메뉴 건너뛰기




Volumn 22, Issue 3, 2005, Pages 219-239

Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae

Author keywords

Cct; Chaperonins; LST8; RSP5; SAP155; SIT4; TOR2

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; PROTEIN SUBUNIT;

EID: 20044382419     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/yea.1210     Document Type: Article
Times cited : (35)

References (79)
  • 2
    • 0033588918 scopus 로고    scopus 로고
    • Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast
    • Beck T, Schmidt A, Hall MN. 1999. Starvation induces vacuolar targeting and degradation of the tryptophan permease in yeast. J Cell Biol 146: 1227-1238.
    • (1999) J. Cell. Biol. , vol.146 , pp. 1227-1238
    • Beck, T.1    Schmidt, A.2    Hall, M.N.3
  • 3
    • 0032516080 scopus 로고    scopus 로고
    • The TOR (target of rapamycin) signal transduction pathway regulates the stability of translation initiation factor eIF4G in the yeast Saccharomyces cerevisiae
    • Berset C, Trachsel H, Altman M. 1998. The TOR (target of rapamycin) signal transduction pathway regulates the stability of translation initiation factor eIF4G in the yeast Saccharomyces cerevisiae. Proc Natl Acad Sci USA 95: 4264-4269.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4264-4269
    • Berset, C.1    Trachsel, H.2    Altman, M.3
  • 4
    • 0037732600 scopus 로고    scopus 로고
    • LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway
    • Chen EJ, Kaiser CA. 2003. LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway. J Cell Biol 161: 333-347.
    • (2003) J. Cell. Biol. , vol.161 , pp. 333-347
    • Chen, E.J.1    Kaiser, C.A.2
  • 5
    • 0015385368 scopus 로고
    • Nonchromosomal antibiotic resistance in bacteria: Genetic transformation of Escherichia coli by R-factor DNA
    • Cohen SN, Chang ACY, Hsu L. 1972. Nonchromosomal antibiotic resistance in bacteria: genetic transformation of Escherichia coli by R-factor DNA. Proc Natl Acad Sci USA 69: 2110-2114.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2110-2114
    • Cohen, S.N.1    Chang, A.C.Y.2    Hsu, L.3
  • 6
    • 4444249882 scopus 로고    scopus 로고
    • NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae
    • Crespo JL, Helliwell SB, Wiederkehr C, et al. 2004. NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent transcription in Saccharomyces cerevisiae. J Biol Chem 279: 37 512-37 517.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37512-37517
    • Crespo, J.L.1    Helliwell, S.B.2    Wiederkehr, C.3
  • 7
    • 0032009398 scopus 로고    scopus 로고
    • Rapid protein identification using a microscale electrospray LC/MS system on an ion trap mass spectrometer
    • Davis MT, Lee TD. 1998. Rapid protein identification using a microscale electrospray LC/MS system on an ion trap mass spectrometer. J Am Soc Mass Spectrom 9: 194-201.
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 194-201
    • Davis, M.T.1    Lee, T.D.2
  • 9
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, archaea; chaperonin and homolog of CCT
    • Ditzel L, Löwe J, Stock D, et al. 1998. Crystal structure of the thermosome, archaea; chaperonin and homolog of CCT. Cell 93: 125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Löwe, J.2    Stock, D.3
  • 10
    • 0141455113 scopus 로고    scopus 로고
    • Suppression of a defect in mitochondrial protein import identifies cytosolic proteins required for viability of yeast cells lacking mitochondrial DNA
    • Dunn CD, Jensen RE. 2003. Suppression of a defect in mitochondrial protein import identifies cytosolic proteins required for viability of yeast cells lacking mitochondrial DNA. Genetics 165 35-45.
    • (2003) Genetics , vol.165 , pp. 35-45
    • Dunn, C.D.1    Jensen, R.E.2
  • 11
    • 17344381954 scopus 로고    scopus 로고
    • Multiple roles of Tap42 in mediating rapamycin-induced transcriptional changes in yeast
    • Düvel K, Santhanam A, Garrett S, Schneper L, Broach JR. 2003. Multiple roles of Tap42 in mediating rapamycin-induced transcriptional changes in yeast. Mol Cell 11: 1467-1478.
    • (2003) Mol. Cell. , vol.11 , pp. 1467-1478
    • Düvel, K.1    Santhanam, A.2    Garrett, S.3    Schneper, L.4    Broach, J.R.5
  • 12
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass-spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR III. 1994. An approach to correlate tandem mass-spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5: 976-989.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 13
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt KL, Hendrick JP, Houry WA, Hartl F-U. 1997. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90: 491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.-U.4
  • 14
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    • Feldman DE, Thulasiraman V, Ferreyra RG, Frydman J. 1999. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol Cell 4: 1051-1061.
    • (1999) Mol. Cell. , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 15
    • 0035155749 scopus 로고    scopus 로고
    • WW domains of Rsp5p define different functions: Determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae
    • Gajewska B, Kamińska J, Jesionowska A, et al. 2001. WW domains of Rsp5p define different functions: determination of roles in fluid phase and uracil permease endocytosis in Saccharomyces cerevisiae. Genetics 157: 91-101.
    • (2001) Genetics , vol.157 , pp. 91-101
    • Gajewska, B.1    Kamińska, J.2    Jesionowska, A.3
  • 16
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC, Bosche M, Krause R, et al. 2002. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1    Bosche, M.2    Krause, R.3
  • 17
    • 0035173012 scopus 로고    scopus 로고
    • Nucleocytoplasmic distribution of budding yeast protein kinase A regulatory subunit Bcy1 requires Zds1 and is regulated by Yak1-dependent phosphorylation of its targeting domain
    • Griffioen G, Branduardi P, Ballarini A, et al. 2001. Nucleocytoplasmic distribution of budding yeast protein kinase A regulatory subunit Bcy1 requires Zds1 and is regulated by Yak1-dependent phosphorylation of its targeting domain. Mol Cell Biol 21: 511-523.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 511-523
    • Griffioen, G.1    Branduardi, P.2    Ballarini, A.3
  • 18
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TRiC(k)s and turns of a folding machine
    • Gutsche I, Essen L-O, Baumeister W. 1999. Group II chaperonins: New TRiC(k)s and turns of a folding machine. J Mol Biol 293: 295-312.
    • (1999) J. Mol. Biol. , vol.293 , pp. 295-312
    • Gutsche, I.1    Essen, L.-O.2    Baumeister, W.3
  • 19
    • 0030045693 scopus 로고    scopus 로고
    • The TOR signalling pathway and growth control in yeast
    • Hall MN. 1996. The TOR signalling pathway and growth control in yeast. Biochem Soc Trans 24: 234-239.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 234-239
    • Hall, M.N.1
  • 20
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding: Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl F-U, Hayer-Hartl M. 2002. Protein folding: molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.-U.1    Hayer-Hartl, M.2
  • 21
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein C, Springael J-Y, Volland C, Haguenauer-Tsapis R, André B. 1995. NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol Microbiol 18: 77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.-Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 22
    • 0028137771 scopus 로고
    • TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast
    • Helliwell SB, Wagner P, Kunz J, et al. 1994. TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast. Mol Biol Cell 5 105-118.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 105-118
    • Helliwell, S.B.1    Wagner, P.2    Kunz, J.3
  • 23
    • 0032488042 scopus 로고    scopus 로고
    • The Rho1 effector Pkc1, but not Bni1, mediates signalling from Tor2 to the actin cytoskeleton
    • Helliwell SB, Schmidt A, Ohya Y, Hall MN. 1998. The Rho1 effector Pkc1, but not Bni1, mediates signalling from Tor2 to the actin cytoskeleton. Curr Biol 8: 1211-1214.
    • (1998) Curr. Biol. , vol.8 , pp. 1211-1214
    • Helliwell, S.B.1    Schmidt, A.2    Ohya, Y.3    Hall, M.N.4
  • 24
    • 0035858866 scopus 로고    scopus 로고
    • Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease
    • Helliwell SB, Losko S, Kaiser CA. 2001. Components of a ubiquitin ligase complex specify polyubiquitination and intracellular trafficking of the general amino acid permease. J Cell Biol 153 649-662.
    • (2001) J. Cell. Biol. , vol.153 , pp. 649-662
    • Helliwell, S.B.1    Losko, S.2    Kaiser, C.A.3
  • 25
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vectors with multiple unique restriction sites
    • Hill JE, Myers AM, Koerner TJ, Tzagoloff A. 1986. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast 2: 163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagoloff, A.4
  • 26
    • 0037050004 scopus 로고    scopus 로고
    • Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
    • Ho Y, Gruhler A, Heilbut A, et al. 2002. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415: 180-183.
    • (2002) Nature , vol.415 , pp. 180-183
    • Ho, Y.1    Gruhler, A.2    Heilbut, A.3
  • 27
    • 0029036701 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse JM, Scheffner M, Beaudenon S, Howley PM. 1995. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 92: 2563-2567.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2563-2567
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 28
    • 0034705567 scopus 로고    scopus 로고
    • Individual subunits of the eukarotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of β -actin
    • Hynes G, Willison KR. 2000. Individual subunits of the eukarotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of β-actin. J Biol Chem 275: 18 985-18 994.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18985-18994
    • Hynes, G.1    Willison, K.R.2
  • 30
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H, Fukuda Y, Murata K, Kimura A. 1983. Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 31
    • 0035930339 scopus 로고    scopus 로고
    • TIP41 interacts with TAP42 and negatively regulates the TOR signalling pathway
    • Jacinto E, Guo B, Arndt KT, Schmelzle T, Hall MN. 2001. TIP41 interacts with TAP42 and negatively regulates the TOR signalling pathway. Mol Cell 8: 1017-1026.
    • (2001) Mol. Cell. , vol.8 , pp. 1017-1026
    • Jacinto, E.1    Guo, B.2    Arndt, K.T.3    Schmelzle, T.4    Hall, M.N.5
  • 32
    • 0033577745 scopus 로고    scopus 로고
    • Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast
    • Jiang Y, Broach JR. 1999. Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast. EMBO J 18: 2782-2792.
    • (1999) EMBO J. , vol.18 , pp. 2782-2792
    • Jiang, Y.1    Broach, J.R.2
  • 33
    • 0036786951 scopus 로고    scopus 로고
    • Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae
    • Kamińska J, Gajewska B, Hopper AK, Zoładek T. 2003. Rsp5p, a new link between the actin cytoskeleton and endocytosis in the yeast Saccharomyces cerevisiae. Mol Cell Biol 22: 6946-6958.
    • (2003) Mol. Cell. Biol. , vol.22 , pp. 6946-6958
    • Kamińska, J.1    Gajewska, B.2    Hopper, A.K.3    Zoładek, T.4
  • 34
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotype selection
    • Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotype selection. Methods Enzymol 154: 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 36
    • 0026683609 scopus 로고
    • T-complex polypeptide is a subunit of a heteromeric particle in the eukaryotic cytosol
    • Lewis VA, Hynes G, Zheng D, Saibil H, Willison KR. 1992. T-complex polypeptide is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature 358: 249-252.
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.2    Zheng, D.3    Saibil, H.4    Willison, K.R.5
  • 37
    • 0030930753 scopus 로고    scopus 로고
    • The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex
    • Lin P, Sherman F. 1997. The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex. Proc Natl Acad Sci USA 94: 10 780-10 785.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10780-10785
    • Lin, P.1    Sherman, F.2
  • 38
    • 0030734629 scopus 로고    scopus 로고
    • Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae
    • Lin P, Cardillo TS, Richard LM, Segel GB, Sherman F. 1997. Analysis of mutationally altered forms of the Cct6 subunit of the chaperonin from Saccharomyces cerevisiae. Genetics 147: 1609-1633.
    • (1997) Genetics , vol.147 , pp. 1609-1633
    • Lin, P.1    Cardillo, T.S.2    Richard, L.M.3    Segel, G.B.4    Sherman, F.5
  • 39
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from subunit composition of CCT microcomplexes
    • Liou AKF, Willison KR. 1997. Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from subunit composition of CCT microcomplexes. EMBO J 16: 4311-4316.
    • (1997) EMBO J. , vol.16 , pp. 4311-4316
    • Liou, A.K.F.1    Willison, K.R.2
  • 40
    • 0031924139 scopus 로고    scopus 로고
    • The chaperonin containing TCP-1 (CCT) displays a single-ring mediated dissembly and reassembly cycle
    • Liou AKF, McCormack EA, Willison KR. 1998. The chaperonin containing TCP-1 (CCT) displays a single-ring mediated dissembly and reassembly cycle. Biol Chem Hoppe-Seyler 379: 311-319.
    • (1998) Biol. Chem. Hoppe-Seyler , vol.379 , pp. 311-319
    • Liou, A.K.F.1    McCormack, E.A.2    Willison, K.R.3
  • 41
    • 0032985364 scopus 로고    scopus 로고
    • 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin
    • Llorca O, Smyth MG, Carrascosa JL, et al. 1999. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Nature Struct Biol 6: 639-642.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 639-642
    • Llorca, O.1    Smyth, M.G.2    Carrascosa, J.L.3
  • 42
    • 0036753494 scopus 로고    scopus 로고
    • Two TOR complexes, only one of which is rapamycin-sensitive, have distinct roles in cell growth control
    • Loewith R, Jacinto E, Wullschleger S, et al. 2002. Two TOR complexes, only one of which is rapamycin-sensitive, have distinct roles in cell growth control. Mol Cell 10: 457-468.
    • (2002) Mol. Cell. , vol.10 , pp. 457-468
    • Loewith, R.1    Jacinto, E.2    Wullschleger, S.3
  • 43
    • 0029664530 scopus 로고    scopus 로고
    • The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase
    • Luke MM, Della Seta F, Di Como CJ, et al. 1996. The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase. Mol Cell Biol 16: 2744-2755.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2744-2755
    • Luke, M.M.1    Della Seta, F.2    Di Como, C.J.3
  • 45
    • 0034604290 scopus 로고    scopus 로고
    • Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease
    • Marchal C, Haguenauer-Tsapis R, Urban-Grimal D. 2000. Casein kinase I-dependent phosphorylation within a PEST sequence and ubiquitination at nearby lysines signal endocytosis of yeast uracil permease. J Biol Chem 275: 23 608-23 614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23608-23614
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 46
    • 0343907201 scopus 로고    scopus 로고
    • Cytoplasmic chaperonin containing TCP-1: Structural and functional characterization
    • Melki R, Batelier G, Soulie S, Williams RC Jr. 1997. Cytoplasmic chaperonin containing TCP-1: structural and functional characterization. Biochemistry 36: 5817-5826.
    • (1997) Biochemistry , vol.36 , pp. 5817-5826
    • Melki, R.1    Batelier, G.2    Soulie, S.3    Williams Jr., R.C.4
  • 47
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • Meyer AS, Gillespie JR, Walther D, et al. 2003. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113: 369-381.
    • (2003) Cell , vol.113 , pp. 369-381
    • Meyer, A.S.1    Gillespie, J.R.2    Walther, D.3
  • 48
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. 1975. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 49
    • 0031793782 scopus 로고    scopus 로고
    • A Candida albicans chaperonin subunits (CaCct8p) as a specific suppressors of morphogenesis and RAS phenotypes C. albicans and Saccharomyces cerevisiae
    • Rademacher F, Kehren V, Stoldt VR, Ernst JF. 1998. A Candida albicans chaperonin subunits (CaCct8p) as a specific suppressors of morphogenesis and RAS phenotypes C. albicans and Saccharomyces cerevisiae. Microbiol 144: 2951-2960.
    • (1998) Microbiol. , vol.144 , pp. 2951-2960
    • Rademacher, F.1    Kehren, V.2    Stoldt, V.R.3    Ernst, J.F.4
  • 51
    • 0035971180 scopus 로고    scopus 로고
    • The TOR kinases link nutrient sensing to cell growth
    • Rohde J, Heitman J, Cardenas ME. 2001. The TOR kinases link nutrient sensing to cell growth. J Biol Chem 276: 9583-9586.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9583-9586
    • Rohde, J.1    Heitman, J.2    Cardenas, M.E.3
  • 52
    • 0030809956 scopus 로고    scopus 로고
    • Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8
    • Roberg KJ, Bickel S, Rowley N, Kaiser CA. 1997. Control of amino acid permease sorting in the late secretory pathway of Saccharomyces cerevisiae by SEC13, LST4, LST7 and LST8. Genetics 147: 1569-1584.
    • (1997) Genetics , vol.147 , pp. 1569-1584
    • Roberg, K.J.1    Bickel, S.2    Rowley, N.3    Kaiser, C.A.4
  • 53
    • 0033574162 scopus 로고    scopus 로고
    • The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins
    • Rommelaere H, De Neve M, Melki R, Vandekerckhove J, Ampe C. 1999. The cytosolic class II chaperonin CCT recognizes delineated hydrophobic sequences in its target proteins. Biochemistry 38 3246-3257.
    • (1999) Biochemistry , vol.38 , pp. 3246-3257
    • Rommelaere, H.1    De Neve, M.2    Melki, R.3    Vandekerckhove, J.4    Ampe, C.5
  • 54
    • 0033593346 scopus 로고    scopus 로고
    • Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro
    • Roobol A, Sahyoun ZP, Carden MJ. 1999a. Selected subunits of the cytosolic chaperonin associate with microtubules assembled in vitro. J Biol Chem 274: 2408-2415.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2408-2415
    • Roobol, A.1    Sahyoun, Z.P.2    Carden, M.J.3
  • 56
    • 0032587044 scopus 로고    scopus 로고
    • Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle
    • Roobol A, Carden MJ. 1999. Subunits of the eukaryotic cytosolic chaperonin CCT do not always behave as components of a uniform hetero-oligomeric particle. Eur J Cell Biol 78: 21-32.
    • (1999) Eur. J. Cell. Biol. , vol.78 , pp. 21-32
    • Roobol, A.1    Carden, M.J.2
  • 57
    • 0034235434 scopus 로고    scopus 로고
    • Ubiquitination and endocytosis of plasma membrane proteins; role of Nedd4/Rsp5p family of ubiquitin-protein ligases
    • Rotin D, Staub O, Haguenauer-Tsapis R. 2000. Ubiquitination and endocytosis of plasma membrane proteins; role of Nedd4/Rsp5p family of ubiquitin-protein ligases. J Membr Biol 176: 1-17.
    • (2000) J Membr. Biol. , vol.176 , pp. 1-17
    • Rotin, D.1    Staub, O.2    Haguenauer-Tsapis, R.3
  • 58
    • 0023850178 scopus 로고
    • Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase
    • Saiki RK, Gelfand DE, Stoffel S, et al. 1988. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science 239: 487-491.
    • (1988) Science , vol.239 , pp. 487-491
    • Saiki, R.K.1    Gelfand, D.E.2    Stoffel, S.3
  • 59
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle T, Hall MN. 2000. TOR, a central controller of cell growth. Cell 103: 253-262.
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 61
    • 0030479340 scopus 로고    scopus 로고
    • Tor2 is required for organization of the actin cytoskeleton in yeast
    • Schmidt A, Kunz J, Hall MN. 1996. Tor2 is required for organization of the actin cytoskeleton in yeast. Proc Natl Acad Sci USA 93: 13 780-13 785.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13780-13785
    • Schmidt, A.1    Kunz, J.2    Hall, M.N.3
  • 62
    • 0030906569 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2
    • Schmidt A, Bickle M, Beck T, Hall MN. 1997. The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2. Cell 88: 531-42.
    • (1997) Cell , vol.88 , pp. 531-542
    • Schmidt, A.1    Bickle, M.2    Beck, T.3    Hall, M.N.4
  • 63
    • 0032403058 scopus 로고    scopus 로고
    • The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease
    • Schmidt A, Beck T, Koller A, Kunz J, Hall MN. 1998. The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits turnover of the tryptophan permease. EMBO J 17: 6924-6931.
    • (1998) EMBO J. , vol.17 , pp. 6924-6931
    • Schmidt, A.1    Beck, T.2    Koller, A.3    Kunz, J.4    Hall, M.N.5
  • 65
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens O, de Craene JO, Andre B. 2001. Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J Biol Chem 276: 43 949-43 957.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1    de Craene, J.O.2    Andre, B.3
  • 66
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
    • Spiess C, Meyer AS, Frydman J. 2004. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol 14: 598-604.
    • (2004) Trends Cell. Biol. , vol.14 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Frydman, J.3
  • 67
    • 0031867271 scopus 로고    scopus 로고
    • Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae
    • Springael JY, Andre B. 1998. Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol Biol Cell 9: 1253-1263.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1253-1263
    • Springael, J.Y.1    Andre, B.2
  • 68
    • 0027195259 scopus 로고
    • A general suppressor of RNA polymerase I, II and II mutations in Saccharomyces cerevisiae
    • Stettler S, Chiannilkulchai N, Hermann-Le Denmat S, et al. 1993. A general suppressor of RNA polymerase I, II and II mutations in Saccharomyces cerevisiae. Mol Gen Genet 239: 169-176.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 169-176
    • Stettler, S.1    Chiannilkulchai, N.2    Hermann-Le Denmat, S.3
  • 69
    • 0029884589 scopus 로고    scopus 로고
    • The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts
    • Stoldt V, Rademacher F, Kehren V, et al. 1996. The Cct eukaryotic chaperonin subunits of Saccharomyces cerevisiae and other yeasts. Yeast 12: 523-529.
    • (1996) Yeast , vol.12 , pp. 523-529
    • Stoldt, V.1    Rademacher, F.2    Kehren, V.3
  • 71
    • 0026345831 scopus 로고
    • The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
    • Ursic D, Culbertson MR. 1991. The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11 2629-2640.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2629-2640
    • Ursic, D.1    Culbertson, M.R.2
  • 72
    • 0023217215 scopus 로고
    • Isolation of the NPR1 gene responsible for the reactivation of ammonia-sensitive amino acid permeases in Saccharomyces cerevisiae. RNA analysis and gene dosage effects
    • Vandenbol M, Jauniaux JC, Vissers S, Grenson M. 1987. Isolation of the NPR1 gene responsible for the reactivation of ammonia-sensitive amino acid permeases in Saccharomyces cerevisiae. RNA analysis and gene dosage effects. Eur J Biochem 164: 607-612.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 607-612
    • Vandenbol, M.1    Jauniaux, J.C.2    Vissers, S.3    Grenson, M.4
  • 73
    • 0037345059 scopus 로고    scopus 로고
    • Tor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae
    • Wedaman KP, Reinke A, Anderson S, et al. 2003. Tor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae. Mol Biol Cell 14: 1204-1220.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 1204-1220
    • Wedaman, K.P.1    Reinke, A.2    Anderson, S.3
  • 74
    • 0038538410 scopus 로고    scopus 로고
    • Yap1 accumulates in the nucleus in response to carbon stress in Saccharomyces cerevisiae
    • Wiatrowski HA, Carlson M. 2003. Yap1 accumulates in the nucleus in response to carbon stress in Saccharomyces cerevisiae. Eukaryot Cell 2: 19-26.
    • (2003) Eukaryot. Cell , vol.2 , pp. 19-26
    • Wiatrowski, H.A.1    Carlson, M.2
  • 75
    • 0036707664 scopus 로고    scopus 로고
    • The role of plant CCTα in salt- and osmotic-stress tolerance
    • Yamada A, Sekiguchi M, Mimura T, Ozeki Y. 2002. The role of plant CCTα in salt- and osmotic-stress tolerance. Plant Cell Physiol 43: 1043-1048.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1043-1048
    • Yamada, A.1    Sekiguchi, M.2    Mimura, T.3    Ozeki, Y.4
  • 76
    • 0031592944 scopus 로고    scopus 로고
    • Structural and functional characterization of homo-oligomeric complexes of α- and β-chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1
    • Yoshida T, Yohda M, Iida T, et al. 1997. Structural and functional characterization of homo-oligomeric complexes of α- and β-chaperonin subunits from the hyperthermophilic archaeum Thermococcus strain KS-1. J Mol Biol 273: 635-645.
    • (1997) J. Mol. Biol. , vol.273 , pp. 635-645
    • Yoshida, T.1    Yohda, M.2    Iida, T.3
  • 77
    • 0029071264 scopus 로고
    • TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin
    • Zheng XF, Florentino D, Chen J, Crabtree GR, Schreiber SL. 1995. TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin. Cell 82: 121-130.
    • (1995) Cell , vol.82 , pp. 121-130
    • Zheng, X.F.1    Florentino, D.2    Chen, J.3    Crabtree, G.R.4    Schreiber, S.L.5
  • 78
    • 0028791882 scopus 로고
    • Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery
    • Zoładek T, Vaduva G, Hunter LA, et al. 1995. Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p implicate the actin cytoskeleton and mRNA 3′ ends and/or protein synthesis in mitochondrial delivery. Mol Cell Biol 15: 6884-6894.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6884-6894
    • Zoładek, T.1    Vaduva, G.2    Hunter, L.A.3
  • 79
    • 1842374437 scopus 로고    scopus 로고
    • MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5
    • Zoładek T, Tobiasz A, Vaduva G, et al. 1997. MDP1, a Saccharomyces cerevisiae gene involved in mitochondrial/cytoplasmic protein distribution, is identical to the ubiquitin-protein ligase gene RSP5. Genetics 145: 595-603.
    • (1997) Genetics , vol.145 , pp. 595-603
    • Zoładek, T.1    Tobiasz, A.2    Vaduva, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.