메뉴 건너뛰기




Volumn 165, Issue 2, 2003, Pages 531-541

A Novel Step in β-Tubulin Folding Is Important for Heterodimer Formation in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; CELL PROTEIN; CHAPERONIN; DIMER; GALACTOSE; PHOSDUCIN; PROTEIN PLP1P; UNCLASSIFIED DRUG;

EID: 0242286609     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (38)
  • 1
    • 0036132659 scopus 로고    scopus 로고
    • Protection from free β-tubulin by the β-tubulin binding protein Rbl2p
    • ABRUZZI, K. C., A. SMITH, W. CHEN and F. SOLOMON, 2002 Protection from free β-tubulin by the β-tubulin binding protein Rbl2p. Mol. Cell. Biol. 22: 138-147.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 138-147
    • Abruzzi, K.C.1    Smith, A.2    Chen, W.3    Solomon, F.4
  • 2
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • ALANI, E., L. CAO and N. KLECKNER, 1987 A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116: 541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 3
    • 0031776859 scopus 로고    scopus 로고
    • Modulation of tubulin polypeptide ratios by the yeast protein Pac10p
    • ALVAREZ, P., A. SMITH, J. FLEMING and F. SOLOMON, 1998 Modulation of tubulin polypeptide ratios by the yeast protein Pac10p. Genetics 149: 857-864.
    • (1998) Genetics , vol.149 , pp. 857-864
    • Alvarez, P.1    Smith, A.2    Fleming, J.3    Solomon, F.4
  • 4
    • 0029164636 scopus 로고
    • Rbl2p, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo
    • ARCHER, J. E., L. R. VEGA and F. SOLOMON, 1995 Rbl2p, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo. Cell 82: 425-434.
    • (1995) Cell , vol.82 , pp. 425-434
    • Archer, J.E.1    Vega, L.R.2    Solomon, F.3
  • 5
    • 0028986667 scopus 로고
    • 1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast
    • 1 cyclin turnover and nutrient uptake are controlled by a common pathway in yeast. Genes Dev. 9: 399-409.
    • (1995) Genes Dev. , vol.9 , pp. 399-409
    • Barral, Y.1    Jentsch, S.2    Mann, C.3
  • 6
    • 0022517408 scopus 로고
    • A chicken-yeast chimeric β-tubulin protein is incorporated into mouse microtubules in vivo
    • BOND, J. F., J. L. FRIDOVICH-KEIL, L. PILLUS, R. C. MULLIGAN and F. SOLOMON, 1986 A chicken-yeast chimeric β-tubulin protein is incorporated into mouse microtubules in vivo. Cell 44: 461-468.
    • (1986) Cell , vol.44 , pp. 461-468
    • Bond, J.F.1    Fridovich-Keil, J.L.2    Pillus, L.3    Mulligan, R.C.4    Solomon, F.5
  • 7
    • 0024582786 scopus 로고
    • Dominant effects of tubulin overexpression in Saccharomyces cerevisiae
    • BURKE, D., P. GASDASKA and L. HARTWELL, 1989 Dominant effects of tubulin overexpression in Saccharomyces cerevisiae. Mol. Cell. Biol. 9: 1049-1059.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1049-1059
    • Burke, D.1    Gasdaska, P.2    Hartwell, L.3
  • 8
    • 0028215472 scopus 로고
    • Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae
    • BURNS, N., B. GRIMWADE, P. B. ROSS-MACDONALD, E. Y. CHOI, K. FINBERG et al., 1994 Large-scale analysis of gene expression, protein localization, and gene disruption in Saccharomyces cerevisiae. Genes Dev. 8: 1087-1105.
    • (1994) Genes Dev. , vol.8 , pp. 1087-1105
    • Burns, N.1    Grimwade, B.2    Ross-Macdonald, P.B.3    Choi, E.Y.4    Finberg, K.5
  • 10
    • 0035783192 scopus 로고    scopus 로고
    • Review: Cellular substrates of the eukaryotic chaperonin TriC/CCT
    • DUNN, A. Y., M. W. MELVILLE and J. FRYDMAN, 2001 Review: cellular substrates of the eukaryotic chaperonin TriC/CCT. J. Struct. Biol. 135: 176-184.
    • (2001) J. Struct. Biol. , vol.135 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 11
    • 0028872562 scopus 로고
    • FtsZ, a prokaryotic homolog of tubulin?
    • ERICKSON, H. P., 1995 FtsZ, a prokaryotic homolog of tubulin? Cell 80: 367-370.
    • (1995) Cell , vol.80 , pp. 367-370
    • Erickson, H.P.1
  • 12
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and normative forms
    • FARR, G. W., E. C. SCHARL, R. J. SCHUMACHER, S. SONDEK and A. L. HORWICH, 1997 Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and normative forms. Cell 89: 927-937.
    • (1997) Cell , vol.89 , pp. 927-937
    • Farr, G.W.1    Scharl, E.C.2    Schumacher, R.J.3    Sondek, S.4    Horwich, A.L.5
  • 13
    • 0034674599 scopus 로고    scopus 로고
    • Functional analysis of Plp1 and Plp2, two homologues of phosducin in yeast
    • FLANARY, P. L., P. R. DIBELLO, P. ESTRADA and H. G. DOHLMAN, 2000 Functional analysis of Plp1 and Plp2, two homologues of phosducin in yeast. J. Biol. Chem. 275: 18462-18469.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18462-18469
    • Flanary, P.L.1    Dibello, P.R.2    Estrada, P.3    Dohlman, H.G.4
  • 14
    • 0033824364 scopus 로고    scopus 로고
    • Function of tubulin binding proteins in vivo
    • FLEMING, J., L. VEGA and F. SOLOMON, 2000 Function of tubulin binding proteins in vivo. Genetics 156: 69-80.
    • (2000) Genetics , vol.156 , pp. 69-80
    • Fleming, J.1    Vega, L.2    Solomon, F.3
  • 15
    • 0014944410 scopus 로고
    • Interaction of morphogenetic genes of bacteriophage T4
    • FLOOR, E., 1970 Interaction of morphogenetic genes of bacteriophage T4. J. Mol. Biol. 47: 293-306.
    • (1970) J. Mol. Biol. , vol.47 , pp. 293-306
    • Floor, E.1
  • 16
    • 0030923317 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways
    • GEISER, J. R., E. J. SCHOTT, T. J. KINGSBURY, N. B. COLE, L. J. TOTIS et al., 1997 Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways. Mol. Biol. Cell 8: 1035-1050.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1035-1050
    • Geiser, J.R.1    Schott, E.J.2    Kingsbury, T.J.3    Cole, N.B.4    Totis, L.J.5
  • 17
    • 0032481303 scopus 로고    scopus 로고
    • A novel protein complex promoting formation of functional alpha- and gamma-tubulin
    • GEISSLER, S., K. SIEGERS and E. SCHIEBEL, 1998 A novel protein complex promoting formation of functional alpha- and gamma-tubulin. EMBO J. 17: 952-966.
    • (1998) EMBO J. , vol.17 , pp. 952-966
    • Geissler, S.1    Siegers, K.2    Schiebel, E.3
  • 19
    • 0345518025 scopus 로고    scopus 로고
    • Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
    • HANSEN, W. J., N. J. COWAN and W. J. WELCH, 1999 Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins. J. Cell Biol. 145: 265-277.
    • (1999) J. Cell Biol. , vol.145 , pp. 265-277
    • Hansen, W.J.1    Cowan, N.J.2    Welch, W.J.3
  • 20
    • 0030748745 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability
    • HOYT, M. A., J. P. MACKE, B. T. ROBERTS and J. R. GEISER, 1997 Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability. Genetics 146: 849-857.
    • (1997) Genetics , vol.146 , pp. 849-857
    • Hoyt, M.A.1    Macke, J.P.2    Roberts, B.T.3    Geiser, J.R.4
  • 21
    • 0029830766 scopus 로고    scopus 로고
    • Fission yeast genes which disrupt mitotic chromosome segregation when overexpressed
    • JAVERZAT, J., G. CRANSTON and R. C. ALLSHIRE, 1996 Fission yeast genes which disrupt mitotic chromosome segregation when overexpressed. Nucleic Acids Res. 24: 4676-4683.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4676-4683
    • Javerzat, J.1    Cranston, G.2    Allshire, R.C.3
  • 22
    • 0025063865 scopus 로고
    • Regulation of tubulin levels and microtubule assembly in Saccharomyces cerevisiae consequences of altered tubulin gene copy number in yeast
    • KATZ, W., B. WEINSTEIN and F. SOLOMON, 1990 Regulation of tubulin levels and microtubule assembly in Saccharomyces cerevisiae consequences of altered tubulin gene copy number in yeast. Mol. Cell. Biol. 10: 2730-2736.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2730-2736
    • Katz, W.1    Weinstein, B.2    Solomon, F.3
  • 23
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • LONGTINE, M. S., A. MCKENZIE, D. J. DEMARINI, N. G. SHAH, A. WACH et al., 1998 Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14: 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    Mckenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5
  • 24
    • 0034193525 scopus 로고    scopus 로고
    • The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking
    • MCCALLUM, C. D., H. DO, A. E. JOHNSON and J. FRYDMAN, 2000 The interaction of the chaperonin tailless complex polypeptide 1 (TCP1) ring complex (TRiC) with ribosome-bound nascent chains examined using photo-cross-linking. J. Cell Biol. 149: 591-601.
    • (2000) J. Cell Biol. , vol.149 , pp. 591-601
    • Mccallum, C.D.1    Do, H.2    Johnson, A.E.3    Frydman, J.4
  • 25
    • 0037062473 scopus 로고    scopus 로고
    • Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex
    • MCLAUGHLIN, J. N., C. D. THULIN, S. J. HART, K. A. RESING, N. G. AHN et al., 2002 Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex. Proc. Natl. Acad. Sci. USA 99: 117-121.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 117-121
    • Mclaughlin, J.N.1    Thulin, C.D.2    Hart, S.J.3    Resing, K.A.4    Ahn, N.G.5
  • 26
    • 0022819847 scopus 로고
    • Genetically essential and nonessential α-tubulin genes specify functionally interchangeable proteins
    • SCHATZ, P. J., F. SOLOMON and D. BOTSTEIN, 1986 Genetically essential and nonessential α-tubulin genes specify functionally interchangeable proteins. Mol. Cell. Biol. 6: 3722-3733.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3722-3733
    • Schatz, P.J.1    Solomon, F.2    Botstein, D.3
  • 27
    • 0023424071 scopus 로고
    • Insertions of up to 17 amino acids into a region of α-tubulin do not disrupt function in vivo
    • SCHATZ, P. J., G. E. GEORGES, F. SOLOMON and D. BOTSTEIN, 1987 Insertions of up to 17 amino acids into a region of α-tubulin do not disrupt function in vivo. Mol. Cell. Biol. 7: 3799-3805.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3799-3805
    • Schatz, P.J.1    Georges, G.E.2    Solomon, F.3    Botstein, D.4
  • 29
    • 0033521523 scopus 로고    scopus 로고
    • Compartmentation of protein foldling in vivo: Sequestration of non-native polypeptides by the chaperonin-GimC system
    • SIEGERS, K., T. WALDMANN, M. R. LEROUX, K. GREIN, A. SHEVCHENKO et al., 1999 Compartmentation of protein foldling in vivo: sequestration of non-native polypeptides by the chaperonin-GimC system. EMBO J. 18: 75-84.
    • (1999) EMBO J. , vol.18 , pp. 75-84
    • Siegers, K.1    Waldmann, T.2    Leroux, M.R.3    Grein, K.4    Shevchenko, A.5
  • 30
    • 0002474415 scopus 로고
    • Methods for studying the yeast cytoskeleton
    • edited by K. Carraway and C. Carraway. Oxford University Press, Oxford
    • SOLOMON, F., L. CONNELL, D. KIRKPATRICK, V. PRAITIS and B. WEINSTEIN, 1992 Methods for studying the yeast cytoskeleton, pp. 197-222 in The Cytoskeleton, edited by K. CARRAWAY and C. CARRAWAY. Oxford University Press, Oxford.
    • (1992) The Cytoskeleton , pp. 197-222
    • Solomon, F.1    Connell, L.2    Kirkpatrick, D.3    Praitis, V.4    Weinstein, B.5
  • 31
    • 0025057481 scopus 로고
    • Yeast mutants sensitive to antimicrotubule drugs define the genes that affect microtubule function
    • STEARNS, T., M. HOYT and D. BOTSTEIN, 1990 Yeast mutants sensitive to antimicrotubule drugs define the genes that affect microtubule function. Genetics 124: 251-262.
    • (1990) Genetics , vol.124 , pp. 251-262
    • Stearns, T.1    Hoyt, M.2    Botstein, D.3
  • 32
    • 0017187520 scopus 로고
    • A genetic analysis of bacteriophage 1 head assembly
    • STERNBERG, N., 1976 A genetic analysis of bacteriophage 1 head assembly. Virology 71: 568-582.
    • (1976) Virology , vol.71 , pp. 568-582
    • Sternberg, N.1
  • 33
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • TIAN, G., S. LEWIS, B. FEIERBACH, T. STEARNS, H. ROMMELAERE et al., 1997 Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J. Cell Biol. 138: 821-832.
    • (1997) J. Cell Biol. , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5
  • 34
    • 0026345831 scopus 로고
    • The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
    • URSIC, D., and M. CULBERTSON, 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.2
  • 35
    • 0032577573 scopus 로고    scopus 로고
    • Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
    • VAINBERG, I. E., S. A. LEWIS, H. ROMMELAERE, C. AMPE, J. VANDEKERCKHOVE et al., 1998 Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93: 863-873.
    • (1998) Cell , vol.93 , pp. 863-873
    • Vainberg, I.E.1    Lewis, S.A.2    Rommelaere, H.3    Ampe, C.4    Vandekerckhove, J.5
  • 36
    • 0031671082 scopus 로고    scopus 로고
    • An α-tubulin mutant destabilizes the heterodimer: Phenotypic consequences and interactions with tubulin-binding proteins
    • VEGA, L., J. FLEMING and F. SOLOMON, 1998 An α-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins. Mol. Biol. Cell 9: 2349-2360.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2349-2360
    • Vega, L.1    Fleming, J.2    Solomon, F.3
  • 37
    • 0025075301 scopus 로고
    • Phenotypic consequences of tubulin overproduction in Saccharomyces cerevisiae: Differences between alpha-tubulin and beta-tubulin
    • WEINSTEIN, B., and F. SOLOMON, 1990 Phenotypic consequences of tubulin overproduction in Saccharomyces cerevisiae: differences between alpha-tubulin and beta-tubulin. Mol. Cell. Biol. 10: 5295-5304.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5295-5304
    • Weinstein, B.1    Solomon, F.2
  • 38
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • WEISSMAN, J., Y. KASHI, W. FENTON and A. HORWICH, 1994 GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78: 693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.1    Kashi, Y.2    Fenton, W.3    Horwich, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.