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Volumn 147, Issue 5, 1999, Pages 981-993

Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins

Author keywords

Cytoskeleton; Protein processing; Septin; Smt3; SUMO

Indexed keywords

CELL PROTEIN; UBIQUITIN;

EID: 0033615965     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.147.5.981     Document Type: Article
Times cited : (334)

References (56)
  • 2
    • 0033555685 scopus 로고    scopus 로고
    • Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast
    • Barral, Y., M. Parra, S. Bidlingmaier, and M. Snyder. 1999. Nim1-related kinases coordinate cell cycle progression with the organization of the peripheral cytoskeleton in yeast. Genes Dev. 13:176-187.
    • (1999) Genes Dev. , vol.13 , pp. 176-187
    • Barral, Y.1    Parra, M.2    Bidlingmaier, S.3    Snyder, M.4
  • 3
    • 0032494183 scopus 로고    scopus 로고
    • Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis
    • Bi, E., P. Maddox, D.J. Lew, E.D. Salmon, J.N. McMillan, E. Yeh, and J.R. Pringle. 1998. Involvement of an actomyosin contractile ring in Saccharomyces cerevisiae cytokinesis. J. Cell Biol. 142:1301-1312.
    • (1998) J. Cell Biol. , vol.142 , pp. 1301-1312
    • Bi, E.1    Maddox, P.2    Lew, D.J.3    Salmon, E.D.4    McMillan, J.N.5    Yeh, E.6    Pringle, J.R.7
  • 4
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance
    • Boeke, J.D., F. LaCroute, and G.R. Fink. 1984. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoroorotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 5
    • 0032476582 scopus 로고    scopus 로고
    • The septins are required for the mitosis-specific activation of the Gin4 kinase
    • Carroll, C.W., R. Altman, D. Schieltz, J.R. Yates, and D. Kellogg. 1998. The septins are required for the mitosis-specific activation of the Gin4 kinase. J. Cell Biol. 143:709-717.
    • (1998) J. Cell Biol. , vol.143 , pp. 709-717
    • Carroll, C.W.1    Altman, R.2    Schieltz, D.3    Yates, J.R.4    Kellogg, D.5
  • 7
    • 0030763146 scopus 로고    scopus 로고
    • A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall
    • DeMarini, D.J., A.E. Adams, H. Fares, C. De Virgilio, G. Valle, J.S. Chuang, and J.R. Pringle. 1997. A septin-based hierarchy of proteins required for localized deposition of chitin in the Saccharomyces cerevisiae cell wall. J. Cell Biol. 139:75-93.
    • (1997) J. Cell Biol. , vol.139 , pp. 75-93
    • DeMarini, D.J.1    Adams, A.E.2    Fares, H.3    De Virgilio, C.4    Valle, G.5    Chuang, J.S.6    Pringle, J.R.7
  • 8
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro, J.M., J. Thomson, and R.T. Hay. 1997. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 417:297-300.
    • (1997) FEBS Lett. , vol.417 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 9
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro, J.M., M.S. Rodriguez, and R.T. Hay. 1998. SUMO-1 modification of IκBα inhibits NF-κB activation. Mol. Cell. 2:233-239.
    • (1998) Mol. Cell. , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 12
    • 0031444358 scopus 로고    scopus 로고
    • An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast
    • Epp, J.A., and J. Chant. 1997. An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Curr. Biol. 7:921-929.
    • (1997) Curr. Biol. , vol.7 , pp. 921-929
    • Epp, J.A.1    Chant, J.2
  • 14
    • 0024004720 scopus 로고
    • Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method
    • Field, J., J. Nikawa, D. Broek, B. MacDonald, L. Rodgers, I.A. Wilson, R.A. Lerner, and M. Wigler. 1988. Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. Mol. Cell. Biol. 8:2159-2165.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2159-2165
    • Field, J.1    Nikawa, J.2    Broek, D.3    MacDonald, B.4    Rodgers, L.5    Wilson, I.A.6    Lerner, R.A.7    Wigler, M.8
  • 15
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
    • Finley, D., E. Özkaynak, and A. Varshavsky. 1987. The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses. Cell. 48:1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • Finley, D.1    Özkaynak, E.2    Varshavsky, A.3
  • 16
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function
    • Frazier, J.A., M.L. Wong, M.S. Longtine, J.R. Pringle, M. Mann, T.J. Mitchison, and C. Field. 1998. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J. Cell Biol. 143:737-749.
    • (1998) J. Cell Biol. , vol.143 , pp. 737-749
    • Frazier, J.A.1    Wong, M.L.2    Longtine, M.S.3    Pringle, J.R.4    Mann, M.5    Mitchison, T.J.6    Field, C.7
  • 17
    • 0030022858 scopus 로고    scopus 로고
    • Peptide-mass profiles of polyvinylidene difluoride-bound proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in the presence of nonionic detergents
    • Gharahdaghi, F., M. Kirchner, J. Fernandez, and S.M. Mische. 1996. Peptide-mass profiles of polyvinylidene difluoride-bound proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in the presence of nonionic detergents. Anal. Biochem. 233:94-99.
    • (1996) Anal. Biochem. , vol.233 , pp. 94-99
    • Gharahdaghi, F.1    Kirchner, M.2    Fernandez, J.3    Mische, S.M.4
  • 18
    • 0031010108 scopus 로고    scopus 로고
    • Functional analysis of the interaction between Afr1p and the Cdc12p septin, two proteins involved in pheromone-induced morphogenesis
    • Giot, L., and J.B. Konopka. 1997. Functional analysis of the interaction between Afr1p and the Cdc12p septin, two proteins involved in pheromone-induced morphogenesis. Mol. Biol. Cell. 8:987-998.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 987-998
    • Giot, L.1    Konopka, J.B.2
  • 19
    • 0030657575 scopus 로고    scopus 로고
    • Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9
    • Gong, L., T. Kamitani, K. Fujise, L.S. Caskey, and E.T. Yeh. 1997. Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9. J. Biol. Chem. 272:28198-28201.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28198-28201
    • Gong, L.1    Kamitani, T.2    Fujise, K.3    Caskey, L.S.4    Yeh, E.T.5
  • 20
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E., and D. Lane. 1988. Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 22
    • 0030826334 scopus 로고    scopus 로고
    • Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p
    • Johnson, E.S., and G. Blobel. 1997. Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p. J. Biol. Chem. 272:26799-26802.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26799-26802
    • Johnson, E.S.1    Blobel, G.2
  • 24
    • 0030794729 scopus 로고    scopus 로고
    • The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer
    • Johnson, E.S., I. Schwienhorst, R.J. Dohmen, and G. Blobel. 1997. The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer. EMBO (Eur. Mol. Biol. Org.) J. 16:5509-5519.
    • (1997) EMBO (Eur. Mol. Biol. Org.) J. , vol.16 , pp. 5509-5519
    • Johnson, E.S.1    Schwienhorst, I.2    Dohmen, R.J.3    Blobel, G.4
  • 25
    • 0032561342 scopus 로고    scopus 로고
    • Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae
    • Kamei, T., K. Tanaka, T. Hihara, M. Umikawa, H. Imamura, M. Kikyo, K. Ozaki, and Y. Takai. 1998. Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae. J. Biol. Chem. 273:28341-28345.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28341-28345
    • Kamei, T.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Imamura, H.5    Kikyo, M.6    Ozaki, K.7    Takai, Y.8
  • 27
    • 15644368249 scopus 로고    scopus 로고
    • Covalent modification of PML by the sentrin family of ubiquitin-like proteins
    • Kamitani, T., H.P. Nguyen, K. Kito, T. Fukuda-Kamitani, and E.T. Yeh. 1998b. Covalent modification of PML by the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273:3117-3120.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3117-3120
    • Kamitani, T.1    Nguyen, H.P.2    Kito, K.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 28
    • 0026019902 scopus 로고
    • Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: Localization of the CDC3 gene product and the timing of events at the budding site
    • Kim, H.B., B.K. Haarer, and J.R. Pringle. 1991. Cellular morphogenesis in the Saccharomyces cerevisiae cell cycle: localization of the CDC3 gene product and the timing of events at the budding site. J. Cell Biol. 112:535-544.
    • (1991) J. Cell Biol. , vol.112 , pp. 535-544
    • Kim, H.B.1    Haarer, B.K.2    Pringle, J.R.3
  • 29
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li, S.J., and M. Hochstrasser. 1999. A new protease required for cell-cycle progression in yeast. Nature. 398:246-251.
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 30
    • 0032576546 scopus 로고    scopus 로고
    • Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating actomyosin ring dynamics and septin distribution
    • Lippincott, J., and R. Li. 1998a. Dual function of Cyk2, a cdc15/PSTPIP family protein, in regulating actomyosin ring dynamics and septin distribution. J. Cell Biol. 143:1947-1960.
    • (1998) J. Cell Biol. , vol.143 , pp. 1947-1960
    • Lippincott, J.1    Li, R.2
  • 31
    • 0032567760 scopus 로고    scopus 로고
    • Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis
    • Lippincott, J., and R. Li. 1998b. Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J. Cell Biol. 140:355-366.
    • (1998) J. Cell Biol. , vol.140 , pp. 355-366
    • Lippincott, J.1    Li, R.2
  • 33
    • 0032476712 scopus 로고    scopus 로고
    • Role of the yeast Gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function
    • Longtine, M.S., H. Fares, and J.R. Pringle. 1998. Role of the yeast Gin4p protein kinase in septin assembly and the relationship between septin assembly and septin function. J. Cell Biol. 143:719-736.
    • (1998) J. Cell Biol. , vol.143 , pp. 719-736
    • Longtine, M.S.1    Fares, H.2    Pringle, J.R.3
  • 34
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan, R., C. Delphin, T. Guan, L. Gerace, and F. Melchior. 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
  • 35
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • Mahajan, R., L. Gerace, and F. Melchior. 1998. Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association. J. Cell Biol. 140:259-270.
    • (1998) J. Cell Biol. , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 36
    • 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., E. Coutavas, and G. Blobel. 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
  • 37
    • 0032498541 scopus 로고    scopus 로고
    • SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex
    • Matunis, M.J., J. Wu, and G. Blobel. 1998. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol. 140:499-509.
    • (1998) J. Cell Biol. , vol.140 , pp. 499-509
    • Matunis, M.J.1    Wu, J.2    Blobel, G.3
  • 38
    • 0029044625 scopus 로고
    • Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C
    • Meluh, P.B., and D. Koshland. 1995. Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C. Mol. Biol. Cell. 6:793-807.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 793-807
    • Meluh, P.B.1    Koshland, D.2
  • 39
    • 0032578776 scopus 로고    scopus 로고
    • Shs1p: A novel member of septin that interacts with spa2p. involved in polarized growth in Saccharomyces cerevisiae
    • Mino, A., K. Tanaka, T. Kamei, M. Umikawa, T. Fujiwara, and Y. Takai. 1998. Shs1p: a novel member of septin that interacts with spa2p. involved in polarized growth in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 251:732-736.
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 732-736
    • Mino, A.1    Tanaka, K.2    Kamei, T.3    Umikawa, M.4    Fujiwara, T.5    Takai, Y.6
  • 40
    • 0037498052 scopus 로고    scopus 로고
    • Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus
    • Müller, S., M.J. Matunis, and A. Dejean. 1998. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO (Eur. Mol. Biol. Org.) J. 17:61-70.
    • (1998) EMBO (Eur. Mol. Biol. Org.) J. , vol.17 , pp. 61-70
    • Müller, S.1    Matunis, M.J.2    Dejean, A.3
  • 42
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- And tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • Okura, T., L. Gong, T. Kamitani, T. Wada, I. Okura, C.F. Wei, H.M. Chang, and E.T. Yeh. 1996. Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J. Immunol. 157:4277-4281.
    • (1996) J. Immunol. , vol.157 , pp. 4277-4281
    • Okura, T.1    Gong, L.2    Kamitani, T.3    Wada, T.4    Okura, I.5    Wei, C.F.6    Chang, H.M.7    Yeh, E.T.8
  • 43
    • 0026092903 scopus 로고
    • Staining of bud scars and other cell wall chitin with calcofluor
    • C. Guthrie and G.R. Fink, editors. Academic Press,San Diego, CA
    • Pringle, J.R. 1991. Staining of bud scars and other cell wall chitin with calcofluor. In Guide to Yeast Genetics and Molecular Biology. Vol. 194. C. Guthrie and G.R. Fink, editors. Academic Press,San Diego, CA. 732-735.
    • (1991) Guide to Yeast Genetics and Molecular Biology , vol.194 , pp. 732-735
    • Pringle, J.R.1
  • 44
    • 0026087181 scopus 로고
    • Immunofluorescence methods for yeast
    • C. Guthrie and G.R. Fink, editors. Academic Press, San Diego, CA
    • Pringle, J.R., A.E.M. Adams, D.G. Drubin, and B.K. Haarer. 1991. Immunofluorescence methods for yeast. In Guide to Yeast Genetics and Molecular Biology. Vol. 194. C. Guthrie and G.R. Fink, editors. Academic Press, San Diego, CA. 565-602.
    • (1991) Guide to Yeast Genetics and Molecular Biology , vol.194 , pp. 565-602
    • Pringle, J.R.1    Adams, A.E.M.2    Drubin, D.G.3    Haarer, B.K.4
  • 45
    • 0032538933 scopus 로고    scopus 로고
    • Nuclear import and the evolution of a multifunctional RNA-binding protein
    • Rosenblum, J.S., L.F. Pemberton, N. Bonifaci, and G. Blobel. 1998. Nuclear import and the evolution of a multifunctional RNA-binding protein. J. Cell Biol. 143:887-899.
    • (1998) J. Cell Biol. , vol.143 , pp. 887-899
    • Rosenblum, J.S.1    Pemberton, L.F.2    Bonifaci, N.3    Blobel, G.4
  • 47
    • 0029999229 scopus 로고    scopus 로고
    • The BUD4 protein of yeast, required for axial budding, is localized to the mother/BUD neck in a cell cycle-dependent manner
    • Sanders, S.L., and I. Herskowitz. 1996. The BUD4 protein of yeast, required for axial budding, is localized to the mother/BUD neck in a cell cycle-dependent manner. J. Cell Biol. 134:413-127.
    • (1996) J. Cell Biol. , vol.134 , pp. 413-1127
    • Sanders, S.L.1    Herskowitz, I.2
  • 49
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert, W., B. Futcher, and S. Jentsch. 1995. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature. 373:78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 50
    • 0030588127 scopus 로고    scopus 로고
    • Associations of UBE21 with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system
    • Shen, Z., P.E. Pardington-Purtymun, J.C. Comeaux, R.K. Moyzis, and D.J. Chen. 1996. Associations of UBE21 with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system. Genomics. 37:183-186.
    • (1996) Genomics , vol.37 , pp. 183-186
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 52
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 53
    • 0033617169 scopus 로고    scopus 로고
    • The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers
    • Sternsdorf, T., K. Jensen, B. Reich, and H. Will. 1999. The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers. J. Biol Chem. 274:12555-12566.
    • (1999) J. Biol Chem. , vol.274 , pp. 12555-12566
    • Sternsdorf, T.1    Jensen, K.2    Reich, B.3    Will, H.4
  • 54
    • 0031426631 scopus 로고    scopus 로고
    • Evidence for covalent modification of the nuclear dot-associated proteins PML and sp100 by PIC1/SUMO-1
    • Sternsdorf, T., K. Jensen, and H. Will. 1997. Evidence for covalent modification of the nuclear dot-associated proteins PML and sp100 by PIC1/SUMO-1. J. Cell Biol. 139:1621-1634.
    • (1997) J. Cell Biol. , vol.139 , pp. 1621-1634
    • Sternsdorf, T.1    Jensen, K.2    Will, H.3
  • 55
    • 0033574967 scopus 로고    scopus 로고
    • Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast
    • Takahashi, Y., M. Iwase, M. Konishi, M. Tanaka, A. Toh-e, and Y. Kikuchi. 1999. Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast. Biochem. Biophys. Res. Commun. 259:582-587.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 582-587
    • Takahashi, Y.1    Iwase, M.2    Konishi, M.3    Tanaka, M.4    Toh-e, A.5    Kikuchi, Y.6
  • 56
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • Yaffe, M.P., and G. Schatz. 1984. Two nuclear mutations that block mitochondrial protein import in yeast. Proc. Natl. Acad. Sci. USA. 81:4819-4823.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2


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