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Volumn 49, Issue 5, 2003, Pages 1297-1307

Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; KARYOPHERIN; NUCLEOLIN; PROTEIN DPH2P; PROTEIN EFT2P; PROTEIN RPS19AP; PROTEIN RPS7AP; PROTEIN SUBUNIT; PROTEIN YIL103WP; RIBOSOME PROTEIN; RNA POLYMERASE II; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0141454918     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03632.x     Document Type: Article
Times cited : (83)

References (53)
  • 1
    • 0034004690 scopus 로고    scopus 로고
    • Type 1 protein phosphatase is required for maintenance of cell wall integrity, morphogenesis and cell cycle progression in Saccharomyces cerevisiae
    • Andrews, P.D., and Stark, M.J.R. (2000) Type 1 protein phosphatase is required for maintenance of cell wall integrity, morphogenesis and cell cycle progression in Saccharomyces cerevisiae. J Cell Sci 113: 507-520.
    • (2000) J Cell Sci , vol.113 , pp. 507-520
    • Andrews, P.D.1    Stark, M.J.R.2
  • 2
    • 0029977005 scopus 로고    scopus 로고
    • The yeast homolog of mammalian ribosomal protein S30 is expressed from a duplicated gene without a ubiquitin-like protein fusion sequence. Evolutionary implications
    • Baker, R.T., Williamson, N.A., and Wettenhall, R.E. (1996) The yeast homolog of mammalian ribosomal protein S30 is expressed from a duplicated gene without a ubiquitin-like protein fusion sequence. Evolutionary implications. J Biol Chem 271: 13549-13555.
    • (1996) J Biol Chem , vol.271 , pp. 13549-13555
    • Baker, R.T.1    Williamson, N.A.2    Wettenhall, R.E.3
  • 3
    • 0025770120 scopus 로고
    • Intracellular expression of Kluyveromyces lactis toxin gamma subunit mimics treatment with exogenous toxin and distinguishes two classes of toxin-resistant mutant
    • Butler, A.R., Porter, M., and Stark, M.J. (1991) Intracellular expression of Kluyveromyces lactis toxin gamma subunit mimics treatment with exogenous toxin and distinguishes two classes of toxin-resistant mutant. Yeast 7: 617-625.
    • (1991) Yeast , vol.7 , pp. 617-625
    • Butler, A.R.1    Porter, M.2    Stark, M.J.3
  • 4
    • 0027980497 scopus 로고
    • Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin
    • Butler, A.R., White, J.H., Folawiyo, Y., Edlin, A., Gardiner, D., and Stark, M.J.R. (1994) Two Saccharomyces cerevisiae genes which control sensitivity to G1 arrest induced by Kluyveromyces lactis toxin. Mol Cell Biol 14: 6306-6316.
    • (1994) Mol Cell Biol , vol.14 , pp. 6306-6316
    • Butler, A.R.1    White, J.H.2    Folawiyo, Y.3    Edlin, A.4    Gardiner, D.5    Stark, M.J.R.6
  • 5
    • 0034730176 scopus 로고    scopus 로고
    • A STAT3-interacting protein (StlP1) regulates cytokine signal transduction
    • Collum, R.G., Brutsaert, S., Lee, G., and Schindler, C. (2000) A STAT3-interacting protein (StlP1) regulates cytokine signal transduction. Proc Natl Acad Sci USA 97: 10120-10125.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10120-10125
    • Collum, R.G.1    Brutsaert, S.2    Lee, G.3    Schindler, C.4
  • 6
    • 0025200729 scopus 로고
    • Cell cycle arrest caused by CLN gene deficiency in Saccharomyces cerevisiae resembles START-I arrest and is independent of the mating pheromone signalling pathway
    • Cross, F.R. (1990) Cell cycle arrest caused by CLN gene deficiency in Saccharomyces cerevisiae resembles START-I arrest and is independent of the mating pheromone signalling pathway. Mol Cell Biol 10: 6482-6490.
    • (1990) Mol Cell Biol , vol.10 , pp. 6482-6490
    • Cross, F.R.1
  • 7
    • 0036091217 scopus 로고    scopus 로고
    • KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin
    • Fichtner, L., and Schaffrath, R. (2002) KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Microbiol 44: 865-875.
    • (2002) Mol Microbiol , vol.44 , pp. 865-875
    • Fichtner, L.1    Schaffrath, R.2
  • 8
    • 0036267462 scopus 로고    scopus 로고
    • Molecular analysis of KTI12/TOT4, a Saccharomyces cerevisiae gene required for Kluyveromyces lactis zymocin action
    • Fichtner, L., Frohloff, F., Bürkner, K., Larsen, M., Breunig, K.D., and Schaffrath, R. (2002a) Molecular analysis of KTI12/TOT4, a Saccharomyces cerevisiae gene required for Kluyveromyces lactis zymocin action. Mol Microbiol 43: 783-791.
    • (2002) Mol Microbiol , vol.43 , pp. 783-791
    • Fichtner, L.1    Frohloff, F.2    Bürkner, K.3    Larsen, M.4    Breunig, K.D.5    Schaffrath, R.6
  • 9
    • 0036360126 scopus 로고    scopus 로고
    • Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity
    • Fichtner, L., Frohloff, F., Jablonowski, D., Stark, M.J.R., and Schaffrath, R. (2002b) Protein interactions within Saccharomyces cerevisiae Elongator, a complex essential for Kluyveromyces lactis zymocicity. Mol Microbiol 45: 817-826.
    • (2002) Mol Microbiol , vol.45 , pp. 817-826
    • Fichtner, L.1    Frohloff, F.2    Jablonowski, D.3    Stark, M.J.R.4    Schaffrath, R.5
  • 10
    • 0035901529 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
    • Frohloff, F., Fichtner, L., Jablonowski, D., Breunig, K.D., and Schaffrath, R. (2001) Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin. EMBO J 20: 1993-2003.
    • (2001) EMBO J , vol.20 , pp. 1993-2003
    • Frohloff, F.1    Fichtner, L.2    Jablonowski, D.3    Breunig, K.D.4    Schaffrath, R.5
  • 11
    • 0037428386 scopus 로고    scopus 로고
    • Subunit communications crucial for the functional integrity of the yeast RNA polymerase II Elongator (γ-toxin target TOT) complex
    • Frohloff, F., Jablonowski, D., Fichtner, L., and Schaffrath, R. (2003) Subunit communications crucial for the functional integrity of the yeast RNA polymerase II Elongator (γ-toxin target TOT) complex. J Biol Chem 278: 956-961.
    • (2003) J Biol Chem , vol.278 , pp. 956-961
    • Frohloff, F.1    Jablonowski, D.2    Fichtner, L.3    Schaffrath, R.4
  • 12
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
    • Furukawa, K., Mizushima, N., Noda, T., and Ohsumi, Y. (2000) A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J Biol Chem 275: 7462-7465.
    • (2000) J Biol Chem , vol.275 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 13
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., St Jean, A., Woods, R.A., and Schiestl, R.H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res 20: 1425.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 15
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito, T., Chiba, T., Ozawa, R., Yoshida, M., Hattori, M., and Sakaki, Y. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci USA 98: 4569-4574.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4569-4574
    • Ito, T.1    Chiba, T.2    Ozawa, R.3    Yoshida, M.4    Hattori, M.5    Sakaki, Y.6
  • 16
    • 0037135604 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RNA polymerase II is affected by Kluyveromyces lactis zymocin
    • Jablonowski, D., and Schaffrath, R. (2002) Saccharomyces cerevisiae RNA polymerase II is affected by Kluyveromyces lactis zymocin. J Biol Chem 277: 26276-26280.
    • (2002) J Biol Chem , vol.277 , pp. 26276-26280
    • Jablonowski, D.1    Schaffrath, R.2
  • 18
    • 0035175582 scopus 로고    scopus 로고
    • Kluyveromyces lactis zymocin mode of action is linked to RNA polymerase II function via Elongator
    • Jablonowski, D., Frohloff, F., Fichtner, L., Stark, M.J.R., and Schaffrath, R. (2001b) Kluyveromyces lactis zymocin mode of action is linked to RNA polymerase II function via Elongator. Mol Microbiol 42: 1095-1105.
    • (2001) Mol Microbiol , vol.42 , pp. 1095-1105
    • Jablonowski, D.1    Frohloff, F.2    Fichtner, L.3    Stark, M.J.R.4    Schaffrath, R.5
  • 19
    • 0035697437 scopus 로고    scopus 로고
    • Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin
    • Jablonowski, D., Butler, A.R., Fichtner, L., Gardiner, D., Schaffrath, R., and Stark, M.J.R. (2001c) Sit4p protein phosphatase is required for sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin. Genetics 159: 1479-1489.
    • (2001) Genetics , vol.159 , pp. 1479-1489
    • Jablonowski, D.1    Butler, A.R.2    Fichtner, L.3    Gardiner, D.4    Schaffrath, R.5    Stark, M.J.R.6
  • 20
    • 0037022226 scopus 로고    scopus 로고
    • Human Elongator facilitates RNA polymerase II transcription through chromatin
    • Kim, J.-H., Lane, W.S., and Reinberg, D. (2002) Human Elongator facilitates RNA polymerase II transcription through chromatin. Proc Natl Acad Sci USA 99: 1241-12461.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1241-12461
    • Kim, J.-H.1    Lane, W.S.2    Reinberg, D.3
  • 21
    • 0036384945 scopus 로고    scopus 로고
    • Defects in yeast RNA polymerase II transcription elicit hypersensitivity to G1 arrest induced by Kluyveromyces lactis zymocin
    • Kitamoto, H.K., Jablonowski, D., Nagase, J., and Schaffrath, R. (2002) Defects in yeast RNA polymerase II transcription elicit hypersensitivity to G1 arrest induced by Kluyveromyces lactis zymocin. Mol Genet Genomics 268: 49-55.
    • (2002) Mol Genet Genomics , vol.268 , pp. 49-55
    • Kitamoto, H.K.1    Jablonowski, D.2    Nagase, J.3    Schaffrath, R.4
  • 22
    • 0032775010 scopus 로고    scopus 로고
    • Epitope tagging of yeast genes using a PCR-based strategy: More tags and improved practical routines
    • Knop, M., Siegers, K., Pereira, G., Zachariae, W., Winsor, B., Nasmyth, K., and Schiebel, E. (1999) Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines. Yeast 15: 963-972.
    • (1999) Yeast , vol.15 , pp. 963-972
    • Knop, M.1    Siegers, K.2    Pereira, G.3    Zachariae, W.4    Winsor, B.5    Nasmyth, K.6    Schiebel, E.7
  • 23
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kölling, R., and Hollenberg, C.P. (1994) The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J 13: 3261-3271.
    • (1994) EMBO J , vol.13 , pp. 3261-3271
    • Kölling, R.1    Hollenberg, C.P.2
  • 24
    • 0035171624 scopus 로고    scopus 로고
    • Characterization of a six-subunit holo-Elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae
    • Krogan, N.J., and Greenblatt, J.F. (2001) Characterization of a six-subunit holo-Elongator complex required for the regulated expression of a group of genes in Saccharomyces cerevisiae. Mol Cell Biol 21: 8203-8212.
    • (2001) Mol Cell Biol , vol.21 , pp. 8203-8212
    • Krogan, N.J.1    Greenblatt, J.F.2
  • 25
    • 0036787862 scopus 로고    scopus 로고
    • RNA polymerase II elongation factors of Saccharomyces cerevisiae: A targeted proteomics approach
    • Krogan, N.J., Kim, M., Ahn, S.H., Zhong, G., Kobor, M.S., Cagney, G., et al. (2002) RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Mol Cell Biol 22: 6979-6992.
    • (2002) Mol Cell Biol , vol.22 , pp. 6979-6992
    • Krogan, N.J.1    Kim, M.2    Ahn, S.H.3    Zhong, G.4    Kobor, M.S.5    Cagney, G.6
  • 28
    • 0027442619 scopus 로고
    • Diphthamide synthesis in Saccharomyces cerevisiae: Structure of the DPH2 gene
    • Mattheakis, L.C., Sor, F., and Collier, R.J. (1993) Diphthamide synthesis in Saccharomyces cerevisiae: structure of the DPH2 gene. Gene 132: 149-154.
    • (1993) Gene , vol.132 , pp. 149-154
    • Mattheakis, L.C.1    Sor, F.2    Collier, R.J.3
  • 29
    • 0038280146 scopus 로고    scopus 로고
    • Mutant casein kinase I (Hrr25p/Ktl14p) abrogates the G1 cell cycle arrest induced by Kluyveromyces lactis zymocin in budding yeast
    • Mehlgarten, C., and Schaffrath, R. (2003) Mutant casein kinase I (Hrr25p/Ktl14p) abrogates the G1 cell cycle arrest induced by Kluyveromyces lactis zymocin in budding yeast. Mol Genet Genomics 269: 188-196.
    • (2003) Mol Genet Genomics , vol.269 , pp. 188-196
    • Mehlgarten, C.1    Schaffrath, R.2
  • 30
    • 0029953712 scopus 로고    scopus 로고
    • Green fluorescent protein as a marker for gene expression and subcellular localization in budding yeast
    • Niedenthal, R.K., Riles, L., Johnston, M., and Hegemann, J.H. (1996) Green fluorescent protein as a marker for gene expression and subcellular localization in budding yeast. Yeast 12: 773-786.
    • (1996) Yeast , vol.12 , pp. 773-786
    • Niedenthal, R.K.1    Riles, L.2    Johnston, M.3    Hegemann, J.H.4
  • 31
    • 0032971711 scopus 로고    scopus 로고
    • Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation
    • Otero, G., Fellows, J., Li, Y., de Bizemont, T., Dirac, A.M., Gustafsson, C.M., et al. (1999) Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Mol Cell 3: 109-118.
    • (1999) Mol Cell , vol.3 , pp. 109-118
    • Otero, G.1    Fellows, J.2    Li, Y.3    De Bizemont, T.4    Dirac, A.M.5    Gustafsson, C.M.6
  • 32
    • 0031898099 scopus 로고    scopus 로고
    • Spc98p directs the yeast γ-tubulin complex into the nucleus and is subject to cell cycle-dependent phosphorylation on the nuclear side of the spindle pole body
    • Pereira, G., Knop, M., and Schiebel, E. (1998) Spc98p directs the yeast γ-tubulin complex into the nucleus and is subject to cell cycle-dependent phosphorylation on the nuclear side of the spindle pole body. Mol Biol Cell 9: 775-793.
    • (1998) Mol Biol Cell , vol.9 , pp. 775-793
    • Pereira, G.1    Knop, M.2    Schiebel, E.3
  • 33
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D.N., Pappin, D.J., Creasy, D.M., and Cotrell, J.S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cotrell, J.S.4
  • 34
    • 0032579887 scopus 로고    scopus 로고
    • The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae
    • Planta, R.J., and Mager, W.H. (1998) The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast 14: 471-477.
    • (1998) Yeast , vol.14 , pp. 471-477
    • Planta, R.J.1    Mager, W.H.2
  • 35
    • 0036241663 scopus 로고    scopus 로고
    • Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo
    • Pokholok, D.K., Hannett, N.M., and Young, R.A. (2002) Exchange of RNA polymerase II initiation and elongation factors during gene expression in vivo. Mol Cell 9: 799-809.
    • (2002) Mol Cell , vol.9 , pp. 799-809
    • Pokholok, D.K.1    Hannett, N.M.2    Young, R.A.3
  • 36
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O., Caspary, F., Rigaut, G., Rutz, B., Bouveret, E., Bragado-Nilsson, E., et al. (2001) The tandem affinity purification (TAP) method: a general procedure of protein complex purification. Methods 24: 218-229.
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6
  • 37
    • 0024834127 scopus 로고
    • An essential G1 function for cyclin-like proteins in yeast
    • Richardson, H.E., Wittenberg, C., Cross, F., and Reed, S.I. (1989) An essential G1 function for cyclin-like proteins in yeast. Cell 59: 1127-1133.
    • (1989) Cell , vol.59 , pp. 1127-1133
    • Richardson, H.E.1    Wittenberg, C.2    Cross, F.3    Reed, S.I.4
  • 38
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture and transport mechanism
    • Rout, M.P., Aitchison, J.D., Suprapto, A., Hjertaas, K., Zhao, Y., and Chait, B.T. (2000) The yeast nuclear pore complex: composition, architecture and transport mechanism. J Cell Biol 148: 635-651.
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 39
    • 0033764315 scopus 로고    scopus 로고
    • Genetics and molecular physiology of the yeast Kluyveromyces lactis
    • Schaffrath, R., and Breunig, K.D. (2000) Genetics and molecular physiology of the yeast Kluyveromyces lactis. Fungal Genet Biol 30: 173-190.
    • (2000) Fungal Genet Biol , vol.30 , pp. 173-190
    • Schaffrath, R.1    Breunig, K.D.2
  • 40
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. (1991) Getting started with yeast. Methods Enzymol 194: 3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 41
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silverstained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silverstained 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
  • 43
    • 0033730418 scopus 로고    scopus 로고
    • Factors affecting nuclear export of the 60S ribosomal subunit in vivo
    • Stage-Zimmermann, T., Schmidt, U., and Silver, P.A. (2000) Factors affecting nuclear export of the 60S ribosomal subunit in vivo. Mol Biol Cell 11: 3777-3789.
    • (2000) Mol Biol Cell , vol.11 , pp. 3777-3789
    • Stage-Zimmermann, T.1    Schmidt, U.2    Silver, P.A.3
  • 44
    • 0022763345 scopus 로고
    • The killer toxin of Kluyveromyces lactis: Characterization of the toxin subunits and identification of the genes which encode them
    • Stark, M.J., and Boyd, A. (1986) The killer toxin of Kluyveromyces lactis: characterization of the toxin subunits and identification of the genes which encode them. EMBO J 5: 1995-2002.
    • (1986) EMBO J , vol.5 , pp. 1995-2002
    • Stark, M.J.1    Boyd, A.2
  • 45
    • 0035934273 scopus 로고    scopus 로고
    • A mutation in the largest (catalytic) subunit of RNA polymerase II and its relation to arrest of the cell cycle in G(1) phase
    • Sugaya, K., Sasanuma, S., Cook, P.R., and Mita, K. (2001) A mutation in the largest (catalytic) subunit of RNA polymerase II and its relation to arrest of the cell cycle in G(1) phase. Gene 274: 77-81.
    • (2001) Gene , vol.274 , pp. 77-81
    • Sugaya, K.1    Sasanuma, S.2    Cook, P.R.3    Mita, K.4
  • 46
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong, A.H., Evangelista, M., Parsons, A.B., Xu, H., Bader, G.D., Page, N., et al. (2001) Systematic genetic analysis with ordered arrays of yeast deletion mutants. Science 294: 2364-2368.
    • (2001) Science , vol.294 , pp. 2364-2368
    • Tong, A.H.1    Evangelista, M.2    Parsons, A.B.3    Xu, H.4    Bader, G.D.5    Page, N.6
  • 47
    • 0028091457 scopus 로고
    • Differential transcription of the two Saccharomyces cerevisiae genes encoding elongation factor 2
    • Veldman, S., Rao, S., and Bodley, J.W. (1994) Differential transcription of the two Saccharomyces cerevisiae genes encoding elongation factor 2. Gene 148: 143-147.
    • (1994) Gene , vol.148 , pp. 143-147
    • Veldman, S.1    Rao, S.2    Bodley, J.W.3
  • 48
    • 0037133234 scopus 로고    scopus 로고
    • Novel interactions of Saccharomyces cerevisiae type 1 protein phosphatase identified by single step affinity purification and mass spectrometry
    • Walsh, E.P., Lamont, D.J., Beattie, K.A., and Stark, M.J.R. (2002) Novel interactions of Saccharomyces cerevisiae type 1 protein phosphatase identified by single step affinity purification and mass spectrometry. Biochemistry 41: 2409-2420.
    • (2002) Biochemistry , vol.41 , pp. 2409-2420
    • Walsh, E.P.1    Lamont, D.J.2    Beattie, K.A.3    Stark, M.J.R.4
  • 50
    • 0037133562 scopus 로고    scopus 로고
    • Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo
    • Winkler, G.S., Kristjuhan, A., Erdjument-Bromage, H., Tempst, P., and Svejstrup, J.Q. (2002) Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proc Natl Acad Sci USA 99: 3517-3522.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3517-3522
    • Winkler, G.S.1    Kristjuhan, A.2    Erdjument-Bromage, H.3    Tempst, P.4    Svejstrup, J.Q.5
  • 51
    • 0033166761 scopus 로고    scopus 로고
    • A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme
    • Wittschieben, B.O., Otero, G., de Bizemont, T., Fellows, J., Erdjument-Bromage, H., Ohba, R., et al. (1999) A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. Mol Cell 4: 123-128.
    • (1999) Mol Cell , vol.4 , pp. 123-128
    • Wittschieben, B.O.1    Otero, G.2    De Bizemont, T.3    Fellows, J.4    Erdjument-Bromage, H.5    Ohba, R.6
  • 52
    • 0035911152 scopus 로고    scopus 로고
    • The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins
    • Yoshida, K., and Blobel, G. (2001) The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins. J Ceil Biol 152: 729-739.
    • (2001) J Ceil Biol , vol.152 , pp. 729-739
    • Yoshida, K.1    Blobel, G.2
  • 53
    • 0343829343 scopus 로고    scopus 로고
    • Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae
    • Zachariae, W., Shin, T.H., Galova, M., Obermaier, B., and Nasmyth, K. (1996) Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae. Science 274: 1201-1204.
    • (1996) Science , vol.274 , pp. 1201-1204
    • Zachariae, W.1    Shin, T.H.2    Galova, M.3    Obermaier, B.4    Nasmyth, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.