquitylation of H2A. Z distinguishes its association with euchromatin or facultative heterochromatin
    • Sarcinella, E., Zuzarte, P.C., Lau, P.N., Draker, R. and Cheung, P. (2007) Monoubiquitylation of H2A.Z distinguishes its association with euchromatin or facultative heterochromatin. Mol. Cell. Biol., 27, 6457-6468.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6457-6468
    • Sarcinella, E.1    Zuzarte, P.C.2    Lau, P.N.3    Draker, R.4    Cheung, P.5
  • 6
    • 27944454433 scopus 로고    scopus 로고
    • Monoubiquitination of human histone H2B: The factors involved and their roles in HOX gene regulation
    • Zhu, B., Zheng, Y., Pham, A.D., Mandal, S.S., Erdjument- Bromage, H., Tempst, P. and Reinberg, D. (2005) Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation. Mol. Cell, 20, 601-611.
    • (2005) Mol. Cell , vol.20 , pp. 601-611
    • Zhu, B.1    Zheng, Y.2    Pham, A.D.3    Mandal, S.S.4    Erdjument- Bromage, H.5    Tempst, P.6    Reinberg, D.7
  • 8
    • 33646691283 scopus 로고    scopus 로고
    • Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II
    • Pavri, R., Zhu, B., Li, G., Trojer, P., Mandal, S., Shilatifard, A. and Reinberg, D. (2006) Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell, 125, 703-717.
    • (2006) Cell , vol.125 , pp. 703-717
    • Pavri, R.1    Zhu, B.2    Li, G.3    Trojer, P.4    Mandal, S.5    Shilatifard, A.6    Reinberg, D.7
  • 9
    • 43149122898 scopus 로고    scopus 로고
    • Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells
    • Minsky, N., Shema, E., Field, Y., Schuster, M., Segal, E. and Oren, M. (2008) Monoubiquitinated H2B is associated with the transcribed region of highly expressed genes in human cells. Nat. Cell Biol., 10, 483-488.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 483-488
    • Minsky, N.1    Shema, E.2    Field, Y.3    Schuster, M.4    Segal, E.5    Oren, M.6
  • 13
    • 0021799821 scopus 로고
    • Preferential localization of variant nucleosomes near the 50-end of the mouse dihydrofolate reductase gene
    • Barsoum, J. and Varshavsky, A. (1985) Preferential localization of variant nucleosomes near the 50-end of the mouse dihydrofolate reductase gene. J. Biol. Chem., 260, 7688-7697.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7688-7697
    • Barsoum, J.1    Varshavsky, A.2
  • 14
    • 0020055316 scopus 로고
    • Selective arrangement of ubiquitinated and D1 protein-containing nucleosomes within the Drosophila genome
    • Levinger, L. and Varshavsky, A. (1982) Selective arrangement of ubiquitinated and D1 protein-containing nucleosomes within the Drosophila genome. Cell, 28, 375-385.
    • (1982) Cell , vol.28 , pp. 375-385
    • Levinger, L.1    Varshavsky, A.2
  • 15
    • 79959847254 scopus 로고    scopus 로고
    • The role of deubiquitinating enzymes in chromatin regulation
    • Atanassov, B.S., Koutelou, E. and Dent, S.Y. (2011) The role of deubiquitinating enzymes in chromatin regulation. FEBS Lett., 585, 2016-2023.
    • (2011) FEBS Lett. , vol.585 , pp. 2016-2023
    • Atanassov, B.S.1    Koutelou, E.2    Dent, S.Y.3
  • 16
    • 0019877029 scopus 로고
    • Metabolism of ubiquitinated histones
    • Wu, R.S., Kohn, K.W. and Bonner, W.M. (1981) Metabolism of ubiquitinated histones. J. Biol. Chem., 256, 5916-5920.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5916-5920
    • Wu, R.S.1    Kohn, K.W.2    Bonner, W.M.3
  • 17
    • 35548986309 scopus 로고    scopus 로고
    • Regulation of cell cycle progression and gene expression by H2A deubiquitination
    • Joo, H.Y., Zhai, L., Yang, C., Nie, S., Erdjument-Bromage, H., Tempst, P., Chang, C. and Wang, H. (2007) Regulation of cell cycle progression and gene expression by H2A deubiquitination. Nature, 449, 1068-1072.
    • (2007) Nature , vol.449 , pp. 1068-1072
    • Joo, H.Y.1    Zhai, L.2    Yang, C.3    Nie, S.4    Erdjument-Bromage, H.5    Tempst, P.6    Chang, C.7    Wang, H.8
  • 18
    • 10044298120 scopus 로고    scopus 로고
    • Ubiquitinated proteins including uH2A on the human and mouse inactive X chromosome: Enrichment in gene rich bands
    • Smith, K.P., Byron, M., Clemson, C.M. and Lawrence, J.B. (2004) Ubiquitinated proteins including uH2A on the human and mouse inactive X chromosome: enrichment in gene rich bands. Chromosoma, 113, 324-335.
    • (2004) Chromosoma , vol.113 , pp. 324-335
    • Smith, K.P.1    Byron, M.2    Clemson, C.M.3    Lawrence, J.B.4
  • 19
    • 0024555818 scopus 로고
    • Purification, characterization, and rapid inactivation of thermolabile ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Mayer, A., Gropper, R., Schwartz, A.L. and Ciechanover, A. (1989) Purification, characterization, and rapid inactivation of thermolabile ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. J. Biol. Chem., 264, 2060-2068.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2060-2068
    • Mayer, A.1    Gropper, R.2    Schwartz, A.L.3    Ciechanover, A.4
  • 20
    • 0021139080 scopus 로고
    • Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85
    • Finley, D., Ciechanover, A. and Varshavsky, A. (1984) Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85. Cell, 37, 43-55.
    • (1984) Cell , vol.37 , pp. 43-55
    • Finley, D.1    Ciechanover, A.2    Varshavsky, A.3
  • 21
    • 0019305278 scopus 로고
    • A temperature-sensitive mutant of cultured mouse cells defective in chromosome condensation
    • Mita, S., Yasuda, H., Marunouchi, T., Ishiko, S. and Yamada, M. (1980) A temperature-sensitive mutant of cultured mouse cells defective in chromosome condensation. Exp. Cell Res., 126, 407-416.
    • (1980) Exp. Cell Res. , vol.126 , pp. 407-416
    • Mita, S.1    Yasuda, H.2    Marunouchi, T.3    Ishiko, S.4    Yamada, M.5
  • 23
    • 33645703441 scopus 로고    scopus 로고
    • A tandem affinity tag for two-step purification under fully denaturing conditions: Application in ubiquitin profiling and protein complex identification combined with in vivocross-linking
    • Tagwerker, C., Flick, K., Cui, M., Guerrero, C., Dou, Y., Auer, B., Baldi, P., Huang, L. and Kaiser, P. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol. Cell. Proteom. MCP, 5, 737-748.
    • (2006) Mol. Cell. Proteom. MCP , vol.5 , pp. 737-748
    • Tagwerker, C.1    Flick, K.2    Cui, M.3    Guerrero, C.4    Dou, Y.5    Auer, B.6    Baldi, P.7    Huang, L.8    Kaiser, P.9
  • 24
    • 37049023673 scopus 로고    scopus 로고
    • Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation
    • Sankaran, S., Crone, D.E., Palazzo, R.E. and Parvin, J.D. (2007) Aurora-A kinase regulates breast cancer associated gene 1 inhibition of centrosome-dependent microtubule nucleation. Cancer Res., 67, 11186-11194.
    • (2007) Cancer Res. , vol.67 , pp. 11186-11194
    • Sankaran, S.1    Crone, D.E.2    Palazzo, R.E.3    Parvin, J.D.4
  • 25
    • 34249854866 scopus 로고    scopus 로고
    • A mechanism for transcriptional repression dependent on the BRCA1 E3 ubiquitin ligase
    • Horwitz, A.A., Affar el, B., Heine, G.F., Shi, Y. and Parvin, J.D. (2007) A mechanism for transcriptional repression dependent on the BRCA1 E3 ubiquitin ligase. Proc. Natl Acad. Sci. USA, 104, 6614-6619.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 6614-6619
    • Horwitz, A.A.1    Affar El, B.2    Heine, G.F.3    Shi, Y.4    Parvin, J.D.5
  • 26
    • 0033013469 scopus 로고    scopus 로고
    • The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin
    • Remboutsika, E., Lutz, Y., Gansmuller, A., Vonesch, J.L., Losson, R. and Chambon, P. (1999) The putative nuclear receptor mediator TIF1alpha is tightly associated with euchromatin. J. Cell Sci., 112(Pt 11), 1671-1683.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 11 , pp. 1671-1683
    • Remboutsika, E.1    Lutz, Y.2    Gansmuller, A.3    Vonesch, J.L.4    Losson, R.5    Chambon, P.6
  • 27
    • 33845925394 scopus 로고    scopus 로고
    • Chromatin immunoprecipitation and microarray-based analysis of protein location
    • Lee, T.I., Johnstone, S.E. and Young, R.A. (2006) Chromatin immunoprecipitation and microarray-based analysis of protein location. Nat. Protocols, 1, 729-748.
    • (2006) Nat. Protocols , vol.1 , pp. 729-748
    • Lee, T.I.1    Johnstone, S.E.2    Young, R.A.3
  • 28
    • 64849110610 scopus 로고    scopus 로고
    • Determination of enriched histone modifications in non-genic portions of the human genome
    • Rosenfeld, J.A., Wang, Z., Schones, D.E., Zhao, K., DeSalle, R. and Zhang, M.Q. (2009) Determination of enriched histone modifications in non-genic portions of the human genome. BMC Genomics, 10, 143.
    • (2009) BMC Genomics , vol.10 , pp. 143
    • Rosenfeld, J.A.1    Wang, Z.2    Schones, D.E.3    Zhao, K.4    Desalle, R.5    Zhang, M.Q.6
  • 29
    • 1542405872 scopus 로고    scopus 로고
    • Pharmacogenomic identification of targets for adjuvant therapy with the topoisomerase poison camptothecin
    • Carson, J.P., Zhang, N., Frampton, G.M., Gerry, N.P., Lenburg, M.E. and Christman, M.F. (2004) Pharmacogenomic identification of targets for adjuvant therapy with the topoisomerase poison camptothecin. Cancer Res., 64, 2096-2104.
    • (2004) Cancer Res. , vol.64 , pp. 2096-2104
    • Carson, J.P.1    Zhang, N.2    Frampton, G.M.3    Gerry, N.P.4    Lenburg, M.E.5    Christman, M.F.6
  • 30
    • 84857860452 scopus 로고    scopus 로고
    • The MuvB complex sequentially recruits B-Myb and FoxM1 to promote mitotic gene expression
    • Sadasivam, S., Duan, S. and DeCaprio, J.A. (2012) The MuvB complex sequentially recruits B-Myb and FoxM1 to promote mitotic gene expression. Genes Dev., 26, 474-489.
    • (2012) Genes Dev. , vol.26 , pp. 474-489
    • Sadasivam, S.1    Duan, S.2    Decaprio, J.A.3
  • 31
    • 77951770756 scopus 로고    scopus 로고
    • BEDTools: A flexible suite of utilities for comparing genomic features
    • Quinlan, A.R. and Hall, I.M. (2010) BEDTools: a flexible suite of utilities for comparing genomic features. Bioinformatics, 26, 841-842.
    • (2010) Bioinformatics , vol.26 , pp. 841-842
    • Quinlan, A.R.1    Hall, I.M.2
  • 32
    • 55949136614 scopus 로고    scopus 로고
    • Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry
    • Meierhofer, D., Wang, X., Huang, L. and Kaiser, P. (2008) Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J. Proteome Res., 7, 4566-4576.
    • (2008) J. Proteome Res. , vol.7 , pp. 4566-4576
    • Meierhofer, D.1    Wang, X.2    Huang, L.3    Kaiser, P.4
  • 33
    • 0032991645 scopus 로고    scopus 로고
    • Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain
    • Mitsui, A. and Sharp, P.A. (1999) Ubiquitination of RNA polymerase II large subunit signaled by phosphorylation of carboxyl-terminal domain. Proc. Natl Acad. Sci. USA, 96, 6054-6059.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6054-6059
    • Mitsui, A.1    Sharp, P.A.2
  • 35
    • 0028783965 scopus 로고
    • Displacement of sequence-specific transcription factors from mitotic chromatin
    • Martinez-Balbas, M.A., Dey, A., Rabindran, S.K., Ozato, K. and Wu, C. (1995) Displacement of sequence-specific transcription factors from mitotic chromatin. Cell, 83, 29-38.
    • (1995) Cell , vol.83 , pp. 29-38
    • Martinez-Balbas, M.A.1    Dey, A.2    Rabindran, S.K.3    Ozato, K.4    Wu, C.5
  • 36
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing
    • Cao, R., Tsukada, Y. and Zhang, Y. (2005) Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol. Cell, 20, 845-854.
    • (2005) Mol. Cell , vol.20 , pp. 845-854
    • Cao, R.1    Tsukada, Y.2    Zhang, Y.3
  • 37
    • 70349731733 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates chromatin dynamics by enhancing nucleosome stability
    • Chandrasekharan, M.B., Huang, F. and Sun, Z.W. (2009) Ubiquitination of histone H2B regulates chromatin dynamics by enhancing nucleosome stability. Proc. Natl Acad. Sci. USA, 106, 16686-16691.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16686-16691
    • Chandrasekharan, M.B.1    Huang, F.2    Sun, Z.W.3
  • 38
    • 13444292904 scopus 로고    scopus 로고
    • Histone modifications defining active genes persist after transcriptional and mitotic inactivation
    • Kouskouti, A. and Talianidis, I. (2005) Histone modifications defining active genes persist after transcriptional and mitotic inactivation. EMBO J., 24, 347-357.
    • (2005) EMBO J. , vol.24 , pp. 347-357
    • Kouskouti, A.1    Talianidis, I.2
  • 39
    • 30044436439 scopus 로고    scopus 로고
    • Role of histone modifications in marking and activating genes through mitosis
    • Valls, E., Sanchez-Molina, S. and Martinez-Balbas, M.A. (2005) Role of histone modifications in marking and activating genes through mitosis. J. Biol. Chem., 280, 42592-42600.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42592-42600
    • Valls, E.1    Sanchez-Molina, S.2    Martinez-Balbas, M.A.3
  • 40
    • 0042818412 scopus 로고    scopus 로고
    • The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p
    • Wood, A., Schneider, J., Dover, J., Johnston, M. and Shilatifard, A. (2003) The Paf1 complex is essential for histone monoubiquitination by the Rad6-Bre1 complex, which signals for histone methylation by COMPASS and Dot1p. J. Biol. Chem., 278, 34739-34742.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34739-34742
    • Wood, A.1    Schneider, J.2    Dover, J.3    Johnston, M.4    Shilatifard, A.5
  • 41
    • 0942290540 scopus 로고    scopus 로고
    • Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B
    • Kao, C.F., Hillyer, C., Tsukuda, T., Henry, K., Berger, S. and Osley, M.A. (2004) Rad6 plays a role in transcriptional activation through ubiquitylation of histone H2B. Genes Dev., 18, 184-195.
    • (2004) Genes Dev. , vol.18 , pp. 184-195
    • Kao, C.F.1    Hillyer, C.2    Tsukuda, T.3    Henry, K.4    Berger, S.5    Osley, M.A.6
  • 43
    • 80455162312 scopus 로고    scopus 로고
    • Genome-wide function of H2B ubiquitylation in promoter and genic regions
    • Batta, K., Zhang, Z., Yen, K., Goffman, D.B. and Pugh, B.F. (2011) Genome-wide function of H2B ubiquitylation in promoter and genic regions. Genes Dev., 25, 2254-2265.
    • (2011) Genes Dev. , vol.25 , pp. 2254-2265
    • Batta, K.1    Zhang, Z.2    Yen, K.3    Goffman, D.B.4    Pugh, B.F.5
  • 44
    • 65249105512 scopus 로고    scopus 로고
    • RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells
    • Kim, J., Guermah, M., McGinty, R.K., Lee, J.S., Tang, Z., Milne, T.A., Shilatifard, A., Muir, T.W. and Roeder, R.G. (2009) RAD6-Mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells. Cell, 137, 459-471.
    • (2009) Cell , vol.137 , pp. 459-471
    • Kim, J.1    Guermah, M.2    McGinty, R.K.3    Lee, J.S.4    Tang, Z.5    Milne, T.A.6    Shilatifard, A.7    Muir, T.W.8    Roeder, R.G.9
  • 48
    • 0344022572 scopus 로고    scopus 로고
    • Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity
    • Ng, H.H., Robert, F., Young, R.A. and Struhl, K. (2003) Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity. Mol. Cell, 11, 709-719.
    • (2003) Mol. Cell , vol.11 , pp. 709-719
    • Ng, H.H.1    Robert, F.2    Young, R.A.3    Struhl, K.4
  • 49
    • 16244384503 scopus 로고    scopus 로고
    • A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation
    • Kizer, K.O., Phatnani, H.P., Shibata, Y., Hall, H., Greenleaf, A.L. and Strahl, B.D. (2005) A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation. Mol. Cell. Biol., 25, 3305-3316.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3305-3316
    • Kizer, K.O.1    Phatnani, H.P.2    Shibata, Y.3    Hall, H.4    Greenleaf, A.L.5    Strahl, B.D.6
  • 50
    • 0037147121 scopus 로고    scopus 로고
    • Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation
    • Li, J., Moazed, D. and Gygi, S.P. (2002) Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation. J. Biol. Chem., 277, 49383-49388.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49383-49388
    • Li, J.1    Moazed, D.2    Gygi, S.P.3
  • 51
    • 27444436367 scopus 로고    scopus 로고
    • Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase
    • Sun, X.J., Wei, J., Wu, X.Y., Hu, M., Wang, L., Wang, H.H., Zhang, Q.H., Chen, S.J., Huang, Q.H. and Chen, Z. (2005) Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J. Biol. Chem., 280, 35261-35271.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35261-35271
    • Sun, X.J.1    Wei, J.2    Wu, X.Y.3    Hu, M.4    Wang, L.5    Wang, H.H.6    Zhang, Q.H.7    Chen, S.J.8    Huang, Q.H.9    Chen, Z.10
  • 53
    • 72149122408 scopus 로고    scopus 로고
    • A reconfigured pattern of MLL occupancy within mitotic chromatin promotes rapid transcriptional reactivation following mitotic exit
    • Blobel, G.A., Kadauke, S., Wang, E., Lau, A.W., Zuber, J., Chou, M.M. and Vakoc, C.R. (2009) A reconfigured pattern of MLL occupancy within mitotic chromatin promotes rapid transcriptional reactivation following mitotic exit. Mol. Cell, 36, 970-983.
    • (2009) Mol. Cell , vol.36 , pp. 970-983
    • Blobel, G.A.1    Kadauke, S.2    Wang, E.3    Lau, A.W.4    Zuber, J.5    Chou, M.M.6    Vakoc, C.R.7
  • 54
    • 53549112774 scopus 로고    scopus 로고
    • The histone H2B-specific ubiquitin ligase RNF20/hBRE1 acts as a putative tumor suppressor through selective regulation of gene expression
    • Shema, E., Tirosh, I., Aylon, Y., Huang, J., Ye, C., Moskovits, N., Raver-Shapira, N., Minsky, N., Pirngruber, J., Tarcic, G. et al. (2008) The histone H2B-specific ubiquitin ligase RNF20/hBRE1 acts as a putative tumor suppressor through selective regulation of gene expression. Genes Dev., 22, 2664-2676.
    • (2008) Genes Dev. , vol.22 , pp. 2664-2676
    • Shema, E.1    Tirosh, I.2    Aylon, Y.3    Huang, J.4    Ye, C.5    Moskovits, N.6    Raver-Shapira, N.7    Minsky, N.8    Pirngruber, J.9    Tarcic, G.10
  • 55
    • 0021812747 scopus 로고
    • Identification of ubiquitinated histones 2A and 2B in Physarum polycephalum. Disappearance of these proteins at metaphase and reappearance at anaphase
    • Mueller, R.D., Yasuda, H., Hatch, C.L., Bonner, W.M. and Bradbury, E.M. (1985) Identification of ubiquitinated histones 2A and 2B in Physarum polycephalum. Disappearance of these proteins at metaphase and reappearance at anaphase. J. Biol. Chem., 260, 5147-5153.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5147-5153
    • Mueller, R.D.1    Yasuda, H.2    Hatch, C.L.3    Bonner, W.M.4    Bradbury, E.M.5
  • 56
    • 65349159712 scopus 로고    scopus 로고
    • Mitotic bookmarking of formerly active genes: Keeping epigenetic memories from fading
    • Sarge, K.D. and Park-Sarge, O.K. (2009) Mitotic bookmarking of formerly active genes: keeping epigenetic memories from fading. Cell Cycle, 8, 818-823.
    • (2009) Cell Cycle , vol.8 , pp. 818-823
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 57
    • 0026340958 scopus 로고
    • Association of ubiquitin-activating enzyme with HeLa cell chromosomes during mitosis
    • Cook, J.C. and Chock, P.B. (1991) Association of ubiquitin-activating enzyme with HeLa cell chromosomes during mitosis. Proc. Natl Acad. Sci. USA, 88, 11388-11392.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 11388-11392
    • Cook, J.C.1    Chock, P.B.2
  • 58
    • 0024022780 scopus 로고
    • Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the BHK cell line
    • Sekiguchi, T., Miyata, T. and Nishimoto, T. (1988) Molecular cloning of the cDNA of human X chromosomal gene (CCG1) which complements the temperature-sensitive G1 mutants, tsBN462 and ts13, of the BHK cell line. EMBO J., 7, 1683-1687.
    • (1988) EMBO J. , vol.7 , pp. 1683-1687
    • Sekiguchi, T.1    Miyata, T.2    Nishimoto, T.3
  • 59
    • 0027526619 scopus 로고
    • The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1
    • Hisatake, K., Hasegawa, S., Takada, R., Nakatani, Y., Horikoshi, M. and Roeder, R.G. (1993) The p250 subunit of native TATA box-binding factor TFIID is the cell-cycle regulatory protein CCG1. Nature, 362, 179-181.
    • (1993) Nature , vol.362 , pp. 179-181
    • Hisatake, K.1    Hasegawa, S.2    Takada, R.3    Nakatani, Y.4    Horikoshi, M.5    Roeder, R.G.6
  • 60
    • 0036144598 scopus 로고    scopus 로고
    • Association of human TFIID-promoter complexes with silenced mitotic chromatin in vivo
    • Christova, R. and Oelgeschlager, T. (2002) Association of human TFIID-promoter complexes with silenced mitotic chromatin in vivo. Nat. Cell Biol., 4, 79-82.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 79-82
    • Christova, R.1    Oelgeschlager, T.2
  • 61
    • 0025256911 scopus 로고
    • Purification of eukaryotic RNA polymerase II by immunoaffinity chromatography. Elution of active enzyme with protein stabilizing agents from a polyol-responsive monoclonal antibody
    • Thompson, N.E., Aronson, D.B. and Burgess, R.R. (1990) Purification of eukaryotic RNA polymerase II by immunoaffinity chromatography. Elution of active enzyme with protein stabilizing agents from a polyol-responsive monoclonal antibody. J. Biol. Chem., 265, 7069-7077.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7069-7077
    • Thompson, N.E.1    Aronson, D.B.2    Burgess, R.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.