메뉴 건너뛰기




Volumn 16, Issue 12, 1996, Pages 7161-7172

A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; MALONYL COENZYME A; MESSENGER RNA; MUTANT PROTEIN; NUCLEOPORIN; VERY LONG CHAIN FATTY ACID;

EID: 0029973561     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.12.7161     Document Type: Article
Times cited : (157)

References (93)
  • 2
    • 0026562139 scopus 로고
    • Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase
    • Al-Feel, W., S. Chirala, and S. Wakil. 1992. Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase. Proc. Natl. Acad. Sci. USA 89:4534-4538.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4534-4538
    • Al-Feel, W.1    Chirala, S.2    Wakil, S.3
  • 3
    • 0023134923 scopus 로고
    • A sphingomyelinase-resistant pool of sphingomyelin in the nuclear membrane of hen erythrocytes
    • Allan, D., and P. J. Raval. 1987. A sphingomyelinase-resistant pool of sphingomyelin in the nuclear membrane of hen erythrocytes. Biochim. Biophys. Acta 897:355-363.
    • (1987) Biochim. Biophys. Acta , vol.897 , pp. 355-363
    • Allan, D.1    Raval, P.J.2
  • 5
    • 0023788651 scopus 로고
    • Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein
    • Aris, J. P., and G. Blobel. 1988. Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein. J Cell Biol. 107:17-31.
    • (1988) J Cell Biol. , vol.107 , pp. 17-31
    • Aris, J.P.1    Blobel, G.2
  • 7
    • 0024150892 scopus 로고
    • Assembly of phospholipids into cellular membranes: Biosynthesis, transmembrane movement and intracellular translocation
    • Bishop, R. W., and R. M. Bell. 1988. Assembly of phospholipids into cellular membranes: biosynthesis, transmembrane movement and intracellular translocation. Annu. Rev. Cell Biol. 4:579-610.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 579-610
    • Bishop, R.W.1    Bell, R.M.2
  • 8
    • 0025993884 scopus 로고
    • Physical properties of the fluid lipid-bilayer component of cell membranes: A perspective
    • Bloom, M., E. Evans, and O. G. Mouritsen. 1991. Physical properties of the fluid lipid-bilayer component of cell membranes: a perspective. Q. Rev. Biophys. 24:293-397.
    • (1991) Q. Rev. Biophys. , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 9
    • 0027944460 scopus 로고
    • nup1 mutants exhibit pleiotropic defects in nuclear pore complex function
    • Bogerd, A. M., J. Hoffman, D. Amberg, G. Fink, and L. Davis. 1994. nup1 mutants exhibit pleiotropic defects in nuclear pore complex function. J. Cell Biol. 127:319-332.
    • (1994) J. Cell Biol. , vol.127 , pp. 319-332
    • Bogerd, A.M.1    Hoffman, J.2    Amberg, D.3    Fink, G.4    Davis, L.5
  • 10
    • 0025785410 scopus 로고
    • A family of low and high copy replicative, integralive and single-stranded S. cerevisiae/E. coli shuttle vectors
    • Bonneaud, N., O. Ozier-Kalogeropoulos, G. Li, M. Labouesse, L. Minvielle-Sebastia, and F. Lacroute. 1991. A family of low and high copy replicative, integralive and single-stranded S. cerevisiae/E. coli shuttle vectors. Yeast 7:609-615.
    • (1991) Yeast , vol.7 , pp. 609-615
    • Bonneaud, N.1    Ozier-Kalogeropoulos, O.2    Li, G.3    Labouesse, M.4    Minvielle-Sebastia, L.5    Lacroute, F.6
  • 11
    • 0017894322 scopus 로고
    • Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase
    • Brown, M. S., J. Faust, J. Goldstein, I. Kaneko, and A. Endo. 1978. Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase. J. Biol. Chem. 253:1121-1128.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1121-1128
    • Brown, M.S.1    Faust, J.2    Goldstein, J.3    Kaneko, I.4    Endo, A.5
  • 12
    • 0027957512 scopus 로고
    • Polyketide biosynthesis: Molecular recognition or genetic programming?
    • Cane, D. E. 1994. Polyketide biosynthesis: molecular recognition or genetic programming? Science 263:338-340.
    • (1994) Science , vol.263 , pp. 338-340
    • Cane, D.E.1
  • 13
    • 0020078214 scopus 로고
    • Two differentially regulated mRNA with different 5′ end encode secreted and intracellular forms of yeast invertase
    • Carlson, M., and D. Botstein. 1982. Two differentially regulated mRNA with different 5′ end encode secreted and intracellular forms of yeast invertase. Cell 28:145-154.
    • (1982) Cell , vol.28 , pp. 145-154
    • Carlson, M.1    Botstein, D.2
  • 14
    • 0028216507 scopus 로고
    • Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: Identification of a functional UASINO and sequences responsible for fatty acid mediated repression
    • Chirala, S. S., Q. Zhong, W. Huang, and W. Al-Feel. 1994. Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: identification of a functional UASINO and sequences responsible for fatty acid mediated repression. Nucleic Acids Res. 22:412-418.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 412-418
    • Chirala, S.S.1    Zhong, Q.2    Huang, W.3    Al-Feel, W.4
  • 15
    • 0026544667 scopus 로고
    • The fatty acid chain elongation system of mammalian endoplasmic reticulum
    • Cinti, D. L., L. Cook, M. Nagi, and S. K. Suneja. 1992. The fatty acid chain elongation system of mammalian endoplasmic reticulum. Prog. Lipid Res. 31:1-51.
    • (1992) Prog. Lipid Res. , vol.31 , pp. 1-51
    • Cinti, D.L.1    Cook, L.2    Nagi, M.3    Suneja, S.K.4
  • 16
    • 0026592312 scopus 로고
    • Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae
    • Conzelmann, A., A. Puoti, R. Lester, and C. Desponds. 1992. Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae. EMBO J. 11:457-466.
    • (1992) EMBO J. , vol.11 , pp. 457-466
    • Conzelmann, A.1    Puoti, A.2    Lester, R.3    Desponds, C.4
  • 17
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis, L. I. 1995. The nuclear pore complex. Annu. Rev. Biochem. 64:365-396.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 365-396
    • Davis, L.I.1
  • 18
    • 0020788538 scopus 로고
    • Synthesis and polymorphic phase behavior of polyunsaturated phosphatidylcholines and phosphatidylethanolamines
    • Dekker, C., G. Van Kessel, J. Klomp, J. Pieters, and B. De Kruijff. 1983. Synthesis and polymorphic phase behavior of polyunsaturated phosphatidylcholines and phosphatidylethanolamines. Chem. Phys. Lipids 33:93-106.
    • (1983) Chem. Phys. Lipids , vol.33 , pp. 93-106
    • Dekker, C.1    Van Kessel, G.2    Klomp, J.3    Pieters, J.4    De Kruijff, B.5
  • 19
    • 0016757668 scopus 로고
    • Control of fatty acid-synthetase biosynthesis in Saccharomyces cerevisiae
    • Dietlein, G., and E. Schweizer. 1975. Control of fatty acid-synthetase biosynthesis in Saccharomyces cerevisiae. Eur. J. Biochem. 58:177-184.
    • (1975) Eur. J. Biochem. , vol.58 , pp. 177-184
    • Dietlein, G.1    Schweizer, E.2
  • 20
    • 0026458016 scopus 로고
    • The nuclear membrane
    • Dingwall, C., and R. Laskey. 1992. The nuclear membrane. Science 258:942-947.
    • (1992) Science , vol.258 , pp. 942-947
    • Dingwall, C.1    Laskey, R.2
  • 21
    • 0028607144 scopus 로고
    • A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution
    • Doye, V., R. Wepf, and E. Hurt. 1994. A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution. EMBO J. 13:6062-6075.
    • (1994) EMBO J. , vol.13 , pp. 6062-6075
    • Doye, V.1    Wepf, R.2    Hurt, E.3
  • 22
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evan, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evan, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 23
    • 0014216989 scopus 로고
    • Chain elongation, 2-hydroxylation, and decarboxylation of long chain fatty acids by yeast
    • Fulco, A. J. 1967. Chain elongation, 2-hydroxylation, and decarboxylation of long chain fatty acids by yeast. J. Biol. Chem. 242:3608-3613.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3608-3613
    • Fulco, A.J.1
  • 24
    • 0029047324 scopus 로고
    • A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes
    • Gorsch, L. C., T. Dockendorff, and C. N. Cole. 1995. A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J. Cell Biol. 129:939-955.
    • (1995) J. Cell Biol. , vol.129 , pp. 939-955
    • Gorsch, L.C.1    Dockendorff, T.2    Cole, C.N.3
  • 25
    • 0026500909 scopus 로고
    • Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein
    • Greber, U. F., and L. Gerace. 1992. Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein. J. Cell Biol. 116:15-30.
    • (1992) J. Cell Biol. , vol.116 , pp. 15-30
    • Greber, U.F.1    Gerace, L.2
  • 26
    • 3643086107 scopus 로고
    • Synthesis of long-chain fatty acids by microsomes of pigeon liver
    • Guchhait, R. B., G. Putz, and J. W. Porter. 1966. Synthesis of long-chain fatty acids by microsomes of pigeon liver. Arch. Biochem. Biophys. 117:541-549.
    • (1966) Arch. Biochem. Biophys. , vol.117 , pp. 541-549
    • Guchhait, R.B.1    Putz, G.2    Porter, J.W.3
  • 27
    • 0029004225 scopus 로고
    • Mapping of the ACC1/FAS3 gene to the right arm of chromosome XIV of Saccharomyces cerevisiae
    • Guerra, C. E., and H. L. Klein. 1995. Mapping of the ACC1/FAS3 gene to the right arm of chromosome XIV of Saccharomyces cerevisiae. Yeast 11: 697-700.
    • (1995) Yeast , vol.11 , pp. 697-700
    • Guerra, C.E.1    Klein, H.L.2
  • 28
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
    • Hampton, R. Y., and J. Rine. 1994. Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J. Cell Biol. 125:299-312.
    • (1994) J. Cell Biol. , vol.125 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 29
    • 0024795323 scopus 로고
    • Regulation of fatty acid synthesis via phosphorylation of acetyl-CoA carboxylase
    • Hardie, D. G. 1989. Regulation of fatty acid synthesis via phosphorylation of acetyl-CoA carboxylase. Prog. Lipid Res. 28:117-146.
    • (1989) Prog. Lipid Res. , vol.28 , pp. 117-146
    • Hardie, D.G.1
  • 30
    • 85035176388 scopus 로고
    • A beta-ketoacyl synthase is essential for normal mitochondrial function
    • Harrington, A., C. Herbert, and P. Slonimski. 1992. A beta-ketoacyl synthase is essential for normal mitochondrial function. Yeast 8:S414.
    • (1992) Yeast , vol.8
    • Harrington, A.1    Herbert, C.2    Slonimski, P.3
  • 31
    • 0027289677 scopus 로고
    • Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism
    • Hasslacher, M., A. Ivessa, F. Paltauf, and S. D. Kohlwein. 1993. Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism. J. Biol. Chem. 268:10946-10952.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10946-10952
    • Hasslacher, M.1    Ivessa, A.2    Paltauf, F.3    Kohlwein, S.D.4
  • 32
    • 0029032146 scopus 로고
    • Intracellular transport of inositol-containing sphingolipids in the yeast, Saccharomyces cerevisiae
    • Hechtberger, P., and G. Daum. 1995. Intracellular transport of inositol-containing sphingolipids in the yeast, Saccharomyces cerevisiae. FEBS Lett. 367:201-204.
    • (1995) FEBS Lett. , vol.367 , pp. 201-204
    • Hechtberger, P.1    Daum, G.2
  • 33
    • 0015850305 scopus 로고
    • An investigation into the role of malonyl-coenzyme A in isoprenoid biosynthesis
    • Higgins, M. J. P., and R. Kekwick. 1973. An investigation into the role of malonyl-coenzyme A in isoprenoid biosynthesis. Biochem. J. 134:295-310.
    • (1973) Biochem. J. , vol.134 , pp. 295-310
    • Higgins, M.J.P.1    Kekwick, R.2
  • 34
    • 0025606149 scopus 로고
    • Molecular genetics of polyketides and its comparison to fatty acid biosynthesis
    • Hopwood, D. A., and D. Sherman. 1990. Molecular genetics of polyketides and its comparison to fatty acid biosynthesis. Annu. Rev. Genet. 24:37-66.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 37-66
    • Hopwood, D.A.1    Sherman, D.2
  • 35
    • 0023324194 scopus 로고
    • Possible involvement of acetyl coenzyme A carboxylase as well as fatty acid synthetase in the temperature-controlled synthesis of fatty acids in Saccharomyces cerevisiae
    • Hori, T., N. Nakamura, and H. Okuyama. 1987. Possible involvement of acetyl coenzyme A carboxylase as well as fatty acid synthetase in the temperature-controlled synthesis of fatty acids in Saccharomyces cerevisiae. J. Biochem. 101:949-956.
    • (1987) J. Biochem. , vol.101 , pp. 949-956
    • Hori, T.1    Nakamura, N.2    Okuyama, H.3
  • 36
    • 0021676607 scopus 로고
    • Acyl chain interdigitation in saturated mixed-chain phosphatidylcholine bilayer dispersions
    • Hui, S., T. Mason, and C.-H. Huang, 1984. Acyl chain interdigitation in saturated mixed-chain phosphatidylcholine bilayer dispersions. Biochemistry 23:5570-5577.
    • (1984) Biochemistry , vol.23 , pp. 5570-5577
    • Hui, S.1    Mason, T.2    Huang, C.-H.3
  • 38
    • 0020529962 scopus 로고
    • Transformation of intact cells with alkali cations
    • Ho, H., Y. Fukada, K. Murata, and A. Kimura. 1983. Transformation of intact cells with alkali cations. J. Bacteriol. 153:163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ho, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 39
    • 0026041521 scopus 로고
    • The gene encoding squalene epoxidase from Saccharomyces cerevisiae: Cloning and characterization
    • Jandrositz, A., F. Turnowsky, and G. Hegenauer. 1991. The gene encoding squalene epoxidase from Saccharomyces cerevisiae: cloning and characterization. Gene 107:155-160.
    • (1991) Gene , vol.107 , pp. 155-160
    • Jandrositz, A.1    Turnowsky, F.2    Hegenauer, G.3
  • 40
    • 0027984281 scopus 로고
    • Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: An assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism
    • Johnson, D. R., L. Knoll, D. Levin, and J. I. Gordon. 1994. Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism. J. Cell Biol. 127:751-762.
    • (1994) J. Cell Biol. , vol.127 , pp. 751-762
    • Johnson, D.R.1    Knoll, L.2    Levin, D.3    Gordon, J.I.4
  • 42
    • 0026506656 scopus 로고
    • A conditional yeast mutant deficient in mRNA transport from nucleus to cytoplasm
    • Kadowaki, T., Y. Zhao, and A. M. Tartakoff. 1992. A conditional yeast mutant deficient in mRNA transport from nucleus to cytoplasm. Proc. Natl. Acad. Sci. USA 89:2312-2316.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2312-2316
    • Kadowaki, T.1    Zhao, Y.2    Tartakoff, A.M.3
  • 43
  • 44
    • 85035176286 scopus 로고    scopus 로고
    • Unpublished observations
    • Kohlwein, S. D. Unpublished observations.
    • Kohlwein, S.D.1
  • 45
    • 0021756791 scopus 로고
    • Uptake of fatty acids by the yeast, Saccharomyces cerevisiae and Yarrowia lipolytica
    • Kohlwein, S. D., and F. Paltauf. 1983. Uptake of fatty acids by the yeast, Saccharomyces cerevisiae and Yarrowia lipolytica. Biochim. Biophys. Acta 792:310-317.
    • (1983) Biochim. Biophys. Acta , vol.792 , pp. 310-317
    • Kohlwein, S.D.1    Paltauf, F.2
  • 46
    • 0025728506 scopus 로고
    • The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated
    • Kottig, H., G. Rottner, K.-F. Beck, M. Schweizer, and E. Schweizer. 1991. The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated. Mol. Gen. Genet. 226:310-314.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 310-314
    • Kottig, H.1    Rottner, G.2    Beck, K.-F.3    Schweizer, M.4    Schweizer, E.5
  • 47
    • 0025129813 scopus 로고
    • Cloning by function: An alternative approach for identifying yeast homologs of genes from other organisms
    • Kranz, J., and C. Holm. 1990. Cloning by function: an alternative approach for identifying yeast homologs of genes from other organisms. Proc. Natl. Acad. Sci. USA 87:6629-6633.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6629-6633
    • Kranz, J.1    Holm, C.2
  • 48
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 49
    • 0345470654 scopus 로고
    • Acetyl coenzyme A carboxylase
    • K. E. Ebner (ed.). Marcel Dekker, Inc., New York
    • Lane, M. D., J. Moss, and S. E. Polakis. 1975. Acetyl coenzyme A carboxylase, p. 181-221. In K. E. Ebner (ed.). Subunit enzymes. Biochemistry and function. Marcel Dekker, Inc., New York.
    • (1975) Subunit Enzymes. Biochemistry and Function , pp. 181-221
    • Lane, M.D.1    Moss, J.2    Polakis, S.E.3
  • 50
    • 0027350083 scopus 로고
    • Sphingolipids with inositolphosphate-containing head groups
    • Lester, R. L., and R. C. Dickson. 1993. Sphingolipids with inositolphosphate-containing head groups. Adv. Lipid Res. 26:253-274.
    • (1993) Adv. Lipid Res. , vol.26 , pp. 253-274
    • Lester, R.L.1    Dickson, R.C.2
  • 51
    • 0027404090 scopus 로고
    • Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerolipids that mimic sphingolipid structure
    • Lester, R. L., G. Wells, G. Oxford, and R. C. Dickson. 1993. Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerolipids that mimic sphingolipid structure. J. Biol. Chem. 268:845-856.
    • (1993) J. Biol. Chem. , vol.268 , pp. 845-856
    • Lester, R.L.1    Wells, G.2    Oxford, G.3    Dickson, R.C.4
  • 52
    • 0029040699 scopus 로고
    • Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes
    • Li, O., C. Heath, D. Amberg, T. Dockendorff, C. Copeland, M. Snyder, and C. N. Cole. 1995. Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes. Mol. Biol. Cell 6:401-417.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 401-417
    • Li, O.1    Heath, C.2    Amberg, D.3    Dockendorff, T.4    Copeland, C.5    Snyder, M.6    Cole, C.N.7
  • 53
    • 0026084947 scopus 로고
    • Effects of small organic molecules on phospholipid phase transitions
    • Lohner, K. 1991. Effects of small organic molecules on phospholipid phase transitions. Chem. Phys. Lipids 57:341-362.
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 341-362
    • Lohner, K.1
  • 54
    • 84886636405 scopus 로고
    • Subunit size and paracrystal structure of avian liver acetyl-CoA carboxylase
    • Mackall, J. C., and M. D. Lane. 1978. Subunit size and paracrystal structure of avian liver acetyl-CoA carboxylase. J. Mol. Biol. 123:595-606.
    • (1978) J. Mol. Biol. , vol.123 , pp. 595-606
    • Mackall, J.C.1    Lane, M.D.2
  • 55
    • 0026588744 scopus 로고
    • The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton
    • Mirzayan, C., C. Copeland, and M. Snyder. 1992. The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton. J. Cell Biol. 116:1319-1332.
    • (1992) J. Cell Biol. , vol.116 , pp. 1319-1332
    • Mirzayan, C.1    Copeland, C.2    Snyder, M.3
  • 56
    • 0019136545 scopus 로고
    • Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin: Apocarboxylase ligase. Eur
    • Mishina, M., R. Roggenkamp, and E. Schweizer. 1980. Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin: apocarboxylase ligase. Eur. J. Biochem. 111:79-87.
    • (1980) J. Biochem. , vol.111 , pp. 79-87
    • Mishina, M.1    Roggenkamp, R.2    Schweizer, E.3
  • 57
    • 0024239166 scopus 로고
    • Primary structure of the multifunctional a subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence
    • Mohamed, A. H., S. Chirala, N. Mody, W.-Y. Huang, and S. Wakil. 1988. Primary structure of the multifunctional a subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence. J. Biol. Chem. 263:12315-12325.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12315-12325
    • Mohamed, A.H.1    Chirala, S.2    Mody, N.3    Huang, W.-Y.4    Wakil, S.5
  • 58
    • 0021474573 scopus 로고
    • Mattress model of lipid-protein interactions in membranes
    • Mouritsen, O. G., and M. Bloom. 1984. Mattress model of lipid-protein interactions in membranes. Biophys. J. 46:141-153.
    • (1984) Biophys. J. , vol.46 , pp. 141-153
    • Mouritsen, O.G.1    Bloom, M.2
  • 59
    • 0027053912 scopus 로고
    • NSP1 depletion in yeast affects nuclear pore formation and nuclear accumulation
    • Mutvei, A., S. Dihlmann, W. Herth, and E. Hurt. 1992, NSP1 depletion in yeast affects nuclear pore formation and nuclear accumulation. Eur. J. Cell Biol. 59:280-295.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 280-295
    • Mutvei, A.1    Dihlmann, S.2    Herth, W.3    Hurt, E.4
  • 60
    • 0015176498 scopus 로고
    • Occurrence of long-chain fatty acids and glycolipids in the cell envelope fraction of baker's yeast
    • Nurminen, T., and H. Suomalainen. 1971. Occurrence of long-chain fatty acids and glycolipids in the cell envelope fraction of baker's yeast. Biochem. J. 125:963-969.
    • (1971) Biochem. J. , vol.125 , pp. 963-969
    • Nurminen, T.1    Suomalainen, H.2
  • 62
    • 0019763102 scopus 로고
    • Cerulenin
    • Omura, S. 1981. Cerulenin. Methods Enzymol. 72:520-532.
    • (1981) Methods Enzymol. , vol.72 , pp. 520-532
    • Omura, S.1
  • 63
    • 0025064559 scopus 로고
    • Lipid traffic in eukaryotic cells: Mechanisms for intracellular transport and organelle-specific enrichment of lipids
    • Pagano, R. E. 1990. Lipid traffic in eukaryotic cells: mechanisms for intracellular transport and organelle-specific enrichment of lipids. Curr. Opin. Cell Biol. 2:652-663.
    • (1990) Curr. Opin. Cell Biol. , vol.2 , pp. 652-663
    • Pagano, R.E.1
  • 64
    • 0025760201 scopus 로고
    • The phosphoinositol sphingolipids of Saccharomyces cerevisiae are highly localized in the plasma membrane
    • Patton, J. L., and R. L. Lester. 1991. The phosphoinositol sphingolipids of Saccharomyces cerevisiae are highly localized in the plasma membrane. J. Bacteriol. 173:3101-3108.
    • (1991) J. Bacteriol. , vol.173 , pp. 3101-3108
    • Patton, J.L.1    Lester, R.L.2
  • 65
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R., and D. J. Lipman. 1988. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA 85:2444-2448.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 66
    • 0026697256 scopus 로고
    • Sphingolipid long-chain-base auxotrophs of Saccharomyces cerevisiae: Genetics, physiology, and a method for their selection
    • Pinto, W. J., B. Srinivasan, S. Shepherd, A. Schmidt, R. C. Dickson, and R. L. Lester. 1992. Sphingolipid long-chain-base auxotrophs of Saccharomyces cerevisiae: genetics, physiology, and a method for their selection. J. Bacteriol. 174:2565-2574.
    • (1992) J. Bacteriol. , vol.174 , pp. 2565-2574
    • Pinto, W.J.1    Srinivasan, B.2    Shepherd, S.3    Schmidt, A.4    Dickson, R.C.5    Lester, R.L.6
  • 67
    • 0027155419 scopus 로고
    • Physical maps of the six smallest chromosomes of Saccharomyces cerevisiae at a resolution of 2.6 kilobase pairs
    • Riles, L., J. Dutchik, A. Baktha, B. McCauley, E. Thayer, M. Leckie, V. Braden, J. Depke, and M. Olson. 1993. Physical maps of the six smallest chromosomes of Saccharomyces cerevisiae at a resolution of 2.6 kilobase pairs. Genetics 134:81-150.
    • (1993) Genetics , vol.134 , pp. 81-150
    • Riles, L.1    Dutchik, J.2    Baktha, A.3    McCauley, B.4    Thayer, E.5    Leckie, M.6    Braden, V.7    Depke, J.8    Olson, M.9
  • 68
    • 0018821092 scopus 로고
    • Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in acetyl-CoA carboxylase
    • Roggenkamp, R., S. Numa, and E. Schweizer. 1980. Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in acetyl-CoA carboxylase. Proc. Natl. Acad. Sci. USA 77:1814-1817.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1814-1817
    • Roggenkamp, R.1    Numa, S.2    Schweizer, E.3
  • 69
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 72
    • 0025149093 scopus 로고
    • Structure of the glycosylphosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease
    • Schneider, P., M. Ferguson, M. McConville, A. Mehlert, S. Homans, and C. Bordier. 1990. Structure of the glycosylphosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease. J. Biol. Chem. 265:16955-16964.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16955-16964
    • Schneider, P.1    Ferguson, M.2    McConville, M.3    Mehlert, A.4    Homans, S.5    Bordier, C.6
  • 73
    • 0002247954 scopus 로고
    • Biosynthesis of fatty acids and related compounds
    • C. Ratledge and S. G. Wilkinson (ed.), Academic Press, New York
    • Schweizer, E. 1989. Biosynthesis of fatty acids and related compounds, p. 3-50. In C. Ratledge and S. G. Wilkinson (ed.), Microbial lipids, vol. 2. Academic Press, New York.
    • (1989) Microbial Lipids , vol.2 , pp. 3-50
    • Schweizer, E.1
  • 74
    • 0014856315 scopus 로고
    • A Saccharomyces cerevisiae mutant defective in saturated fatty acid biosynthesis
    • Schweizer, E., and H. Bolling. 1970. A Saccharomyces cerevisiae mutant defective in saturated fatty acid biosynthesis. Proc. Natl. Acad. Sci. USA 67:660-666.
    • (1970) Proc. Natl. Acad. Sci. USA , vol.67 , pp. 660-666
    • Schweizer, E.1    Bolling, H.2
  • 75
    • 0015713331 scopus 로고
    • Pantetheine-free mutants of the yeast fatty-acid-synthetase complex
    • Schweizer, E., B. Kniep, H. Castorph, and U. Holzner. 1973. Pantetheine-free mutants of the yeast fatty-acid-synthetase complex. Eur. J. Biochem. 39:353-362.
    • (1973) Eur. J. Biochem. , vol.39 , pp. 353-362
    • Schweizer, E.1    Kniep, B.2    Castorph, H.3    Holzner, U.4
  • 76
    • 0017157457 scopus 로고
    • Nuclear pore absence from areas of close association between nucleus and vacuole in synchronous yeast cultures
    • Severs, N. J., E. Jordan, and D. H. Williamson. 1976. Nuclear pore absence from areas of close association between nucleus and vacuole in synchronous yeast cultures. J. Ultrastruct. Res. 54:374-387.
    • (1976) J. Ultrastruct. Res. , vol.54 , pp. 374-387
    • Severs, N.J.1    Jordan, E.2    Williamson, D.H.3
  • 77
    • 0027908038 scopus 로고
    • Enzymatic synthesis of a bacterial polyketide from acetyl and malonyl coenzyme A
    • Shen, B., and C. R. Hutchinson. 1993. Enzymatic synthesis of a bacterial polyketide from acetyl and malonyl coenzyme A. Science 262:1535-1540.
    • (1993) Science , vol.262 , pp. 1535-1540
    • Shen, B.1    Hutchinson, C.R.2
  • 79
    • 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
  • 80
    • 0024021255 scopus 로고
    • Mutations that alter both localization and production of a yeast nuclear protein
    • Silver, P. A., A. Chiang, and I. Sadler. 1988. Mutations that alter both localization and production of a yeast nuclear protein. Genes Dev. 2:707-717.
    • (1988) Genes Dev. , vol.2 , pp. 707-717
    • Silver, P.A.1    Chiang, A.2    Sadler, I.3
  • 81
    • 0024614502 scopus 로고
    • The contact site A glycoprotein of Dictyostelium discoideum carries a phospholipid anchor of a novel type
    • Stadler, J., T. Keenan, G. Bauer, and G. Gerisch. 1989. The contact site A glycoprotein of Dictyostelium discoideum carries a phospholipid anchor of a novel type. EMBO J. 8:371-377.
    • (1989) EMBO J. , vol.8 , pp. 371-377
    • Stadler, J.1    Keenan, T.2    Bauer, G.3    Gerisch, G.4
  • 82
    • 0025790362 scopus 로고
    • A role for unsaturated fatty acids in mitochondrial movement and inheritance
    • Stewart, L. C., and M. Y. Yaffe. 1991. A role for unsaturated fatty acids in mitochondrial movement and inheritance. J. Cell Biol. 115:1249-1257.
    • (1991) J. Cell Biol. , vol.115 , pp. 1249-1257
    • Stewart, L.C.1    Yaffe, M.Y.2
  • 83
    • 0014578732 scopus 로고
    • Die Synthese verschiedener Carbonsauren durch den Multienzymkomplex der Fettsauresynthese aus Hefe und die Erklarung ihrer Bildung
    • Sumper, M., D. Oesterhelt, C. Riepertinger, and F. Lynen. 1969. Die Synthese verschiedener Carbonsauren durch den Multienzymkomplex der Fettsauresynthese aus Hefe und die Erklarung ihrer Bildung. Eur. J. Biochem. 10:377-387.
    • (1969) Eur. J. Biochem. , vol.10 , pp. 377-387
    • Sumper, M.1    Oesterhelt, D.2    Riepertinger, C.3    Lynen, F.4
  • 84
    • 0027219942 scopus 로고
    • Molecular evolution of biotin-dependent carboxylases
    • Toh, H., H. Kondo, and T. Tanabe. 1993. Molecular evolution of biotin-dependent carboxylases. Eur. J. Biochem. 215:687-696.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 687-696
    • Toh, H.1    Kondo, H.2    Tanabe, T.3
  • 85
    • 0028032936 scopus 로고
    • Generation of glycerophospholipid molecular species in the yeast Saccharomyces cerevisiae. Fatty acid pattern of phospholipid classes and selective acyl turnover at sn-1 and sn-2 positions
    • Wagner, S., and F. Paltauf. 1994. Generation of glycerophospholipid molecular species in the yeast Saccharomyces cerevisiae. Fatty acid pattern of phospholipid classes and selective acyl turnover at sn-1 and sn-2 positions. Yeast 10:1429-1437.
    • (1994) Yeast , vol.10 , pp. 1429-1437
    • Wagner, S.1    Paltauf, F.2
  • 86
    • 0021023293 scopus 로고
    • The isolation and characterization of a mutant strain of Saccharomyces cerevisiae that requires a long chain base for growth and for synthesis of phosphosphingolipids
    • Wells, G. B., and R. L. Lester. 1983. The isolation and characterization of a mutant strain of Saccharomyces cerevisiae that requires a long chain base for growth and for synthesis of phosphosphingolipids. J. Biol. Chem. 258:10200-10203.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10200-10203
    • Wells, G.B.1    Lester, R.L.2
  • 87
    • 0027428431 scopus 로고
    • A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic
    • Wente, S. R., and G. Blobel. 1993. A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic. J. Cell Biol. 123:275-284.
    • (1993) J. Cell Biol. , vol.123 , pp. 275-284
    • Wente, S.R.1    Blobel, G.2
  • 88
    • 0028233485 scopus 로고
    • NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure
    • Wente, S. R., and G. Blobel. 1994. NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J. Cell Biol. 125:955-969.
    • (1994) J. Cell Biol. , vol.125 , pp. 955-969
    • Wente, S.R.1    Blobel, G.2
  • 89
    • 0026463881 scopus 로고
    • A new family of yeast nuclear pore complex proteins
    • Wente, S. R., M. Rout, and G. Blobel. 1992. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119:705-723.
    • (1992) J. Cell Biol. , vol.119 , pp. 705-723
    • Wente, S.R.1    Rout, M.2    Blobel, G.3
  • 90
    • 0018130990 scopus 로고
    • Altered nuclear pore diameters in G1-arrested cells of the yeast Saccharomyces cerevisiae
    • Willison, J. H. M., and G. C. Johnston. 1978. Altered nuclear pore diameters in G1-arrested cells of the yeast Saccharomyces cerevisiae. J. Bacteriol. 136: 318-323.
    • (1978) J. Bacteriol. , vol.136 , pp. 318-323
    • Willison, J.H.M.1    Johnston, G.C.2
  • 91
    • 0025356714 scopus 로고
    • Yeast acetyl-CoA carboxylase: In vitro phosphorylation by mammalian and yeast protein kinases
    • Witters, L. A., and T. D. Watts. 1990. Yeast acetyl-CoA carboxylase: in vitro phosphorylation by mammalian and yeast protein kinases. Biochem. Biophys. Res. Commun. 169:369-376.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 369-376
    • Witters, L.A.1    Watts, T.D.2
  • 92
    • 0028313943 scopus 로고
    • POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope
    • Wozniak, R. W., G. Blobel, and M. P. Rout. 1994. POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope. J. Cell Biol. 125:31-42.
    • (1994) J. Cell Biol. , vol.125 , pp. 31-42
    • Wozniak, R.W.1    Blobel, G.2    Rout, M.P.3
  • 93
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import
    • Yaffe, M. P., and G. Schatz. 1984. Two nuclear mutations that block mitochondrial protein import. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.