메뉴 건너뛰기




Volumn 17, Issue 22, 2003, Pages 2733-2740

Transcriptional regulation by histone ubiquitination and deubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DEOXYRIBONUCLEASE I; DIHYDROFOLATE REDUCTASE; DNA DIRECTED RNA POLYMERASE; FUNGAL PROTEIN; GALACTOSE; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HYDROLASE; LIGASE; MAGNESIUM CHLORIDE; POLYUBIQUITIN; PROTEASOME; PROTEIN BRE1; PROTEIN CDC34; PROTEIN DERIVATIVE; PROTEIN RAD6; RIBOSOME RNA; SATELLITE DNA; TRANSCRIPTION FACTOR; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0344442779     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1156403     Document Type: Review
Times cited : (348)

References (73)
  • 3
    • 0021799821 scopus 로고
    • Preferential localization of variant nucleosomes near the 5′-end of the mouse dihydrofolate reductase gene
    • Barsoum, J. and Varshavsky, A. 1985. Preferential localization of variant nucleosomes near the 5′-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
  • 4
    • 0035423749 scopus 로고    scopus 로고
    • SAGA is an essential in vivo target of the yeast acidic activator Gal4p
    • Bhaumik, S.R. and Green, M.R. 2001. SAGA is an essential in vivo target of the yeast acidic activator Gal4p. Genes & Dev. 15: 1935-1945.
    • (2001) Genes & Dev. , vol.15 , pp. 1935-1945
    • Bhaumik, S.R.1    Green, M.R.2
  • 5
    • 0018471240 scopus 로고
    • Histone 1 is proximal to histone 2A and to A24
    • Bonner, W.M. and Stedman, J.D. 1979. Histone 1 is proximal to histone 2A and to A24. Proc. Natl. Acad. Sci. 76: 2190-2194.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 2190-2194
    • Bonner, W.M.1    Stedman, J.D.2
  • 7
    • 0037716755 scopus 로고    scopus 로고
    • Independent recruitment in vivo by Gal4 of two complexes required for transcription
    • Bryant, G.O. and Ptashne, M. 2003. Independent recruitment in vivo by Gal4 of two complexes required for transcription. Mol. Cell 11: 1301-1309.
    • (2003) Mol. Cell , vol.11 , pp. 1301-1309
    • Bryant, G.O.1    Ptashne, M.2
  • 8
    • 0028068811 scopus 로고
    • Homo-and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of histone H5
    • Cerf, C., Lippens, G., Ramakrishnan, V., Muyldermans, S., Segers, A., Wyns, L., Wodak, S.J., and Hallenga, K. 1994. Homo-and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Full assignment, tertiary structure, and comparison with the globular domain of histone H5. Biochemistry 33: 11079-11086.
    • (1994) Biochemistry , vol.33 , pp. 11079-11086
    • Cerf, C.1    Lippens, G.2    Ramakrishnan, V.3    Muyldermans, S.4    Segers, A.5    Wyns, L.6    Wodak, S.J.7    Hallenga, K.8
  • 9
    • 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
  • 10
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung, P., Allis, C.D., and Sassone-Corsi, P. 2000. Signaling to chromatin through histone modifications. Cell 103: 263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 11
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway, R.C., Brower, C.S., and Conaway, J.W. 2002. Emerging roles of ubiquitin in transcription regulation. Science 296: 1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 12
    • 0031760462 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: A new class of biological regulators
    • D'Andrea, A. and Pellman, D. 1998. Deubiquitinating enzymes: A new class of biological regulators. Crit. Rev. Biochem. Mol. Biol. 33: 337-352.
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 337-352
    • D'Andrea, A.1    Pellman, D.2
  • 13
    • 0025341218 scopus 로고
    • Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription
    • Davie, J.R. and Murphy, L.C. 1990. Level of ubiquitinated histone H2B in chromatin is coupled to ongoing transcription. Biochemistry 29: 4752-4757.
    • (1990) Biochemistry , vol.29 , pp. 4752-4757
    • Davie, J.R.1    Murphy, L.C.2
  • 14
    • 0028235824 scopus 로고
    • Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution
    • Davies, N. and Lindsey, G.G. 1994. Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution. Biochim. Biophys. Acta 1218: 187-193.
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 187-193
    • Davies, N.1    Lindsey, G.G.2
  • 15
    • 0025904349 scopus 로고
    • Affinity isolation of active murine erythroleukemia cell chromatin: Uniform distribution of ubiquitinated histone H2A between active and inactive fractions
    • Dawson, B.A., Herman, T., Haas, A.L., and Lough, J. 1991. Affinity isolation of active murine erythroleukemia cell chromatin: Uniform distribution of ubiquitinated histone H2A between active and inactive fractions. J. Cell. Biochem. 46: 166-173.
    • (1991) J. Cell. Biochem. , vol.46 , pp. 166-173
    • Dawson, B.A.1    Herman, T.2    Haas, A.L.3    Lough, J.4
  • 16
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signalling connection
    • Di Fiore, P.P., Polo, S., and Hofmann, K. 2003. When ubiquitin meets ubiquitin receptors: A signalling connection. Nat. Rev. Mol. Cell. Biol. 4: 491-497.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 18
    • 0023009034 scopus 로고
    • Inhibition of transcription does not affect the total amount of ubiquitinated histone 2A in chromatin
    • Ericsson, C., Goldknopf, I.L., and Daneholt, B. 1986. Inhibition of transcription does not affect the total amount of ubiquitinated histone 2A in chromatin. Exp. Cell. Res. 167: 127-134.
    • (1986) Exp. Cell. Res. , vol.167 , pp. 127-134
    • Ericsson, C.1    Goldknopf, I.L.2    Daneholt, B.3
  • 19
    • 0023722309 scopus 로고
    • The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme
    • Goebl, M.G., Yochem, J., Jentsch, S., McGrath, J.P., Varshavsky, A., and Byers, B. 1988. The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme. Science 241: 1331-1335.
    • (1988) Science , vol.241 , pp. 1331-1335
    • Goebl, M.G.1    Yochem, J.2    Jentsch, S.3    McGrath, J.P.4    Varshavsky, A.5    Byers, B.6
  • 22
    • 0030797349 scopus 로고    scopus 로고
    • Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex
    • Grant, P.A., Duggan, L., Cote, J., Roberts, S.M., Brownell, J.E., Candau, R., Ohba, R., Owen-Hughes, T., Allis, C.D., Winston, F., et al. 1997. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes & Dev. 11: 640-1650.
    • (1997) Genes & Dev. , vol.11 , pp. 640-1650
    • Grant, P.A.1    Duggan, L.2    Cote, J.3    Roberts, S.M.4    Brownell, J.E.5    Candau, R.6    Ohba, R.7    Owen-Hughes, T.8    Allis, C.D.9    Winston, F.10
  • 23
    • 0025774994 scopus 로고
    • Ubiquitin conjugation by the yeast RAD6 and CDC34 gene products. Comparison to their putative rabbit homologs, E2(20K) AND E2(32K)
    • Haas, A.L., Reback, P.B., and Chau, V. 1991. Ubiquitin conjugation by the yeast RAD6 and CDC34 gene products. Comparison to their putative rabbit homologs, E2(20K) AND E2(32K). J. Biol. Chem. 266: 5104-5112.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5104-5112
    • Haas, A.L.1    Reback, P.B.2    Chau, V.3
  • 24
  • 26
    • 0030758377 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in Saccharomyces cerevisiae
    • Huang, H., Kahana, A., Gottschling, D.E., Prakash, L., and Liebman, S.W. 1997. The ubiquitin-conjugating enzyme Rad6 (Ubc2) is required for silencing in Saccharomyces cerevisiae. Mol. Cell. Biol. 17: 6693-6699.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6693-6699
    • Huang, H.1    Kahana, A.2    Gottschling, D.E.3    Prakash, L.4    Liebman, S.W.5
  • 27
    • 0022444464 scopus 로고
    • The active immunoglobulin κ chain gene is packaged by non-ubiquitin-conjugated nucleosomes
    • Huang, S.Y., Barnard, M.B., Xu, M., Matsui, S., Rose, S.M., and Garrard, W.T. 1986. The active immunoglobulin κ chain gene is packaged by non-ubiquitin-conjugated nucleosomes. Proc. Natl. Acad. Sci. 83: 3738-3742.
    • (1986) Proc. Natl. Acad. Sci. , vol.83 , pp. 3738-3742
    • Huang, S.Y.1    Barnard, M.B.2    Xu, M.3    Matsui, S.4    Rose, S.M.5    Garrard, W.T.6
  • 28
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang, W.W., Venkatasubrahmanyam, S., Ianculescu, A.G., Tong, A., Boone, C., and Madhani, H.D. 2003. A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell 11: 261-266.
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 29
    • 0035805498 scopus 로고    scopus 로고
    • Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A
    • Jason, L.J., Moore, S.C., Ausio, J., and Lindsey, G. 2001. Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A. J. Biol. Chem. 276: 14597-14601.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14597-14601
    • Jason, L.J.1    Moore, S.C.2    Ausio, J.3    Lindsey, G.4
  • 31
    • 0023236126 scopus 로고
    • The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme
    • Jentsch, S., McGrath, J.P., and Varshavsky, A. 1987. The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. Nature 329: 131-134.
    • (1987) Nature , vol.329 , pp. 131-134
    • Jentsch, S.1    McGrath, J.P.2    Varshavsky, A.3
  • 32
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein, T. and Allis, C.D. 2001. Translating the histone code. Science 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 33
    • 0019878049 scopus 로고
    • Structure of nucleosome core particles containing uH2A (A24)
    • Kleinschmidt, A.M. and Martinson, H.G. 1981. Structure of nucleosome core particles containing uH2A (A24). Nucleic Acids Res. 9: 2423-2431.
    • (1981) Nucleic Acids Res. , vol.9 , pp. 2423-2431
    • Kleinschmidt, A.M.1    Martinson, H.G.2
  • 35
    • 0037524702 scopus 로고    scopus 로고
    • The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation
    • Krogan, N.J., Dover, J., Wood, A., Schneider, J., Heidt, J., Boateng, M.A., Dean, K., Ryan, O.W., Golshani, A., Johnston, M., et al, 2003a. The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: Linking transcriptional elongation to histone methylation. Mol. Cell 11: 721-729.
    • (2003) Mol. Cell , vol.11 , pp. 721-729
    • Krogan, N.J.1    Dover, J.2    Wood, A.3    Schneider, J.4    Heidt, J.5    Boateng, M.A.6    Dean, K.7    Ryan, O.W.8    Golshani, A.9    Johnston, M.10
  • 37
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner, M. and Jenuwein, T. 2002. The many faces of histone lysine methylation. Curr. Opin. Cell. Biol. 14: 286-298.
    • (2002) Curr. Opin. Cell. Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 38
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., and Jenuwein, T. 2001. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410: 116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 39
    • 0035425099 scopus 로고    scopus 로고
    • The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4
    • Larschan, E. and Winston, F. 2001. The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4. Genes & Dev. 15: 1946-1956.
    • (2001) Genes & Dev. , vol.15 , pp. 1946-1956
    • Larschan, E.1    Winston, F.2
  • 40
    • 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
  • 41
    • 0037512273 scopus 로고    scopus 로고
    • The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Li, B., Howe, L., Anderson, S., Yates III, J.R., and Workman, J.L. 2003. The Set2 histone methyltransferase functions through the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 278: 8897-8903.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8897-8903
    • Li, B.1    Howe, L.2    Anderson, S.3    Yates III, J.R.4    Workman, J.L.5
  • 42
    • 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
  • 43
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger, K., Mader, A.W., Richmond, R.K., Sargent, D.F., and Richmond, T.J. 1997. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389: 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 44
    • 0018451385 scopus 로고
    • Semihistone protein A24 replaces H2A as an integral component of the nucleosome histone core
    • Martinson, H.G., True, R., Burch, J.B., and Kunkel, G. 1979. Semihistone protein A24 replaces H2A as an integral component of the nucleosome histone core. Proc. Natl. Acad. Sci. 76: 1030-1034.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 1030-1034
    • Martinson, H.G.1    True, R.2    Burch, J.B.3    Kunkel, G.4
  • 45
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae
    • Moazed, D. and Johnson, D. 1996. A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86: 667-677.
    • (1996) Cell , vol.86 , pp. 667-677
    • Moazed, D.1    Johnson, D.2
  • 46
    • 0035986066 scopus 로고    scopus 로고
    • The elusive structural role of ubiquitinated histones
    • Moore, S.C., Jason, L., and Ausio, J. 2002. The elusive structural role of ubiquitinated histones. Biochem. Cell. Biol. 80: 311-319.
    • (2002) Biochem. Cell. Biol. , vol.80 , pp. 311-319
    • Moore, S.C.1    Jason, L.2    Ausio, J.3
  • 47
    • 0038660703 scopus 로고    scopus 로고
    • Identification of Uhp1, a ubiquitinated histone-like protein, as a target/mediator of Rhp6 in mating-type silencing in fission yeast
    • Naresh, A., Saini, S., and Singh, J. 2003. Identification of Uhp1, a ubiquitinated histone-like protein, as a target/mediator of Rhp6 in mating-type silencing in fission yeast. J. Biol. Chem. 278: 9185-9194.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9185-9194
    • Naresh, A.1    Saini, S.2    Singh, J.3
  • 48
    • 0037144393 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79
    • Ng, H.H., Xu, R.M., Zhang, Y., and Struhl, K. 2002. Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. J. Biol. Chem. 277: 34655-34657.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34655-34657
    • Ng, H.H.1    Xu, R.M.2    Zhang, Y.3    Struhl, K.4
  • 49
    • 0037452770 scopus 로고    scopus 로고
    • Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: A potential mechanism for position-effect variegation
    • Ng, H.H., Ciccone, D.N., Morshead, K.B., Oettinger, M.A., and Struhl, K. 2003a. Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: A potential mechanism for position-effect variegation. Proc. Natl. Acad. Sci. 100: 1820-1825.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 1820-1825
    • Ng, H.H.1    Ciccone, D.N.2    Morshead, K.B.3    Oettinger, M.A.4    Struhl, K.5
  • 50
    • 0141483281 scopus 로고    scopus 로고
    • The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B
    • Ng, H.H., Dole, S., and Struhl, K. 2003b. The Rtf1 component of the Paf1 transcriptional elongation complex is required for ubiquitination of histone H2B. J. Biol. Chem. 278: 33625-33628.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33625-33628
    • Ng, H.H.1    Dole, S.2    Struhl, K.3
  • 51
    • 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. 2003c. 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
  • 52
    • 0024595905 scopus 로고
    • Structure of polyubiquitinated histone H2A
    • Nickel, B.E. and Davie, J.R. 1989. Structure of polyubiquitinated histone H2A. Biochemistry 28: 964-968.
    • (1989) Biochemistry , vol.28 , pp. 964-968
    • Nickel, B.E.1    Davie, J.R.2
  • 53
    • 0024505572 scopus 로고
    • Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin
    • Nickel, B.E., Allis, C.D., and Davie, J.R. 1989. Ubiquitinated histone H2B is preferentially located in transcriptionally active chromatin. Biochemistry 28: 958-963.
    • (1989) Biochemistry , vol.28 , pp. 958-963
    • Nickel, B.E.1    Allis, C.D.2    Davie, J.R.3
  • 54
    • 0025344438 scopus 로고
    • Enrichment of ubiquitinated histone H2A in a low salt extract of micrococcal nuclease-digested myotube nuclei
    • Parlow, M.H., Haas, A.L., and Lough, J. 1990. Enrichment of ubiquitinated histone H2A in a low salt extract of micrococcal nuclease-digested myotube nuclei. J. Biol. Chem. 265: 7507-7512.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7507-7512
    • Parlow, M.H.1    Haas, A.L.2    Lough, J.3
  • 55
    • 0034730745 scopus 로고    scopus 로고
    • II250, a mediator of activation of gene expression in Drosophila
    • II250, 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
  • 56
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C.M. 2001. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70: 503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 57
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk, K., Recht, J., and Osley, M.A. 2000. Rad6-dependent ubiquitination of histone H2B in yeast. Science 287: 501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 59
    • 0035163063 scopus 로고    scopus 로고
    • Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S., and Khochbin, S. 2001. Identification of components of the murine histone deacetylase 6 complex: Link between acetylation and ubiquitination signaling pathways. Mol. Cell. Biol. 21: 8035-8044.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdel, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5    Rousseaux, S.6    Khochbin, S.7
  • 60
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B.D. and Allis, C.D. 2000. The language of covalent histone modifications. Nature 403: 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 61
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun, Z.W. and Allis, C.D. 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418: 104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 62
    • 0032794445 scopus 로고    scopus 로고
    • The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast
    • Swaminathan, S., Amerik, A.Y., and Hochstrasser, M. 1999. The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast. Mol. Biol. Cell 10: 2583-2594.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2583-2594
    • Swaminathan, S.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 64
  • 65
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen, F., Gafken, P.R., and Gottschling, D.E. 2002. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109: 745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 66
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • Vijay-Kumar, S., Bugg, C.E., and Cook, W.J. 1987. Structure of ubiquitin refined at 1.8 A resolution. J. Mol. Biol. 194: 531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 67
    • 0019332014 scopus 로고
    • Histone 2B can be modified by the attachment of ubiquitin
    • West, M.H. and Bonner, W.M. 1980. Histone 2B can be modified by the attachment of ubiquitin. Nucleic Acids Res. 8: 4671-4680.
    • (1980) Nucleic Acids Res. , vol.8 , pp. 4671-4680
    • West, M.H.1    Bonner, W.M.2
  • 68
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson, K.D. 2000. Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome. Semin. Cell. Dev. Biol. 11: 141-148.
    • (2000) Semin. Cell. Dev. Biol. , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 70
    • 0042818412 scopus 로고    scopus 로고
    • The Paf1 complex is essential for histone monoubiquitination by the Rad6-Brel complex, which signals for histone methylation by COMPASS and Dot1p
    • Wood, A., Schneider, J., Dover, J., Johnston, M., and Shilatifard, A. 2003b. The Paf1 complex is essential for histone monoubiquitination by the Rad6-Brel 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
  • 71
    • 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
  • 73
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang, Y. and Reinberg, D. 2001. Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails. Genes & Dev. 15: 2343-2360.
    • (2001) Genes & Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.