메뉴 건너뛰기




Volumn 9, Issue 2, 2013, Pages

The Amidation Step of Diphthamide Biosynthesis in Yeast Requires DPH6, a Gene Identified through Mining the DPH1-DPH5 Interaction Network

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMIDASE; DIPHTHAMIDE; DIPHTHERIA TOXIN; ELONGATION FACTOR 2; HISTIDINE; SORDARIN; UNCLASSIFIED DRUG;

EID: 84874772792     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1003334     Document Type: Article
Times cited : (49)

References (85)
  • 1
    • 77149158441 scopus 로고    scopus 로고
    • Unrestricted identification of modified proteins using MS/MS
    • Ahrne E, Muller M, Lisacek F, (2010) Unrestricted identification of modified proteins using MS/MS. Proteomics 10: 671-686.
    • (2010) Proteomics , vol.10 , pp. 671-686
    • Ahrne, E.1    Muller, M.2    Lisacek, F.3
  • 3
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: the chemistry of proteome diversifications
    • Walsh CT, Garneau-Tsodikova S, Gatto GJJ, (2005) Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed Engl 44: 7342-7372.
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.J.3
  • 4
    • 79960576138 scopus 로고    scopus 로고
    • Unique modifications of translation elongation factors
    • Greganova E, Altmann M, Butikofer P, (2011) Unique modifications of translation elongation factors. FEBS J 278: 2613-2624.
    • (2011) FEBS J , vol.278 , pp. 2613-2624
    • Greganova, E.1    Altmann, M.2    Butikofer, P.3
  • 5
    • 0019333178 scopus 로고
    • ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products
    • Van Ness BG, Howard JB, Bodley JW, (1980) ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products. J Biol Chem 255: 10710-10716.
    • (1980) J Biol Chem , vol.255 , pp. 10710-10716
    • Van Ness, B.G.1    Howard, J.B.2    Bodley, J.W.3
  • 6
    • 49349093245 scopus 로고    scopus 로고
    • A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3
    • Bär C, Zabel R, Liu S, Stark MJ, Schaffrath R, (2008) A versatile partner of eukaryotic protein complexes that is involved in multiple biological processes: Kti11/Dph3. Mol Microbiol 69: 1221-1233.
    • (2008) Mol Microbiol , vol.69 , pp. 1221-1233
    • Bär, C.1    Zabel, R.2    Liu, S.3    Stark, M.J.4    Schaffrath, R.5
  • 7
    • 42949164918 scopus 로고    scopus 로고
    • A chemical genomic screen in Saccharomyces cerevisiae reveals a role for diphthamidation of translation elongation factor 2 in inhibition of protein synthesis by sordarin
    • Botet J, Rodriguez-Mateos M, Ballesta JP, Revuelta JL, Remacha M, (2008) A chemical genomic screen in Saccharomyces cerevisiae reveals a role for diphthamidation of translation elongation factor 2 in inhibition of protein synthesis by sordarin. Antimicrob Agents Chemother 52: 1623-1629.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1623-1629
    • Botet, J.1    Rodriguez-Mateos, M.2    Ballesta, J.P.3    Revuelta, J.L.4    Remacha, M.5
  • 8
    • 0019333247 scopus 로고
    • ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products
    • Van Ness BG, Howard JB, Bodley JW, (1980) ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products. J Biol Chem 255: 10717-107120.
    • (1980) J Biol Chem , vol.255 , pp. 10717-107120
    • Van Ness, B.G.1    Howard, J.B.2    Bodley, J.W.3
  • 9
    • 0033529540 scopus 로고    scopus 로고
    • Sordarin inhibits fungal protein synthesis by blocking translocation differently to fusidic acid
    • Dominguez JM, Gomez-Lorenzo MG, Martin JJ, (1999) Sordarin inhibits fungal protein synthesis by blocking translocation differently to fusidic acid. J Biol Chem 274: 22423-22427.
    • (1999) J Biol Chem , vol.274 , pp. 22423-22427
    • Dominguez, J.M.1    Gomez-Lorenzo, M.G.2    Martin, J.J.3
  • 10
    • 0242516080 scopus 로고    scopus 로고
    • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
    • Jørgensen R, Ortiz PA, Carr-Schmid A, Nissen P, Kinzy TG, et al. (2003) Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Nat Struct Biol 10: 379-385.
    • (2003) Nat Struct Biol , vol.10 , pp. 379-385
    • Jørgensen, R.1    Ortiz, P.A.2    Carr-Schmid, A.3    Nissen, P.4    Kinzy, T.G.5
  • 11
    • 0019819635 scopus 로고
    • Diphtheria toxin. Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2
    • Oppenheimer NJ, Bodley JW, (1981) Diphtheria toxin. Site and configuration of ADP-ribosylation of diphthamide in elongation factor 2. J Biol Chem 256: 8579-8581.
    • (1981) J Biol Chem , vol.256 , pp. 8579-8581
    • Oppenheimer, N.J.1    Bodley, J.W.2
  • 14
    • 0022352148 scopus 로고
    • Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae
    • Chen JY, Bodley JW, Livingston DM, (1985) Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae. Mol Cell Biol 5: 3357-3360.
    • (1985) Mol Cell Biol , vol.5 , pp. 3357-3360
    • Chen, J.Y.1    Bodley, J.W.2    Livingston, D.M.3
  • 15
    • 0141527346 scopus 로고    scopus 로고
    • Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins
    • Liu S, Leppla SH, (2003) Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins. Mol Cell 12: 603-613.
    • (2003) Mol Cell , vol.12 , pp. 603-613
    • Liu, S.1    Leppla, S.H.2
  • 16
    • 6344252525 scopus 로고    scopus 로고
    • Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2
    • Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH, (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24: 9487-9497.
    • (2004) Mol Cell Biol , vol.24 , pp. 9487-9497
    • Liu, S.1    Milne, G.T.2    Kuremsky, J.G.3    Fink, G.R.4    Leppla, S.H.5
  • 17
    • 0020519742 scopus 로고
    • Biosynthetic labeling of diphthamide in Saccharomyces cerevisiae
    • Dunlop PC, Bodley JW, (1983) Biosynthetic labeling of diphthamide in Saccharomyces cerevisiae. J Biol Chem 258: 4754-4758.
    • (1983) J Biol Chem , vol.258 , pp. 4754-4758
    • Dunlop, P.C.1    Bodley, J.W.2
  • 18
    • 80053560047 scopus 로고    scopus 로고
    • S-adenosylmethionine-dependent alkylation reactions: when are radical reactions used?
    • Lin H, (2011) S-adenosylmethionine-dependent alkylation reactions: when are radical reactions used? Bioorg Chem 39: 161-170.
    • (2011) Bioorg Chem , vol.39 , pp. 161-170
    • Lin, H.1
  • 19
    • 0018862384 scopus 로고
    • Posttranslational modification of elongation factor 2 in diphtheria-toxin-resistant mutants of CHO-K1 cells
    • Moehring JM, Moehring TJ, Danley DE, (1980) Posttranslational modification of elongation factor 2 in diphtheria-toxin-resistant mutants of CHO-K1 cells. Proc Natl Acad Sci USA 77: 1010-1014.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1010-1014
    • Moehring, J.M.1    Moehring, T.J.2    Danley, D.E.3
  • 20
    • 0141454918 scopus 로고    scopus 로고
    • Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification
    • Fichtner L, Jablonowski D, Schierhorn A, Kitamoto HK, Stark MJ, et al. (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49: 1297-1307.
    • (2003) Mol Microbiol , vol.49 , pp. 1297-1307
    • Fichtner, L.1    Jablonowski, D.2    Schierhorn, A.3    Kitamoto, H.K.4    Stark, M.J.5
  • 21
    • 77953723343 scopus 로고    scopus 로고
    • Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme
    • Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, et al. (2010) Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature 465: 891-896.
    • (2010) Nature , vol.465 , pp. 891-896
    • Zhang, Y.1    Zhu, X.2    Torelli, A.T.3    Lee, M.4    Dzikovski, B.5
  • 22
    • 78650116470 scopus 로고    scopus 로고
    • Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis
    • Zhu X, Dzikovski B, Su X, Torelli AT, Zhang Y, et al. (2011) Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis. Mol Biosyst 7: 74-81.
    • (2011) Mol Biosyst , vol.7 , pp. 74-81
    • Zhu, X.1    Dzikovski, B.2    Su, X.3    Torelli, A.T.4    Zhang, Y.5
  • 23
    • 36448989752 scopus 로고    scopus 로고
    • Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain
    • Proudfoot M, Sanders SA, Singer A, Zhang R, Brown G, et al. (2008) Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain. J Mol Biol 375: 301-315.
    • (2008) J Mol Biol , vol.375 , pp. 301-315
    • Proudfoot, M.1    Sanders, S.A.2    Singer, A.3    Zhang, R.4    Brown, G.5
  • 24
    • 84859779168 scopus 로고    scopus 로고
    • Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4
    • Thakur A, Chitoor B, Goswami AV, Pareek G, Atreya HS, et al. (2012) Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. J Biol Chem 287: 13194-13205.
    • (2012) J Biol Chem , vol.287 , pp. 13194-13205
    • Thakur, A.1    Chitoor, B.2    Goswami, A.V.3    Pareek, G.4    Atreya, H.S.5
  • 25
    • 0036091217 scopus 로고    scopus 로고
    • KTI11 and KTI13, Saccharomyces cerevisiae genes controlling sensitivity to G1 arrest induced by Kluyveromyces lactis zymocin
    • Fichtner L, 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
  • 26
    • 58649104923 scopus 로고    scopus 로고
    • An iron-sulfur cluster domain in Elp3 important for the structural integrity of elongator
    • Greenwood C, Selth LA, Dirac-Svejstrup AB, Svejstrup JQ, (2009) An iron-sulfur cluster domain in Elp3 important for the structural integrity of elongator. J Biol Chem 284: 141-149.
    • (2009) J Biol Chem , vol.284 , pp. 141-149
    • Greenwood, C.1    Selth, L.A.2    Dirac-Svejstrup, A.B.3    Svejstrup, J.Q.4
  • 27
    • 15444371415 scopus 로고    scopus 로고
    • An early step in wobble uridine tRNA modification requires the Elongator complex
    • Huang B, Johansson MJ, Byström AS, (2005) An early step in wobble uridine tRNA modification requires the Elongator complex. RNA 11: 424-436.
    • (2005) RNA , vol.11 , pp. 424-436
    • Huang, B.1    Johansson, M.J.2    Byström, A.S.3
  • 28
    • 33645070795 scopus 로고    scopus 로고
    • The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine
    • Paraskevopoulou C, Fairhurst SA, Lowe DJ, Brick P, Onesti S, (2006) The Elongator subunit Elp3 contains a Fe4S4 cluster and binds S-adenosylmethionine. Mol Microbiol 59: 795-806.
    • (2006) Mol Microbiol , vol.59 , pp. 795-806
    • Paraskevopoulou, C.1    Fairhurst, S.A.2    Lowe, D.J.3    Brick, P.4    Onesti, S.5
  • 29
    • 0023724627 scopus 로고
    • Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase
    • Chen JY, Bodley JW, (1988) Biosynthesis of diphthamide in Saccharomyces cerevisiae. Partial purification and characterization of a specific S-adenosylmethionine:elongation factor 2 methyltransferase. J Biol Chem 263: 11692-11696.
    • (1988) J Biol Chem , vol.263 , pp. 11692-11696
    • Chen, J.Y.1    Bodley, J.W.2
  • 30
    • 0026746489 scopus 로고
    • DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae
    • Mattheakis LC, Shen WH, Collier RJ, (1992) DPH5, a methyltransferase gene required for diphthamide biosynthesis in Saccharomyces cerevisiae. Mol Cell Biol 12: 4026-4037.
    • (1992) Mol Cell Biol , vol.12 , pp. 4026-4037
    • Mattheakis, L.C.1    Shen, W.H.2    Collier, R.J.3
  • 31
    • 0021251336 scopus 로고
    • In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin
    • Moehring TJ, Danley DE, Moehring JM, (1984) In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin. Mol Cell Biol 4: 642-650.
    • (1984) Mol Cell Biol , vol.4 , pp. 642-650
    • Moehring, T.J.1    Danley, D.E.2    Moehring, J.M.3
  • 32
    • 78149346156 scopus 로고    scopus 로고
    • Reconstitution of diphthine synthase activity in vitro
    • Zhu X, Kim J, Su X, Lin H, (2010) Reconstitution of diphthine synthase activity in vitro. Biochemistry 49: 9649-9657.
    • (2010) Biochemistry , vol.49 , pp. 9649-9657
    • Zhu, X.1    Kim, J.2    Su, X.3    Lin, H.4
  • 33
    • 46249109336 scopus 로고    scopus 로고
    • The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A
    • Zhang Y, Liu S, Lajoie G, Merrill AR, (2008) The role of the diphthamide-containing loop within eukaryotic elongation factor 2 in ADP-ribosylation by Pseudomonas aeruginosa exotoxin A. Biochem J 413: 163-174.
    • (2008) Biochem J , vol.413 , pp. 163-174
    • Zhang, Y.1    Liu, S.2    Lajoie, G.3    Merrill, A.R.4
  • 36
    • 33845951105 scopus 로고    scopus 로고
    • Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance
    • Ortiz PA, Ulloque R, Kihara GK, Zheng H, Kinzy TG, (2006) Translation elongation factor 2 anticodon mimicry domain mutants affect fidelity and diphtheria toxin resistance. J Biol Chem 281: 32639-32648.
    • (2006) J Biol Chem , vol.281 , pp. 32639-32648
    • Ortiz, P.A.1    Ulloque, R.2    Kihara, G.K.3    Zheng, H.4    Kinzy, T.G.5
  • 37
    • 0028241366 scopus 로고
    • Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth
    • Kimata Y, Kohno K, (1994) Elongation factor 2 mutants deficient in diphthamide formation show temperature-sensitive cell growth. J Biol Chem 269: 13497-13501.
    • (1994) J Biol Chem , vol.269 , pp. 13497-13501
    • Kimata, Y.1    Kohno, K.2
  • 38
    • 1042278043 scopus 로고    scopus 로고
    • Ovca1 regulates cell proliferation, embryonic development, and tumorigenesis
    • Chen CM, Behringer RR, (2004) Ovca1 regulates cell proliferation, embryonic development, and tumorigenesis. Genes Dev 18: 320-332.
    • (2004) Genes Dev , vol.18 , pp. 320-332
    • Chen, C.M.1    Behringer, R.R.2
  • 39
    • 33646551181 scopus 로고    scopus 로고
    • Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development
    • Liu S, Wiggins JF, Sreenath T, Kulkarni AB, Ward JM, et al. (2006) Dph3, a small protein required for diphthamide biosynthesis, is essential in mouse development. Mol Cell Biol 26: 3835-3841.
    • (2006) Mol Cell Biol , vol.26 , pp. 3835-3841
    • Liu, S.1    Wiggins, J.F.2    Sreenath, T.3    Kulkarni, A.B.4    Ward, J.M.5
  • 40
    • 55449100858 scopus 로고    scopus 로고
    • Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development
    • Webb TR, Cross SH, McKie L, Edgar R, Vizor L, et al. (2008) Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development. J Cell Sci 121: 3140-3145.
    • (2008) J Cell Sci , vol.121 , pp. 3140-3145
    • Webb, T.R.1    Cross, S.H.2    McKie, L.3    Edgar, R.4    Vizor, L.5
  • 41
    • 70849098603 scopus 로고    scopus 로고
    • Haploid genetic screens in human cells identify host factors used by pathogens
    • Carette JE, Guimaraes CP, Varadarajan M, Park AS, Wuethrich I, et al. (2009) Haploid genetic screens in human cells identify host factors used by pathogens. Science 326: 1231-1235.
    • (2009) Science , vol.326 , pp. 1231-1235
    • Carette, J.E.1    Guimaraes, C.P.2    Varadarajan, M.3    Park, A.S.4    Wuethrich, I.5
  • 42
    • 84862972630 scopus 로고    scopus 로고
    • YBR246W is required for the third step of diphthamide biosynthesis
    • Su X, Chen W, Lee W, Jiang H, Zhang S, et al. (2012) YBR246W is required for the third step of diphthamide biosynthesis. J Am Chem Soc 134: 773-776.
    • (2012) J Am Chem Soc , vol.134 , pp. 773-776
    • Su, X.1    Chen, W.2    Lee, W.3    Jiang, H.4    Zhang, S.5
  • 43
    • 77949425833 scopus 로고    scopus 로고
    • Systematic analysis of genome-wide fitness data in yeast reveals novel gene function and drug action
    • Hillenmeyer ME, Ericson E, Davis RW, Nislow C, Koller D, et al. (2010) Systematic analysis of genome-wide fitness data in yeast reveals novel gene function and drug action. Genome Biol 11: R30.
    • (2010) Genome Biol , vol.11
    • Hillenmeyer, M.E.1    Ericson, E.2    Davis, R.W.3    Nislow, C.4    Koller, D.5
  • 46
    • 0035861532 scopus 로고    scopus 로고
    • Systematic genetic analysis with ordered arrays of yeast deletion mutants
    • Tong AH, Evangelista M, Parsons AB, Xu H, Bader GD, 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
  • 47
    • 10744230485 scopus 로고    scopus 로고
    • Global mapping of the yeast genetic interaction network
    • Tong AH, Lesage G, Bader GD, Ding H, Xu H, et al. (2004) Global mapping of the yeast genetic interaction network. Science 303: 808-813.
    • (2004) Science , vol.303 , pp. 808-813
    • Tong, A.H.1    Lesage, G.2    Bader, G.D.3    Ding, H.4    Xu, H.5
  • 50
    • 84874780407 scopus 로고    scopus 로고
    • DRYGIN
    • DRYGIN [http://drygin.ccbr.utoronto.ca/].
  • 51
    • 84874776197 scopus 로고    scopus 로고
    • FitDB
    • FitDB [http://drygin.ccbr.utoronto.ca/].
  • 52
    • 42349100173 scopus 로고    scopus 로고
    • The chemical genomic portrait of yeast: uncovering a phenotype for all genes
    • Hillenmeyer ME, Fung E, Wildenhain J, Pierce SE, Hoon S, et al. (2008) The chemical genomic portrait of yeast: uncovering a phenotype for all genes. Science 320: 362-365.
    • (2008) Science , vol.320 , pp. 362-365
    • Hillenmeyer, M.E.1    Fung, E.2    Wildenhain, J.3    Pierce, S.E.4    Hoon, S.5
  • 53
    • 0032488918 scopus 로고    scopus 로고
    • Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis
    • Justice MC, Hsu MJ, Tse B, Ku T, Balkovec J, et al. (1998) Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis. J Biol Chem 273: 3148-3151.
    • (1998) J Biol Chem , vol.273 , pp. 3148-3151
    • Justice, M.C.1    Hsu, M.J.2    Tse, B.3    Ku, T.4    Balkovec, J.5
  • 54
    • 33846953573 scopus 로고    scopus 로고
    • Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2
    • Søe R, Mosley RT, Justice M, Nielsen-Kahn J, Shastry M, et al. (2007) Sordarin derivatives induce a novel conformation of the yeast ribosome translocation factor eEF2. J Biol Chem 282: 657-666.
    • (2007) J Biol Chem , vol.282 , pp. 657-666
    • Søe, R.1    Mosley, R.T.2    Justice, M.3    Nielsen-Kahn, J.4    Shastry, M.5
  • 55
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression
    • Mumberg D, Muller R, Funk M, (1994) Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res 22: 5767-5768.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 57
    • 1842576803 scopus 로고    scopus 로고
    • Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
    • Spahn CM, Gomez-Lorenzo MG, Grassucci RA, Jorgensen R, Andersen GR, et al. (2004) Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation. EMBO J 23: 1008-1019.
    • (2004) EMBO J , vol.23 , pp. 1008-1019
    • Spahn, C.M.1    Gomez-Lorenzo, M.G.2    Grassucci, R.A.3    Jorgensen, R.4    Andersen, G.R.5
  • 58
    • 26944457020 scopus 로고    scopus 로고
    • Dominant-negative mutant phenotypes and the regulation of translation elongation factor 2 levels in yeast
    • Ortiz PA, Kinzy TG, (2005) Dominant-negative mutant phenotypes and the regulation of translation elongation factor 2 levels in yeast. Nucleic Acids Res 33: 5740-5748.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5740-5748
    • Ortiz, P.A.1    Kinzy, T.G.2
  • 59
    • 0035919680 scopus 로고    scopus 로고
    • Ty1 retrotransposition and programmed +1 ribosomal frameshifting require the integrity of the protein synthetic translocation step
    • Harger JW, Meskauskas A, Nielsen J, Justice MC, Dinman JD, (2001) Ty1 retrotransposition and programmed +1 ribosomal frameshifting require the integrity of the protein synthetic translocation step. Virology 286: 216-224.
    • (2001) Virology , vol.286 , pp. 216-224
    • Harger, J.W.1    Meskauskas, A.2    Nielsen, J.3    Justice, M.C.4    Dinman, J.D.5
  • 60
    • 84872248324 scopus 로고    scopus 로고
    • Comparative genomic analysis of the DUF71/COG2102 family predicts roles in diphthamide biosynthesis and B12 salvage
    • de Crecy-Lagard V, Forouhar F, Brochier-Armanet C, Tong L, Hunt JF, (2012) Comparative genomic analysis of the DUF71/COG2102 family predicts roles in diphthamide biosynthesis and B12 salvage. Biology Direct 7: 32.
    • (2012) Biology Direct , vol.7 , pp. 32
    • de Crecy-Lagard, V.1    Forouhar, F.2    Brochier-Armanet, C.3    Tong, L.4    Hunt, J.F.5
  • 61
    • 84870625500 scopus 로고    scopus 로고
    • Chemogenomic approach identified yeast YLR143W as diphthamide synthetase
    • Su X, Lin Z, Chen W, Jiang H, Zhang S, et al. (2012) Chemogenomic approach identified yeast YLR143W as diphthamide synthetase. Proc Natl Acad Sci USA 109: 19983-19987.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 19983-19987
    • Su, X.1    Lin, Z.2    Chen, W.3    Jiang, H.4    Zhang, S.5
  • 63
    • 34249778986 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family
    • Burman JD, Stevenson CE, Sawers RG, Lawson DM, (2007) The crystal structure of Escherichia coli TdcF, a member of the highly conserved YjgF/YER057c/UK114 family. BMC Struct Biol 7: 30.
    • (2007) BMC Struct Biol , vol.7 , pp. 30
    • Burman, J.D.1    Stevenson, C.E.2    Sawers, R.G.3    Lawson, D.M.4
  • 64
    • 0033539606 scopus 로고    scopus 로고
    • Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family
    • Sinha S, Rappu P, Lange SC, Mantsala P, Zalkin H, et al. (1999) Crystal structure of Bacillus subtilis YabJ, a purine regulatory protein and member of the highly conserved YjgF family. Proc Natl Acad Sci USA 96: 13074-13079.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13074-13079
    • Sinha, S.1    Rappu, P.2    Lange, S.C.3    Mantsala, P.4    Zalkin, H.5
  • 65
    • 0032725980 scopus 로고    scopus 로고
    • A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli
    • Volz K, (1999) A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli. Protein Sci 8: 2428-2437.
    • (1999) Protein Sci , vol.8 , pp. 2428-2437
    • Volz, K.1
  • 66
    • 27544497898 scopus 로고    scopus 로고
    • Structure-based ligand binding sites of protein p14.5, a member of protein family YER057c/YIL051c/YjgF
    • Mistiniene E, Pozdniakovaite N, Popendikyte V, Naktinis V, (2005) Structure-based ligand binding sites of protein p14.5, a member of protein family YER057c/YIL051c/YjgF. Int J Biol Macromol 37: 61-68.
    • (2005) Int J Biol Macromol , vol.37 , pp. 61-68
    • Mistiniene, E.1    Pozdniakovaite, N.2    Popendikyte, V.3    Naktinis, V.4
  • 67
    • 84856267557 scopus 로고    scopus 로고
    • Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5′-phosphate (PLP)-dependent enzyme reactions
    • Lambrecht JA, Flynn JM, Downs DM, (2012) Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5′-phosphate (PLP)-dependent enzyme reactions. J Biol Chem 287: 3454-3461.
    • (2012) J Biol Chem , vol.287 , pp. 3454-3461
    • Lambrecht, J.A.1    Flynn, J.M.2    Downs, D.M.3
  • 68
    • 80655144724 scopus 로고    scopus 로고
    • Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway
    • Shi Y, Stefan CJ, Rue SM, Teis D, Emr SD, (2011) Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway. Mol Biol Cell 22: 4093-4107.
    • (2011) Mol Biol Cell , vol.22 , pp. 4093-4107
    • Shi, Y.1    Stefan, C.J.2    Rue, S.M.3    Teis, D.4    Emr, S.D.5
  • 69
    • 67849106506 scopus 로고    scopus 로고
    • Genetic identification of factors that modulate ribosomal DNA transcription in Saccharomyces cerevisiae
    • Hontz RD, Niederer RO, Johnson JM, Smith JS, (2009) Genetic identification of factors that modulate ribosomal DNA transcription in Saccharomyces cerevisiae. Genetics 182: 105-119.
    • (2009) Genetics , vol.182 , pp. 105-119
    • Hontz, R.D.1    Niederer, R.O.2    Johnson, J.M.3    Smith, J.S.4
  • 70
    • 47549095879 scopus 로고    scopus 로고
    • The diphthamide modification on elongation factor-2 renders mammalian cells resistant to ricin
    • Gupta PK, Liu S, Batavia MP, Leppla SH, (2008) The diphthamide modification on elongation factor-2 renders mammalian cells resistant to ricin. Cell Microbiol 10: 1687-1694.
    • (2008) Cell Microbiol , vol.10 , pp. 1687-1694
    • Gupta, P.K.1    Liu, S.2    Batavia, M.P.3    Leppla, S.H.4
  • 71
    • 84865282692 scopus 로고    scopus 로고
    • Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development
    • Liu S, Bachran C, Gupta P, Miller-Randolph S, Wang H, et al. (2012) Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development. Proc Natl Acad Sci USA 109: 13817-13822.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 13817-13822
    • Liu, S.1    Bachran, C.2    Gupta, P.3    Miller-Randolph, S.4    Wang, H.5
  • 72
    • 15444380476 scopus 로고    scopus 로고
    • Gene trap mutagenesis-based forward genetic approach reveals that the tumor suppressor OVCA1 is a component of the biosynthetic pathway of diphthamide on elongation factor 2
    • Nobukuni Y, Kohno K, Miyagawa K, (2005) Gene trap mutagenesis-based forward genetic approach reveals that the tumor suppressor OVCA1 is a component of the biosynthetic pathway of diphthamide on elongation factor 2. J Biol Chem 280: 10572-10577.
    • (2005) J Biol Chem , vol.280 , pp. 10572-10577
    • Nobukuni, Y.1    Kohno, K.2    Miyagawa, K.3
  • 73
    • 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
  • 74
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St Jean A, Woods RA, Schiestl RH, (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
  • 75
    • 78650819063 scopus 로고    scopus 로고
    • A dominant-negative approach that prevents diphthamide formation confers resistance to Pseudomonas exotoxin A and diphtheria toxin
    • doi:10.1371/journal.pone.0015753
    • Roy V, Ghani K, Caruso M, (2010) A dominant-negative approach that prevents diphthamide formation confers resistance to Pseudomonas exotoxin A and diphtheria toxin. PLoS ONE 5: e15753 doi:10.1371/journal.pone.0015753.
    • (2010) PLoS ONE , vol.5
    • Roy, V.1    Ghani, K.2    Caruso, M.3
  • 76
    • 0034777422 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae cell wall chitin, the Kluyveromyces lactis zymocin receptor
    • Jablonowski D, Fichtner L, Martin VJ, Klassen R, Meinhardt F, et al. (2001) Saccharomyces cerevisiae cell wall chitin, the Kluyveromyces lactis zymocin receptor. Yeast 18: 1285-1299.
    • (2001) Yeast , vol.18 , pp. 1285-1299
    • Jablonowski, D.1    Fichtner, L.2    Martin, V.J.3    Klassen, R.4    Meinhardt, F.5
  • 77
    • 0037428386 scopus 로고    scopus 로고
    • Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-toxin target (TOT)) complex
    • Frohloff F, Jablonowski D, Fichtner L, Schaffrath R, (2003) Subunit communications crucial for the functional integrity of the yeast RNA polymerase II elongator (gamma-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
  • 78
    • 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, et al. (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
  • 79
    • 0343829343 scopus 로고    scopus 로고
    • Identification of subunits of the anaphase-promoting complex of Saccharomyces cerevisiae
    • Zachariae W, Shin TH, Galova M, Obermaier B, 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
  • 80
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz RD, Sugino A, (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74: 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 81
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
    • Janke C, Magiera MM, Rathfelder N, Taxis C, Reber S, et al. (2004) A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast 21: 947-962.
    • (2004) Yeast , vol.21 , pp. 947-962
    • Janke, C.1    Magiera, M.M.2    Rathfelder, N.3    Taxis, C.4    Reber, S.5
  • 82
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M, (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 84
    • 0035901529 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
    • Frohloff F, Fichtner L, Jablonowski D, Breunig KD, 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
  • 85
    • 37749009135 scopus 로고    scopus 로고
    • Zymocin, a composite chitinase and tRNase killer toxin from yeast
    • Jablonowski D, Schaffrath R, (2007) Zymocin, a composite chitinase and tRNase killer toxin from yeast,. Biochem Soc Trans 35: 1533-1537.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1533-1537
    • Jablonowski, D.1    Schaffrath, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.