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Volumn 45, Issue 3, 2006, Pages 1035-1042

Sumoylation of the yeast Gcn5 protein

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYMES; HISTOLOGY; MUTAGENESIS; PROTEINS; SUBSTRATES;

EID: 31044444152     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051624q     Document Type: Article
Times cited : (23)

References (44)
  • 2
    • 0037041022 scopus 로고    scopus 로고
    • Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation
    • Balasubramanian, R., Pray-Grant, M. G., Selleck, W., Grant, P. A., and Tan, S. (2002) Role of the Ada2 and Ada3 transcriptional coactivators in histone acetylation, J. Biol. Chem. 277, 7989-7995.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7989-7995
    • Balasubramanian, R.1    Pray-Grant, M.G.2    Selleck, W.3    Grant, P.A.4    Tan, S.5
  • 3
    • 4944255743 scopus 로고    scopus 로고
    • Posttranslational modification of p53 in tumorigenesis
    • Bode, A. M., and Dong, Z. (2004) Posttranslational modification of p53 in tumorigenesis, Nat. Rev. Cancer 4, 793-805.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 4
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • Boyer, L. A., Langer, M. R., Crowley, K. A., Tan, S., Denu, J. M., and Peterson, C. L. (2002) Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes, Mol. Cell 10, 935-942.
    • (2002) Mol. Cell , vol.10 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5    Peterson, C.L.6
  • 5
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J. E., Zhou, J., Ranalli, T., Kobayashi, R., Edmondson, D. G., Roth, S. Y., and Allis, C. D. (1996) Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation, Cell 84, 843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 6
    • 0030030611 scopus 로고    scopus 로고
    • Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5
    • Candau, R., Moore, P. A., Wang, L., Barlev, N., Ying, C. Y., Rosen, C. A., and Berger, S. L. (1996) Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5, Mol. Cell. Biol. 16, 593-602.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 593-602
    • Candau, R.1    Moore, P.A.2    Wang, L.3    Barlev, N.4    Ying, C.Y.5    Rosen, C.A.6    Berger, S.L.7
  • 7
    • 0031031755 scopus 로고    scopus 로고
    • Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
    • Candau, R., Zhou, J. X., Allis, C. D., and Berger, S. L. (1997) Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo, EMBO J. 16, 555-565.
    • (1997) EMBO J. , vol.16 , pp. 555-565
    • Candau, R.1    Zhou, J.X.2    Allis, C.D.3    Berger, S.L.4
  • 9
    • 0345826106 scopus 로고    scopus 로고
    • Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription
    • Daniel, J. A., Torok, M. S., Sun, Z. W., Schieltz, D., Allis, C. D., Yates, J. R., III, and Grant, P. A. (2004) Deubiquitination of histone H2B by a yeast acetyltransferase complex regulates transcription, J. Biol. Chem. 279, 1867-1871.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1867-1871
    • Daniel, J.A.1    Torok, M.S.2    Sun, Z.W.3    Schieltz, D.4    Allis, C.D.5    Yates III, J.R.6    Grant, P.A.7
  • 11
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., and Zhou, M. M. (1999) Structure and ligand of a histone acetyltransferase bromodomain, Nature 399, 491-496.
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5    Zhou, M.M.6
  • 14
    • 0242361623 scopus 로고    scopus 로고
    • Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8
    • Henry, K. W., Wyce, A., Lo, W. S., Duggan, L. J., Emre, N. C., Kao, C. F., Pillus, L., Shilatifard, A., Osley, M. A., and Berger, S. L. (2003) Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8, Genes Dev. 17, 2648-2663.
    • (2003) Genes Dev. , vol.17 , pp. 2648-2663
    • Henry, K.W.1    Wyce, A.2    Lo, W.S.3    Duggan, L.J.4    Emre, N.C.5    Kao, C.F.6    Pillus, L.7    Shilatifard, A.8    Osley, M.A.9    Berger, S.L.10
  • 15
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G., and Jentsch, S. (2002) RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO, Nature 419, 135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 16
    • 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
  • 17
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E. S. (2004) Protein modification by SUMO, Annu. Rev. Biochem. 73, 355-382.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 18
    • 0033615965 scopus 로고    scopus 로고
    • Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins
    • Johnson, E. S., and Blobel, G. (1999) Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins, J. Cell Biol. 147, 981-994.
    • (1999) J. Cell Biol. , vol.147 , pp. 981-994
    • Johnson, E.S.1    Blobel, G.2
  • 19
    • 0035929279 scopus 로고    scopus 로고
    • An E3-like factor that promotes SUMO conjugation to the yeast septins
    • Johnson, E. S., and Gupta, A. A. (2001) An E3-like factor that promotes SUMO conjugation to the yeast septins, Cell 106, 735-744.
    • (2001) Cell , vol.106 , pp. 735-744
    • Johnson, E.S.1    Gupta, A.A.2
  • 20
    • 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
  • 21
    • 0034269239 scopus 로고    scopus 로고
    • Global role for chromatin remodeling enzymes in mitotic gene expression
    • Krebs, J. E., Fry, C. J., Samuels, M. L., and Peterson, C. L. (2000) Global role for chromatin remodeling enzymes in mitotic gene expression, Cell 102, 587-598.
    • (2000) Cell , vol.102 , pp. 587-598
    • Krebs, J.E.1    Fry, C.J.2    Samuels, M.L.3    Peterson, C.L.4
  • 23
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A., III, Demarini, D. J., Shah, N. G., Wach, A., Brachat, A., Philippsen, P., and Pringle, J. R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae, Yeast 14, 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 24
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., Delphin, C., Guan, T., Gerace, L., and Melchior, F. (1997) A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2, Cell 88, 97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 25
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., Coutavas, E., and Blobel, G. (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex, J. Cell Biol. 135, 1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 26
    • 0034687807 scopus 로고    scopus 로고
    • Co valent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H., Karvonen, U., Janne, O. A., and Palvimo, J. J. (2000) Co valent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1), Proc. Natl. Acad. Sci. U.S.A. 97, 14145-14150.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 28
    • 0030876429 scopus 로고    scopus 로고
    • Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes
    • Roberts, S. M., and Winston, F. (1997) Essential functional interactions of SAGA, a Saccharomyces cerevisiae complex of Spt, Ada, and Gcn5 proteins, with the Snf/Swi and Srb/mediator complexes, Genetics 147, 451-465.
    • (1997) Genetics , vol.147 , pp. 451-465
    • Roberts, S.M.1    Winston, F.2
  • 29
    • 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
  • 34
    • 0344824404 scopus 로고    scopus 로고
    • Histone sumoylation is associated with transcriptional repression
    • Shiio, Y., and Eisenman, R. N. (2003) Histone sumoylation is associated with transcriptional repression, Proc. Natl. Acad. Sci. U.S.A. 100, 13225-13230.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 13225-13230
    • Shiio, Y.1    Eisenman, R.N.2
  • 35
    • 0037015044 scopus 로고    scopus 로고
    • SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription
    • Sterner, D. E., Belotserkovskaya, R., and Berger, S. L. (2002) SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates with activated transcription, Proc. Natl. Acad. Sci. U.S.A. 99, 11622-11627.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11622-11627
    • Sterner, D.E.1    Belotserkovskaya, R.2    Berger, S.L.3
  • 36
    • 0032911635 scopus 로고    scopus 로고
    • Functional organization of the yeast SAGA complex: Distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction
    • Sterner, D. E., Grant, P. A., Roberts, S. M., Duggan, L. J., Belotserkovskaya, R., Pacella, L. A., Winston, F., Workman, J. L., and Berger, S. L. (1999) Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction, Mol. Cell. Biol. 19, 86-98.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 86-98
    • Sterner, D.E.1    Grant, P.A.2    Roberts, S.M.3    Duggan, L.J.4    Belotserkovskaya, R.5    Pacella, L.A.6    Winston, F.7    Workman, J.L.8    Berger, S.L.9
  • 37
    • 0037040978 scopus 로고    scopus 로고
    • The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex
    • Sterner, D. E., Wang, X., Bloom, M. H., Simon, G. M., and Berger, S. L. (2002) The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex, J. Biol. Chem. 277, 8178-8186.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8178-8186
    • Sterner, D.E.1    Wang, X.2    Bloom, M.H.3    Simon, G.M.4    Berger, S.L.5
  • 38
    • 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
  • 41
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO. A role in transcriptional regulation
    • Verger, A., Perdomo, J., and Crossley, M. (2003) Modification with SUMO. A role in transcriptional regulation, EMBO Rep. 4, 137-142.
    • (2003) EMBO Rep. , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 42
    • 0032031606 scopus 로고    scopus 로고
    • Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo
    • Wang, L., Liu, L., and Berger, S. L. (1998) Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo, Genes Dev. 12, 640-653.
    • (1998) Genes Dev. , vol.12 , pp. 640-653
    • Wang, L.1    Liu, L.2    Berger, S.L.3
  • 43
    • 8544273758 scopus 로고    scopus 로고
    • Global analysis of protein sumoylation in Saccharomyces cerevisiae
    • Wohlschlegel, J. A., Johnson, E. S., Reed, S. I., and Yates, J. R., III (2004) Global analysis of protein sumoylation in Saccharomyces cerevisiae, J. Biol. Chem. 279, 45662-45668.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45662-45668
    • Wohlschlegel, J.A.1    Johnson, E.S.2    Reed, S.I.3    Yates III, J.R.4
  • 44
    • 7044250740 scopus 로고    scopus 로고
    • Lysine acetylation and the bromodomain: A new partnership for signaling
    • Yang, X. J. (2004) Lysine acetylation and the bromodomain: a new partnership for signaling, BioEssays 26, 1076-1087.
    • (2004) BioEssays , vol.26 , pp. 1076-1087
    • Yang, X.J.1


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