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Volumn 32, Issue 1-2, 1996, Pages 275-302

Proteolysis in plants: Mechanisms and functions

Author keywords

20S and 26S proteasome; Arabidopsis; biotechnology; ClpAP protease; protein degradation; ubiquitin

Indexed keywords


EID: 0030267548     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00039386     Document Type: Article
Times cited : (339)

References (221)
  • 1
    • 0028082429 scopus 로고
    • Early auxin-induced genes encode short-lived nuclear proteins
    • Abel S, Oeller PW, Theologis A: Early auxin-induced genes encode short-lived nuclear proteins. Proc Natl Acad Sci USA 91: 326-330 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 326-330
    • Abel, S.1    Oeller, P.W.2    Theologis, A.3
  • 2
    • 0025890282 scopus 로고
    • The ubiquitin-encoding multigene family of flax, Linum usitatissimum
    • Agarwal ML, Cullis CA: The ubiquitin-encoding multigene family of flax, Linum usitatissimum. Gene 99: 69-75 (1991).
    • (1991) Gene , vol.99 , pp. 69-75
    • Agarwal, M.L.1    Cullis, C.A.2
  • 3
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic signals and trigger the activation of heat shock genes
    • Anathan J, Goldberg AL, Vollemy R: Abnormal proteins serve as eukaryotic signals and trigger the activation of heat shock genes. Science 232: 522-524 (1986).
    • (1986) Science , vol.232 , pp. 522-524
    • Anathan, J.1    Goldberg, A.L.2    Vollemy, R.3
  • 4
    • 0027980297 scopus 로고
    • The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex
    • Anbudurai PR, Mor TS, Ohad I, Shestakov SV, Pakrasi HB: The ctpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex. Proc Natl Acad Sci USA 91: 8082-8086 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8082-8086
    • Anbudurai, P.R.1    Mor, T.S.2    Ohad, I.3    Shestakov, S.V.4    Pakrasi, H.B.5
  • 5
    • 0023754392 scopus 로고
    • Cotranslational processing and protein turnover in eukaryotic cells
    • Arfin S Bradshaw R: Cotranslational processing and protein turnover in eukaryotic cells. Biochemistry 27: 7979-7990 (1988).
    • (1988) Biochemistry , vol.27 , pp. 7979-7990
    • Arfin, S.1    Bradshaw, R.2
  • 6
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason T, Ellison MJ: Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol Cell Biol 14: 7876-7883 (1994).
    • (1994) Mol Cell Biol , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 7
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A: In vivo half-life of a protein is a function of its amino-terminal residue. Science 234: 179-186 (1986).
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 8
    • 0025685244 scopus 로고
    • Pertubation of the ubiquitin system causes leaf curling, vascular tissue alterations, and necrotic lesions in a higher plant
    • Bachmair A, Becker F, Masterson V, Schell J: Pertubation of the ubiquitin system causes leaf curling, vascular tissue alterations, and necrotic lesions in a higher plant. EMBO J 9: 4543-4549 (1991).
    • (1991) EMBO J , vol.9 , pp. 4543-4549
    • Bachmair, A.1    Becker, F.2    Masterson, V.3    Schell, J.4
  • 9
    • 0027388885 scopus 로고
    • Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent proteolysis
    • Bachmair A, Becker F, Schell J: Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent proteolysis. Proc Natl Acad Sci USA 90: 418-421 (1993)
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 418-421
    • Bachmair, A.1    Becker, F.2    Schell, J.3
  • 10
    • 0028314007 scopus 로고
    • Specific complex formation between yeast Rad6 and Rad18 proteins: A potential mechanism for targeting Rad6 ubiquitin-conjugating activity to DNA damage sites
    • Bailly V, Lamb J, Sung P, Prakash S, Prakash L: Specific complex formation between yeast Rad6 and Rad18 proteins: a potential mechanism for targeting Rad6 ubiquitin-conjugating activity to DNA damage sites. Genes Devel 8: 811-820 (1994).
    • (1994) Genes Devel , vol.8 , pp. 811-820
    • Bailly, V.1    Lamb, J.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 11
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long sought dibasic processing endoproteases
    • Barr PJ: Mammalian subtilisins: the long sought dibasic processing endoproteases. Cell 66: 1-3 (1991).
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 12
    • 0001777272 scopus 로고
    • The classes of proteolytic enzymes
    • Dalling MJ (ed) CRC Press, Boca Ratpn, FL
    • Barret AJ: The classes of proteolytic enzymes. In: Dalling MJ (ed) Plant ProteolyticEnzymes, pp. 1-16. CRC Press, Boca Ratpn, FL (1986).
    • (1986) Plant ProteolyticEnzymes , pp. 1-16
    • Barret, A.J.1
  • 13
    • 0027675474 scopus 로고
    • Functional expression and molecular characterization of AtUBC2-1, a novel ubiquitin conjugating enzyme (E2) from Arabidopsis thaliana
    • Bartling D, Rehling P, Weiler EW: Functional expression and molecular characterization of AtUBC2-1, a novel ubiquitin conjugating enzyme (E2) from Arabidopsis thaliana. Plant Mol Biol 23: 387-396 (1993).
    • (1993) Plant Mol Biol , vol.23 , pp. 387-396
    • Bartling, D.1    Rehling, P.2    Weiler, E.W.3
  • 14
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal R, Deveraux Q, Xia G, Rechsteiner M, Pickart C: Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc Natl Acad Sci USA 93: 861-866 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 15
    • 0026777839 scopus 로고
    • Subcellular localization of ubiquitin and ubiquitinated proteins in Arabidopsis
    • Beers E, Moreno TN, Callis JA: Subcellular localization of ubiquitin and ubiquitinated proteins in Arabidopsis. J Biol Chem 267: 15432-15439 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 15432-15439
    • Beers, E.1    Moreno, T.N.2    Callis, J.A.3
  • 16
    • 0030038126 scopus 로고    scopus 로고
    • Isolation of intact protein storage vacuoles from barley aleurone
    • Bethke PC, Hillmer S, Jones RL: Isolation of intact protein storage vacuoles from barley aleurone. Plant Physiol 110: 521-529 (1996).
    • (1996) Plant Physiol , vol.110 , pp. 521-529
    • Bethke, P.C.1    Hillmer, S.2    Jones, R.L.3
  • 17
    • 0026229773 scopus 로고
    • Structure and expression of sunflower ubiquitin genes
    • Binet M-N, Weil J-H, Tessier L-H: Structure and expression of sunflower ubiquitin genes. Plant Mol Biol 17: 395-407 (1991).
    • (1991) Plant Mol Biol , vol.17 , pp. 395-407
    • Binet, M.-N.1    Weil, J.-H.2    Tessier, L.-H.3
  • 18
    • 0001830556 scopus 로고
    • Roles of proteolytic enzymes in interactions of plants with other organisms
    • Dalling MJ (ed) CRC Press, Boca Raton, FL
    • Boller T: Roles of proteolytic enzymes in interactions of plants with other organisms. In: Dalling MJ (ed) Plant Proteolytic Enzymes, pp. 67-96. CRC Press, Boca Raton, FL (1986).
    • (1986) Plant Proteolytic Enzymes , pp. 67-96
    • Boller, T.1
  • 19
    • 0026150603 scopus 로고
    • Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants
    • Boston RS, Fontes EBP, Shank BB, Wrobel RL: Increased expression of the maize immunoglobulin binding protein homolog b-70 in three zein regulatory mutants. Plant Cell 3: 497-505 (1991).
    • (1991) Plant Cell , vol.3 , pp. 497-505
    • Boston, R.S.1    Fontes, E.B.P.2    Shank, B.B.3    Wrobel, R.L.4
  • 20
    • 0026607096 scopus 로고
    • Early hydrogen-bonding events in the folding reaction of ubiquitin
    • Briggs MS, Roder H: Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc Natl Acad Sci USA 89: 2017-2021 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2017-2021
    • Briggs, M.S.1    Roder, H.2
  • 21
    • 0028986075 scopus 로고
    • Control of IκB-α by site-specific, signal-induced phosphorylation
    • Brown K, Gerstberger S, Carlson L, Franzoso G, Siebenlist U: Control of IκB-α by site-specific, signal-induced phosphorylation. Science 267: 1485-1488 (1995).
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 22
    • 0024060207 scopus 로고
    • Characterization of a polyubiquitin gene in Arabidopsis thaliana
    • Burke TJ, Callis JA, Vierstra RD: Characterization of a polyubiquitin gene in Arabidopsis thaliana. Mol Gen Genet 213: 435-443 (1988).
    • (1988) Mol Gen Genet , vol.213 , pp. 435-443
    • Burke, T.J.1    Callis, J.A.2    Vierstra, R.D.3
  • 23
    • 0027141619 scopus 로고
    • A purified zinc protease of pea chloroplasts, EP1, degrades the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Bushnell T, Bushnell D, Jagendorf AT: A purified zinc protease of pea chloroplasts, EP1, degrades the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. Plant Physiol 103: 585-591 (1993).
    • (1993) Plant Physiol , vol.103 , pp. 585-591
    • Bushnell, T.1    Bushnell, D.2    Jagendorf, A.T.3
  • 25
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • Callis, JA: Regulation of protein degradation. Plant Cell 7: 845-857 (1995).
    • (1995) Plant Cell , vol.7 , pp. 845-857
    • Callis, J.A.1
  • 27
    • 0025370073 scopus 로고
    • Ubiquitin extension proteins in Arabidopsis thaliana: Structure, localization, and expression of their promoters in transgenic tobacco
    • Callis JA, Raasch JA, Vierstra RD: Ubiquitin extension proteins in Arabidopsis thaliana: structure, localization, and expression of their promoters in transgenic tobacco. J Biol Chem 265: 12486-12493 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 12486-12493
    • Callis, J.A.1    Raasch, J.A.2    Vierstra, R.D.3
  • 28
    • 0028836104 scopus 로고
    • Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia
    • Callis JA, Carpenter TB, Sun CW, Vierstra RD: Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia. Genetics 139: 921-939 (1995).
    • (1995) Genetics , vol.139 , pp. 921-939
    • Callis, J.A.1    Carpenter, T.B.2    Sun, C.W.3    Vierstra, R.D.4
  • 30
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M: Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell 74: 357-369 (1993).
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 31
    • 0026076015 scopus 로고
    • 25k) and overexpression of the functional enzyme in Escherichia coli
    • 25k) and overexpression of the functional enzyme in Escherichia coli. J Biol Chem 266: 15698-15704 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 15698-15704
    • Chen, Z.1    Niles, E.G.2    Pickart, C.M.3
  • 32
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang H-L, Terlecky SR, Plant CP, Dice JF: A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246: 382-385 (1989).
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.-L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 33
    • 0026816010 scopus 로고
    • Maize polyubiquitin genes: Structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation
    • Christensen AH, Sharrock RA, Quail PH: Maize polyubiquitin genes: structure, thermal perturbation of expression and transcript splicing, and promoter activity following transfer to protoplasts by electroporation. Plant Mol Biol 18: 675-689 (1992).
    • (1992) Plant Mol Biol , vol.18 , pp. 675-689
    • Christensen, A.H.1    Sharrock, R.A.2    Quail, P.H.3
  • 34
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A: The ubiquitin-proteasome proteolytic pathway. Cell 79: 13-21 (1994).
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 35
    • 26844488686 scopus 로고
    • Ubiquitinated proteins in differentiating vascular tissue of Coleus blumei
    • Collins BA, Reed PD, Rubinstein B: Ubiquitinated proteins in differentiating vascular tissue of Coleus blumei. Plant Physiol 102: 125 (1993).
    • (1993) Plant Physiol , vol.102 , pp. 125
    • Collins, B.A.1    Reed, P.D.2    Rubinstein, B.3
  • 36
    • 0026653834 scopus 로고
    • Three-dimensional structure of a ubiquitin conjugating enzyme (E2)
    • Cook WJ, Jeffrey LC, Sullivan ML, Vierstra RD: Three-dimensional structure of a ubiquitin conjugating enzyme (E2). J Biol Chem 267: 15116-15121 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 15116-15121
    • Cook, W.J.1    Jeffrey, L.C.2    Sullivan, M.L.3    Vierstra, R.D.4
  • 37
    • 0026746290 scopus 로고
    • Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2)
    • Cook WJ, Jeffrey LC, Carson M, Chen Z, Pickart CM: Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2). J Biol Chem 267: 16467-16471 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 16467-16471
    • Cook, W.J.1    Jeffrey, L.C.2    Carson, M.3    Chen, Z.4    Pickart, C.M.5
  • 38
    • 0027788114 scopus 로고
    • Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: Crystal structure of yeast Ubc4
    • Cook WJ, Jeffrey LC, Xu Y, Chau V: Tertiary structures of class I ubiquitin-conjugating enzymes are highly conserved: crystal structure of yeast Ubc4. Biochemistry 32: 13809-13817 (1993).
    • (1993) Biochemistry , vol.32 , pp. 13809-13817
    • Cook, W.J.1    Jeffrey, L.C.2    Xu, Y.3    Chau, V.4
  • 39
    • 0027975055 scopus 로고
    • Changes in protein ubiquitination and the expression of ubiquitin-encoding transcripts in daylily petals during floral development and senescence
    • Courtney SE, Rider CC, Stead AD: Changes in protein ubiquitination and the expression of ubiquitin-encoding transcripts in daylily petals during floral development and senescence. Physiol Plant 91: 196-204 (1994).
    • (1994) Physiol Plant , vol.91 , pp. 196-204
    • Courtney, S.E.1    Rider, C.C.2    Stead, A.D.3
  • 40
    • 0028110821 scopus 로고
    • The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly
    • Crane DI, Kalish JU, Gould SJ: The Pichia pastoris PAS4 gene encodes a ubiquitin-conjugating enzyme required for peroxisome assembly. J Biol Chem 269: 21835-21844 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 21835-21844
    • Crane, D.I.1    Kalish, J.U.2    Gould, S.J.3
  • 41
    • 0029328453 scopus 로고
    • Nitrate: Nutrient and signal for plant growth
    • Crawford NM: Nitrate: nutrient and signal for plant growth. Plant Cell 7: 859-868 (1995).
    • (1995) Plant Cell , vol.7 , pp. 859-868
    • Crawford, N.M.1
  • 42
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall DE, DeMartino GN: Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev 71: 813-847 (1991).
    • (1991) Physiol Rev , vol.71 , pp. 813-847
    • Croall, D.E.1    DeMartino, G.N.2
  • 43
    • 0003169169 scopus 로고
    • Chloroplast senescence and proteolytic enzymes
    • Dalling MJ (ed) CRC Press, Boca Raton, FL
    • Dalling MJ, Nettleton AM: Chloroplast senescence and proteolytic enzymes. In: Dalling MJ (ed) Plant Proteolytic Enzymes, pp. 125-53. CRC Press, Boca Raton, FL (1986).
    • (1986) Plant Proteolytic Enzymes , pp. 125-153
    • Dalling, M.J.1    Nettleton, A.M.2
  • 44
    • 0000900838 scopus 로고
    • Physiolocial aspects of protein turnover
    • Coulter D, Partier B (eds) Springer-Verlag, Berlin
    • Davies DD: Physiolocial aspects of protein turnover. In: Coulter D, Partier B (eds) Encyclopedia of Plant Physiology, vol 14A, pp. 189-228. Springer-Verlag, Berlin (1982).
    • (1982) Encyclopedia of Plant Physiology , vol.14 A , pp. 189-228
    • Davies, D.D.1
  • 45
  • 46
    • 0028464995 scopus 로고
    • Novel vascular cell-specific genes whose expression is regulated temporally and spatially during vascular system development
    • Demura T, Fukuda H: Novel vascular cell-specific genes whose expression is regulated temporally and spatially during vascular system development. Plant Cell 6: 967-981 (1994).
    • (1994) Plant Cell , vol.6 , pp. 967-981
    • Demura, T.1    Fukuda, H.2
  • 47
    • 0005868498 scopus 로고
    • Liver mitochondria contain an ATP-dependent vanadate-sensitive pathway for the degradation of proteins
    • Desautels M, Goldberg AL: Liver mitochondria contain an ATP-dependent vanadate-sensitive pathway for the degradation of proteins. Proc Natl Acad Sci USA 79: 18691873 (1982).
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1869-1873
    • Desautels, M.1    Goldberg, A.L.2
  • 48
  • 49
    • 0029619753 scopus 로고
    • Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26S protease subunit S5a
    • Deveraux Q, van Nocker S, Mahaffey D, Vierstra RD, Rechsteiner M: Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26S protease subunit S5a. J Biol Chem 270: 29660-29663 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 29660-29663
    • Deveraux, Q.1    Van Nocker, S.2    Mahaffey, D.3    Vierstra, R.D.4    Rechsteiner, M.5
  • 50
    • 0023545339 scopus 로고
    • Molular determinants of protein half-lives in eukaryotic cells
    • Dice JF: Molular determinants of protein half-lives in eukaryotic cells. FASEB J 1: 349-357 (1987).
    • (1987) FASEB J , vol.1 , pp. 349-357
    • Dice, J.F.1
  • 52
    • 0028213449 scopus 로고
    • Heat-inducible degron: A method for constructing temperature-sensitive mutants
    • Dohmen RJ, Wu P, Varshavsky A: Heat-inducible degron: a method for constructing temperature-sensitive mutants. Science 263: 1273-1276 (1994).
    • (1994) Science , vol.263 , pp. 1273-1276
    • Dohmen, R.J.1    Wu, P.2    Varshavsky, A.3
  • 54
    • 0028928658 scopus 로고
    • Ubiquitin in the prokaryote Anabaena variabilis
    • Durner J, Boger P: Ubiquitin in the prokaryote Anabaena variabilis. J Biol Chem 270: 3720-3725 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 3720-3725
    • Durner, J.1    Boger, P.2
  • 56
    • 0001523735 scopus 로고
    • Catalase degradation in sunflower cotyledons during peroxisome transition from glyoxysomal to leaf peroxisomal function
    • Eising R, Gerhardt B: Catalase degradation in sunflower cotyledons during peroxisome transition from glyoxysomal to leaf peroxisomal function. Plant Physiol 84: 225-232 (1987).
    • (1987) Plant Physiol , vol.84 , pp. 225-232
    • Eising, R.1    Gerhardt, B.2
  • 58
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL: Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268: 726-731 (1995).
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 59
    • 0000860075 scopus 로고
    • Molular and cellular biology associated with endosperm mobilization in germinating cereal grains
    • Fincher GB: Molular and cellular biology associated with endosperm mobilization in germinating cereal grains. Annu Rev Plant Physiol Plant Mol Biol 40: 305-346 (1989).
    • (1989) Annu Rev Plant Physiol Plant Mol Biol , vol.40 , pp. 305-346
    • Fincher, G.B.1
  • 60
    • 0024593537 scopus 로고
    • The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis
    • Finley D, Bartel B, Varshavsky A: The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis. Nature 338: 394-401 (1989).
    • (1989) Nature , vol.338 , pp. 394-401
    • Finley, D.1    Bartel, B.2    Varshavsky, A.3
  • 61
    • 0029147711 scopus 로고
    • Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli CIpP is a tetradecamer with an axial pore
    • Flannagan JM, Wall JS, Capel MS, Schneider DK, Shanklin JS: Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli CIpP is a tetradecamer with an axial pore. Biochemistry 34: 10910-10917 (1995).
    • (1995) Biochemistry , vol.34 , pp. 10910-10917
    • Flannagan, J.M.1    Wall, J.S.2    Capel, M.S.3    Schneider, D.K.4    Shanklin, J.S.5
  • 62
    • 0026932671 scopus 로고
    • Expression of stress-responsive ubiquitin genes in potato tubers
    • Garbarino JE, Rockhold DR, Belknap WR: Expression of stress-responsive ubiquitin genes in potato tubers. Plant Mol Biol 20: 235-244 (1992).
    • (1992) Plant Mol Biol , vol.20 , pp. 235-244
    • Garbarino, J.E.1    Rockhold, D.R.2    Belknap, W.R.3
  • 63
    • 0029614715 scopus 로고
    • Isolation of a polyubiquitin promoter and its expression in transgenic potato plants
    • Garbarino JE, Oosumi T, Belknap WR: Isolation of a polyubiquitin promoter and its expression in transgenic potato plants. Plant Physiol 109: 1371-1378 (1995).
    • (1995) Plant Physiol , vol.109 , pp. 1371-1378
    • Garbarino, J.E.1    Oosumi, T.2    Belknap, W.R.3
  • 64
    • 0027214605 scopus 로고
    • γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaszynska M, Rock KL, Goldberg AL: γ-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365: 264-267 (1993).
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaszynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 65
    • 0027953117 scopus 로고
    • Structural and functional aspects of chaperonin-mediated protein folding
    • Gatenby AA, Viitanen PV: Structural and functional aspects of chaperonin-mediated protein folding. Annu Rev Plant Physiol Plant Mol Biol 45: 469-491 (1994).
    • (1994) Annu Rev Plant Physiol Plant Mol Biol , vol.45 , pp. 469-491
    • Gatenby, A.A.1    Viitanen, P.V.2
  • 66
    • 0027021315 scopus 로고
    • Ubiquitin genes are differentially regulated in protoplast-derived cultures of Nicotiana sylvestris and in response to various stresses
    • Genschik P, Parmentier Y, Durr A, Marbach J, Criqui M-C, Jamet E, Fleck J: Ubiquitin genes are differentially regulated in protoplast-derived cultures of Nicotiana sylvestris and in response to various stresses. Plant Mol Biol 20: 897-910 (1992).
    • (1992) Plant Mol Biol , vol.20 , pp. 897-910
    • Genschik, P.1    Parmentier, Y.2    Durr, A.3    Marbach, J.4    Criqui, M.-C.5    Jamet, E.6    Fleck, J.7
  • 67
    • 0026658062 scopus 로고
    • Cloning and sequence analysis of a cDNA clone from Arabidopsis thaliana homologous to a proteasome α subunit from Drosophila
    • Genschik P, Philipps G, Gigot C, Heck J: Cloning and sequence analysis of a cDNA clone from Arabidopsis thaliana homologous to a proteasome α subunit from Drosophila. FEBS Lett 309: 311-315 (1992).
    • (1992) FEBS Lett , vol.309 , pp. 311-315
    • Genschik, P.1    Philipps, G.2    Gigot, C.3    Heck, J.4
  • 68
    • 0027991620 scopus 로고
    • Differential expression of several E2-type ubiquitin-carrier protein genes at different developmental stages of Arabidopsis thaliana and Nicotiana sylvestris
    • Genschik P, Durr A, Fleck J: Differential expression of several E2-type ubiquitin-carrier protein genes at different developmental stages of Arabidopsis thaliana and Nicotiana sylvestris. Mol Gen Genet 244: 548-556 (1994).
    • (1994) Mol Gen Genet , vol.244 , pp. 548-556
    • Genschik, P.1    Durr, A.2    Fleck, J.3
  • 69
    • 0028519157 scopus 로고
    • Molular characterization of a β-type proteasome subunit from Arabidopsis thaliana co-expressed at high level with an α-type proteasome subunit early in the cell cycle
    • Genschik P, Jamet E, Philipps, Parmentier Y, Gigot C, Fleck J: Molular characterization of a β-type proteasome subunit from Arabidopsis thaliana co-expressed at high level with an α-type proteasome subunit early in the cell cycle. Plant J 6: 537-546 (1994).
    • (1994) Plant J , vol.6 , pp. 537-546
    • Genschik, P.1    Jamet, E.2    Philipps3    Parmentier, Y.4    Gigot, C.5    Fleck, J.6
  • 70
    • 0027444947 scopus 로고
    • S. cerevisiae 26S proteasome mutants arrest cell division in G2/metaphase
    • Ghislain M, Udvardy A, Mann C: S. cerevisiae 26S proteasome mutants arrest cell division in G2/metaphase. Nature 366: 358-362 (1993).
    • (1993) Nature , vol.366 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 71
    • 0027388957 scopus 로고
    • A major ubiquitin conjugation system in wheat germ extracts involves a 15-kDa ubiquitin conjugating enzyme (E2) homologous to the yeast UBC4/UBC5 gene products
    • Girod P-A, Vierstra RD: A major ubiquitin conjugation system in wheat germ extracts involves a 15-kDa ubiquitin conjugating enzyme (E2) homologous to the yeast UBC4/UBC5 gene products. J Biol Chem 268: 955-960 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 955-960
    • Girod, P.-A.1    Vierstra, R.D.2
  • 72
    • 0027582362 scopus 로고
    • Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana
    • Girod P-A, Carpenter TB, van Nocker S, Sullivan ML, Vierstra RD: Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in yeast are encoded by a multigene family in Arabidopsis thaliana. Plant J 3: 545-552 (1993).
    • (1993) Plant J , vol.3 , pp. 545-552
    • Girod, P.-A.1    Carpenter, T.B.2    Van Nocker, S.3    Sullivan, M.L.4    Vierstra, R.D.5
  • 73
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzner M, Murray A, Kirschner MW: Cyclin is degraded by the ubiquitin pathway. Nature 349: 132-138 (1991).
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzner, M.1    Murray, A.2    Kirschner, M.W.3
  • 74
    • 0022344755 scopus 로고
    • Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes
    • Goff SA, Goldberg AL: Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes. Cell 41: 587-595 (1985).
    • (1985) Cell , vol.41 , pp. 587-595
    • Goff, S.A.1    Goldberg, A.L.2
  • 75
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg AL: The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur J Biochem 203: 9-23 (1992).
    • (1992) Eur J Biochem , vol.203 , pp. 9-23
    • Goldberg, A.L.1
  • 76
    • 0029071646 scopus 로고
    • Functions of the proteasome: The lysis at the end of the tunnel
    • Goldberg AL: Functions of the proteasome: the lysis at the end of the tunnel. Science 268: 522-523 (1995).
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 77
    • 0016908233 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells: Part 2
    • Goldberg AL, St John AC: Intracellular protein degradation in mammalian and bacterial cells: part 2. Annu Rev Biochem 45: 747-803 (1976).
    • (1976) Annu Rev Biochem , vol.45 , pp. 747-803
    • Goldberg, A.L.1    St John, A.C.2
  • 78
    • 0026764311 scopus 로고
    • Proteolysis, proteasomes and antigen presentation
    • Goldberg Al, Rock KL: Proteolysis, proteasomes and antigen presentation. Nature 357: 375-379 (1992).
    • (1992) Nature , vol.357 , pp. 375-379
    • Al, G.1    Rock, K.L.2
  • 80
    • 0027379925 scopus 로고
    • Defective mitosis due to a mutation in the gene for a fission yeast 26S proteasome subunit
    • Gordon C, McGirk D, Dillon P, Rosen C, Hastie ND: Defective mitosis due to a mutation in the gene for a fission yeast 26S proteasome subunit. Nature 366: 355-357 (1993).
    • (1993) Nature , vol.366 , pp. 355-357
    • Gordon, C.1    McGirk, D.2    Dillon, P.3    Rosen, C.4    Hastie, N.D.5
  • 81
    • 0029075876 scopus 로고
    • Redirecting the specificity of ubiquitination through modification of ubiquitin conjugating enzymes (E2s)
    • Gosink M, Vierstra RD: Redirecting the specificity of ubiquitination through modification of ubiquitin conjugating enzymes (E2s). Proc Natl Acad Sci USA 92: 9117-9121 (1995).
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9117-9121
    • Gosink, M.1    Vierstra, R.D.2
  • 83
    • 0027364289 scopus 로고
    • C1pX, an alternative subunit for the ATP-dependent C1p protease of Escherichia coli: Sequence and in vivo activities
    • Gottesman S, Clark WP, Crecy-Lagard VD, Maurizi MR: C1pX, an alternative subunit for the ATP-dependent C1p protease of Escherichia coli: sequence and in vivo activities. J Biol Chem 268: 22618-11626 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 22618-111626
    • Gottesman, S.1    Clark, W.P.2    Crecy-Lagard, V.D.3    Maurizi, M.R.4
  • 84
    • 0026952853 scopus 로고
    • Temporal and spatial expression of a thiolprotease gene during pea ovary senescence and its regulation by gibberellin
    • Granell A, Harris N, Pisabarro AG, Carbonell J: Temporal and spatial expression of a thiolprotease gene during pea ovary senescence and its regulation by gibberellin. Plant J 2: 907-915 (1992).
    • (1992) Plant J , vol.2 , pp. 907-915
    • Granell, A.1    Harris, N.2    Pisabarro, A.G.3    Carbonell, J.4
  • 85
    • 0027648727 scopus 로고
    • Arabidopsis mutants compromised for the control of cellular damage during pathogenesis and aging
    • Greenberg JT, Ausubel FM: Arabidopsis mutants compromised for the control of cellular damage during pathogenesis and aging. Plant J 4: 327-341 (1993).
    • (1993) Plant J , vol.4 , pp. 327-341
    • Greenberg, J.T.1    Ausubel, F.M.2
  • 86
    • 0025689449 scopus 로고
    • Nucleotide sequence of a wheat chloroplast gene encoding the proteolytic subunit of an ATP-dependent protease
    • Grey JC, Hird Sm, Dyer TA: Nucleotide sequence of a wheat chloroplast gene encoding the proteolytic subunit of an ATP-dependent protease. Plant Mol Biol 15: 947-950 (1990).
    • (1990) Plant Mol Biol , vol.15 , pp. 947-950
    • Grey, J.C.1    Hird, Sm.2    Dyer, T.A.3
  • 87
    • 0028895656 scopus 로고
    • Ubiquitin is attached to membranes of Bacuolvirus particles by a novel type of phospholipid anchor
    • Guarino LA, Smith G, Dong W: Ubiquitin is attached to membranes of Bacuolvirus particles by a novel type of phospholipid anchor. Cell (1995).
    • (1995) Cell
    • Guarino, L.A.1    Smith, G.2    Dong, W.3
  • 88
    • 0026530899 scopus 로고
    • A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains
    • Hadir T, Warms JVB, Rose IA, Hershko A: A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. J Biol Chem 267: 719-727 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 719-727
    • Hadir, T.1    Warms, J.V.B.2    Rose, I.A.3    Hershko, A.4
  • 89
    • 0000334676 scopus 로고
    • Ubiquitin-dependent proteolytic pathway in wheat germ: Isolation of multiple forms of ubiquitin-activating enzyme
    • Hatfield PM, Vierstra RD: Ubiquitin-dependent proteolytic pathway in wheat germ: Isolation of multiple forms of ubiquitin-activating enzyme. Biochemistry 28: 735-742 (1989).
    • (1989) Biochemistry , vol.28 , pp. 735-742
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 90
    • 0024995885 scopus 로고
    • Cloning of ubiquitin activating enzyme from wheat and expression of a functional protein in Escherichia coli
    • Hatfield PM, Callis J, Vierstra RD: Cloning of ubiquitin activating enzyme from wheat and expression of a functional protein in Escherichia coli. J Biol Chem 265: 15813-15817 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 15813-15817
    • Hatfield, P.M.1    Callis, J.2    Vierstra, R.D.3
  • 91
    • 0026769411 scopus 로고
    • Multiple forms of ubiquitin-activating enzyme (E1) from wheat: Identification of an essential cysteine by in vitro mutagenesis
    • Hatfield PM, Vierstra RD: Multiple forms of ubiquitin-activating enzyme (E1) from wheat: identification of an essential cysteine by in vitro mutagenesis. J Biol Chem 267: 14799-14803 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 14799-14803
    • Hatfield, P.M.1    Vierstra, R.D.2
  • 93
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked Ring10 gene, codes for a yeast proteasome unit necessary for chymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer W, Gruhler A, Möhrle V, Mahé Y, Wolf DH: PRE2, highly homologous to the human major histocompatibility complex-linked Ring10 gene, codes for a yeast proteasome unit necessary for chymotryptic activity and degradation of ubiquitinated proteins. J Biol Chem 268: 5115-5120 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Möhrle, V.3    Mahé, Y.4    Wolf, D.H.5
  • 94
    • 0027597690 scopus 로고
    • Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis
    • Hensel LL, Grbic V, Baumgarten DA, Bleecker AB: Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis. Plant Cell 5: 553-564 (1993).
    • (1993) Plant Cell , vol.5 , pp. 553-564
    • Hensel, L.L.1    Grbic, V.2    Baumgarten, D.A.3    Bleecker, A.B.4
  • 95
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A: The ubiquitin system for protein degradation. Annu Rev Biochem 61: 761-807 (1992).
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 96
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke L, Riezman H: Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84: 277-287 (1996).
    • (1996) Cell , vol.84 , pp. 277-287
    • Hicke, L.1    Riezman, H.2
  • 97
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M: Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Opin Cell Biol 7: 215-223 (1995).
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 98
    • 0027319328 scopus 로고
    • Anaphase is initiated by proteolysis rather than by inactivation of maturation-promoting factor
    • Holloway SL, Glotzer M, King RW, Murray AW: Anaphase is initiated by proteolysis rather than by inactivation of maturation-promoting factor. Cell 73: 1393-1402 (1993).
    • (1993) Cell , vol.73 , pp. 1393-1402
    • Holloway, S.L.1    Glotzer, M.2    King, R.W.3    Murray, A.W.4
  • 99
    • 0026828751 scopus 로고
    • Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions
    • Holwerda BC, Padgett HS, Rogers JC: Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell 4: 307-318 (1992).
    • (1992) Plant Cell , vol.4 , pp. 307-318
    • Holwerda, B.C.1    Padgett, H.S.2    Rogers, J.C.3
  • 100
    • 0026847823 scopus 로고
    • Novel applications of the ubiquitin-dependent proteolytic pathway in plant genetic engineering
    • Hondred D, Vierstra RD: Novel applications of the ubiquitin-dependent proteolytic pathway in plant genetic engineering. Curr Opin Biotechnol. 3: 147-151 (1992).
    • (1992) Curr Opin Biotechnol. , vol.3 , pp. 147-151
    • Hondred, D.1    Vierstra, R.D.2
  • 101
    • 0028303252 scopus 로고
    • Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines
    • Hou D, Cenciarelli D, Jensen JP, Nguyen HB, Weissman AM: Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines. J Biol Chem 269: 14244-14247 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 14244-14247
    • Hou, D.1    Cenciarelli, D.2    Jensen, J.P.3    Nguyen, H.B.4    Weissman, A.M.5
  • 102
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Huang Y, Baker RT, Fischer-Vize JA: Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science 270: 1828-1831 (1995).
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, R.T.2    Fischer-Vize, J.A.3
  • 103
    • 0000506727 scopus 로고
    • Protein turnover in plants and possible means of its regulation
    • Huffaker RC, Peterson LW: Protein turnover in plants and possible means of its regulation. Annu Rev Plant Physiol 25: 363-392 (1974).
    • (1974) Annu Rev Plant Physiol , vol.25 , pp. 363-392
    • Huffaker, R.C.1    Peterson, L.W.2
  • 104
    • 0028907874 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: A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 92: 2563-2567 (1995).
    • (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
  • 105
    • 0024978147 scopus 로고
    • Ubiquitin-phytochrome conjugates: Pool dynamics during in vivo phytochrome degradation
    • Jabben M, Shanklin J, Vierstra RD: Ubiquitin-phytochrome conjugates: pool dynamics during in vivo phytochrome degradation. J Biol Chem 264: 4998-5005 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 4998-5005
    • Jabben, M.1    Shanklin, J.2    Vierstra, R.D.3
  • 106
    • 0001719153 scopus 로고
    • Red light-induced accumulation of ubiquitin-phytochrome conjugates in both moncots and dicots
    • Jabben M, Shanklin J, Vierstra RD: Red light-induced accumulation of ubiquitin-phytochrome conjugates in both moncots and dicots. Plant Physiol 90: 380-384 (1989).
    • (1989) Plant Physiol , vol.90 , pp. 380-384
    • Jabben, M.1    Shanklin, J.2    Vierstra, R.D.3
  • 107
    • 0028273861 scopus 로고
    • Arabidopsis homeotic gene APETALA3 ectopic expression: Transcriptional and posttranscriptional regulation determine floral organ identity
    • Jack T, Fox GL, Meyerowitz EM: Arabidopsis homeotic gene APETALA3 ectopic expression: transcriptional and posttranscriptional regulation determine floral organ identity. Cell 76: 703-716 (1994).
    • (1994) Cell , vol.76 , pp. 703-716
    • Jack, T.1    Fox, G.L.2    Meyerowitz, E.M.3
  • 109
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch S: The ubiquitin-conjugation system. Annu Rev Genet 26: 179-207 (1992).
    • (1992) Annu Rev Genet , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 110
    • 0026089795 scopus 로고
    • A plastome mutation affects processing of both chloroplast and nuclear DNA-encoded plastid proteins
    • Johnson EM, Schnabeirauch LS, Sears BB: A plastome mutation affects processing of both chloroplast and nuclear DNA-encoded plastid proteins. Mol Gen Genet 225: 106-112 (1991).
    • (1991) Mol Gen Genet , vol.225 , pp. 106-112
    • Johnson, E.M.1    Schnabeirauch, L.S.2    Sears, B.B.3
  • 111
    • 0025345753 scopus 로고
    • Cis-trans recognition and subunit-specific degradation of short-lived proteins
    • Johnson ES, Gonda DK, Varshavsky A: Cis-trans recognition and subunit-specific degradation of short-lived proteins. Nature 346: 287-291 (1990).
    • (1990) Nature , vol.346 , pp. 287-291
    • Johnson, E.S.1    Gonda, D.K.2    Varshavsky, A.3
  • 112
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson ES, Ma PC, Ota IM, Varshavsky A: A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 270: 17442-17456 (1995).
    • (1995) J Biol Chem , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 113
    • 0025871691 scopus 로고
    • Three proteolytic systems in the yeast Saccharomyces cerevisiae
    • Jones EW: Three proteolytic systems in the yeast Saccharomyces cerevisiae. J Biol Chem 266: 7963-7966 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 7963-7966
    • Jones, E.W.1
  • 115
    • 0028317624 scopus 로고
    • Post-translational regulation of nitrate reductase in higher plants
    • Kaiser WM, Huber SC: Post-translational regulation of nitrate reductase in higher plants. Plant Physiol 106: 817-821 (1994).
    • (1994) Plant Physiol , vol.106 , pp. 817-821
    • Kaiser, W.M.1    Huber, S.C.2
  • 116
    • 0024278557 scopus 로고
    • Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro
    • Kassenbrock CK, Garcia PD, Walter P, Kelly RB: Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro. Nature 333: 90-93 (1988).
    • (1988) Nature , vol.333 , pp. 90-93
    • Kassenbrock, C.K.1    Garcia, P.D.2    Walter, P.3    Kelly, R.B.4
  • 117
    • 0030024281 scopus 로고    scopus 로고
    • Role of peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler KC, Waller PRH, Sauer RT: Role of peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993 (1996).
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 119
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli C1pAP protease and the eukaryotic 26S proteasome
    • Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh K, Steven AC: Homology in structural organization between E. coli C1pAP protease and the eukaryotic 26S proteasome. J Mol Biol 250: 587-594 (1995).
    • (1995) J Mol Biol , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Kocsis, E.4    Trus, B.L.5    Singh, K.6    Steven, A.C.7
  • 120
    • 0001048545 scopus 로고
    • Turnover of 1-aminocyclopropane-1-carboxylic acid synthase protein in wounded tomato fruit tissue
    • Kim WT, Yang SF: Turnover of 1-aminocyclopropane-1-carboxylic acid synthase protein in wounded tomato fruit tissue. Plant Physiol. 100: 1126-1131 (1992).
    • (1992) Plant Physiol. , vol.100 , pp. 1126-1131
    • Kim, W.T.1    Yang, S.F.2
  • 121
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B
    • King RW, Peters J-M, Tugendreich S, Rolfe M, Hieter P, Kirschner MW: A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B. Cell 81: 279-288 (1995).
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W.1    Peters, J.-M.2    Tugendreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.W.6
  • 122
    • 0027369993 scopus 로고
    • Characterization of cDNA for a dehydration-inducible gene that encodes a C1pA, B-like protein in Arabidopsis thaliana L
    • Kiyosue T, Yamaguchi-Shinozaki K, Shinozaki K: Characterization of cDNA for a dehydration-inducible gene that encodes a C1pA, B-like protein in Arabidopsis thaliana L. Biochem Biophys Res Commun 196: 1214-1220 (1993).
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 1214-1220
    • Kiyosue, T.1    Yamaguchi-Shinozaki, K.2    Shinozaki, K.3
  • 123
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner RD, Sitia R: Protein degradation in the endoplasmic reticulum. Cell 62: 611-614 (1990).
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 124
    • 0025465440 scopus 로고
    • Hormonal regulation, processing and secretion of cysteine proteinases in barley aleurone layers
    • Koehler SM, Ho T-HD: Hormonal regulation, processing and secretion of cysteine proteinases in barley aleurone layers. Plant Cell 2: 769-783 (1990).
    • (1990) Plant Cell , vol.2 , pp. 769-783
    • Koehler, S.M.1    Ho, T.-H.D.2
  • 125
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gcn4
    • Kornitzer D, Raboy B, Kulka RG, Fink GR: Regulated degradation of the transcription factor Gcn4. EMBO J 13: 6021-6030 (1994).
    • (1994) EMBO J , vol.13 , pp. 6021-6030
    • Kornitzer, D.1    Raboy, B.2    Kulka, R.G.3    Fink, G.R.4
  • 126
    • 0026610823 scopus 로고
    • Characterization of a prolyl endopeptidase from spinach thylakoids
    • Kuwabara T: Characterization of a prolyl endopeptidase from spinach thylakoids. FEBS Lett 300: 127-130 (1992).
    • (1992) FEBS Lett , vol.300 , pp. 127-130
    • Kuwabara, T.1
  • 127
    • 0030021004 scopus 로고    scopus 로고
    • Induction and regulation of heat-shock gene expression by an amino acid analog in soybean seedlings
    • Lee Y-R, Nagao RT, Lin C-Y, Key JL: Induction and regulation of heat-shock gene expression by an amino acid analog in soybean seedlings. Plant Physiol 110: 241-248 (1996).
    • (1996) Plant Physiol , vol.110 , pp. 241-248
    • Lee, Y.-R.1    Nagao, R.T.2    Lin, C.-Y.3    Key, J.L.4
  • 128
    • 0027165626 scopus 로고
    • Arabidopsis auxin resistance gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1
    • Leyser HMO, Lincoln CA, Timpte C, Lammer D, Turner J, Estelle M: Arabidopsis auxin resistance gene AXR1 encodes a protein related to ubiquitin-activating enzyme E1. Nature 364: 161-164 (1993).
    • (1993) Nature , vol.364 , pp. 161-164
    • Leyser, H.M.O.1    Lincoln, C.A.2    Timpte, C.3    Lammer, D.4    Turner, J.5    Estelle, M.6
  • 129
    • 0027296517 scopus 로고
    • Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation
    • Lin W-C, Desiderio S: Regulation of V(D)J recombination activator protein RAG-2 by phosphorylation. Science 260: 953-958 (1993).
    • (1993) Science , vol.260 , pp. 953-958
    • Lin, W.-C.1    Desiderio, S.2
  • 130
    • 48749135011 scopus 로고
    • ATP-dependent proteolysis in pea chloroplasts
    • Liu X-Q, Jagendorf AT: ATP-dependent proteolysis in pea chloroplasts. FEBS Lett 166: 248-252 (1984).
    • (1984) FEBS Lett , vol.166 , pp. 248-252
    • Liu, X.-Q.1    Jagendorf, A.T.2
  • 131
    • 0000164781 scopus 로고
    • Neutral peptidases in the stroma of pea chloroplasts
    • Liu X-Q, Jagendorf AT: Neutral peptidases in the stroma of pea chloroplasts. Plant Physiol 81: 603-608 (1986)
    • (1986) Plant Physiol , vol.81 , pp. 603-608
    • Liu, X.-Q.1    Jagendorf, A.T.2
  • 132
    • 0026722530 scopus 로고
    • The interferon-inducible 15 kDa ubiquitin homolog conjugates to intracellular proteins
    • Loeb KR, Haas AL: The interferon-inducible 15 kDa ubiquitin homolog conjugates to intracellular proteins. J Biol Chem 267: 7806-7813 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 7806-7813
    • Loeb, K.R.1    Haas, A.L.2
  • 133
    • 0028134248 scopus 로고
    • Molular analysis of natural leaf senescence in Arabidopsis thaliana
    • Lohman KN, Gan S, John MC, Amasino RM: Molular analysis of natural leaf senescence in Arabidopsis thaliana. Physiol Plant 92: 322-328 (1994).
    • (1994) Physiol Plant , vol.92 , pp. 322-328
    • Lohman, K.N.1    Gan, S.2    John, M.C.3    Amasino, R.M.4
  • 134
    • 0030070190 scopus 로고    scopus 로고
    • A member of the KNOTTED class of homeodomain proteins encoded by the STM gene of Arabidopsis
    • Long JA, Moan EI, Medford JI, MK Barton: A member of the KNOTTED class of homeodomain proteins encoded by the STM gene of Arabidopsis. Nature 379: 66-69 (1996).
    • (1996) Nature , vol.379 , pp. 66-69
    • Long, J.A.1    Moan, E.I.2    Medford, J.I.3    Barton, M.K.4
  • 135
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe J, Stock D, Jap F, Zwickl P, Baumeister W, Huber R: Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268: 533-539 (1995).
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, F.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 136
    • 0028169361 scopus 로고
    • Degradation of Gα by the N-End Rule pathway
    • Madura K, Varshavsky A: Degradation of Gα by the N-End Rule pathway. Science 265: 1454-1458 (1994).
    • (1994) Science , vol.265 , pp. 1454-1458
    • Madura, K.1    Varshavsky, A.2
  • 137
    • 0001040455 scopus 로고
    • Newly synthesized proteins are degraded by an ATP-stimulated proteolytic process in isolated pea chloroplasts
    • Malek L, Bogorad L, Ayers AR, Goldberg AL: Newly synthesized proteins are degraded by an ATP-stimulated proteolytic process in isolated pea chloroplasts. FEBS Lett 166: 253-257 (1984).
    • (1984) FEBS Lett , vol.166 , pp. 253-257
    • Malek, L.1    Bogorad, L.2    Ayers, A.R.3    Goldberg, A.L.4
  • 138
    • 0028000093 scopus 로고
    • Genetic and molecular analysis of hyperplastic discs, a gene whose product is required for regulation of cell proliferation in Drosophila melanogaster imaginal discs and germ cells
    • Mansfield, E, Hersperger E, Biggs J, Shearn A: Genetic and molecular analysis of hyperplastic discs, a gene whose product is required for regulation of cell proliferation in Drosophila melanogaster imaginal discs and germ cells. Devel Biol 165: 507-526 (1994).
    • (1994) Devel Biol , vol.165 , pp. 507-526
    • Mansfield, E.1    Hersperger, E.2    Biggs, J.3    Shearn, A.4
  • 139
    • 0003004669 scopus 로고
    • Protein degradation
    • Coulter D, Partier B (eds) New Series, Springer-Verlag, Berlin
    • Matile PH: Protein degradation. In: Coulter D, Partier B (eds) Encyclopedia of Plant Physiology, New Series, Vol. 14A, pp. 169-188, Springer-Verlag, Berlin (1982).
    • (1982) Encyclopedia of Plant Physiology , vol.14 A , pp. 169-188
    • Matile, P.H.1
  • 140
    • 0001294420 scopus 로고
    • Regulation of protein metabolism; coupling of photosynthetic electron transport to the in vivo degradation of the rapidly metabolized 32-kilodalton protein in the chloroplast membranes
    • Mattoo AK, Hoffman-Falk H, Marder JB, Edelman M: Regulation of protein metabolism; coupling of photosynthetic electron transport to the in vivo degradation of the rapidly metabolized 32-kilodalton protein in the chloroplast membranes. Proc Natl Acad Sci USA 81: 1380-1384 (1984).
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1380-1384
    • Mattoo, A.K.1    Hoffman-Falk, H.2    Marder, J.B.3    Edelman, M.4
  • 141
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3 glucanase in bean leaves
    • Mauch F, Staehelin LA: Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3 glucanase in bean leaves. Plant Cell 1: 447-457 (1989).
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, L.A.2
  • 142
    • 0025323156 scopus 로고
    • C1pP represents a unique family of serine proteases
    • Maurizi MR, Clark WP, Kim SH, Gottesman S: C1pP represents a unique family of serine proteases. J Biol Chem 265: 12456-12552 (1990).
    • (1990) J Biol Chem , vol.265 , pp. 12456-12552
    • Maurizi, M.R.1    Clark, W.P.2    Kim, S.H.3    Gottesman, S.4
  • 143
    • 0026601663 scopus 로고
    • Protease and protein degradation in Escherichia coli
    • Maurizi MR: Protease and protein degradation in Escherichia coli. Experientia 48: 178-201 (1992).
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 144
    • 0025967290 scopus 로고
    • UBA1: An essential yeast gene encoding-ubiquitin-activating enzyme
    • McGrath JP, Jentsch S, Varshavsky A: UBA1: an essential yeast gene encoding-ubiquitin-activating enzyme. EMBO J 10: 227-236 (1991).
    • (1991) EMBO J , vol.10 , pp. 227-236
    • McGrath, J.P.1    Jentsch, S.2    Varshavsky, A.3
  • 145
    • 0022972973 scopus 로고
    • Rapid degradation of apoplastocyanin in Cu(II)-deficient cells of Chlamydomonas reinhardtii
    • Merchant S, Bogorad L: Rapid degradation of apoplastocyanin in Cu(II)-deficient cells of Chlamydomonas reinhardtii. J Biol Chem 261: 15850-15853 (1986).
    • (1986) J Biol Chem , vol.261 , pp. 15850-15853
    • Merchant, S.1    Bogorad, L.2
  • 146
    • 0028891682 scopus 로고
    • In situ detection of nDNA fragmentation during the differentiation of trachery elements in higher plants
    • Mittler R, Lam E: In situ detection of nDNA fragmentation during the differentiation of trachery elements in higher plants. Plant Physiol. 108: 489-493 (1995).
    • (1995) Plant Physiol. , vol.108 , pp. 489-493
    • Mittler, R.1    Lam, E.2
  • 147
    • 0027550578 scopus 로고
    • Characterization of a cDNA clone encoding a chloroplast-targeted C1p homologue
    • Moore T, Keegstra K: Characterization of a cDNA clone encoding a chloroplast-targeted C1p homologue. Plant Mol Biol 21: 525-537 (1993).
    • (1993) Plant Mol Biol , vol.21 , pp. 525-537
    • Moore, T.1    Keegstra, K.2
  • 148
    • 0029614380 scopus 로고
    • Examination of the contribution of vacuolar proteases to intracellular protein degradation in Chara corallina
    • Moriyasu Y: Examination of the contribution of vacuolar proteases to intracellular protein degradation in Chara corallina. Plant Physiol 109: 1309-1315 (1995).
    • (1995) Plant Physiol , vol.109 , pp. 1309-1315
    • Moriyasu, Y.1
  • 149
    • 0025284693 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 ad D1 by increasing apoprotein stability
    • Mullet JE, Gamble-Klein, Klein RR: Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 ad D1 by increasing apoprotein stability. Proc Natl Acad Sci USA 87: 4038-4042 (1990).
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4038-4042
    • Mullet, J.E.1    Gamble-Klein2    Klein, R.R.3
  • 151
    • 0027185303 scopus 로고
    • The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes
    • Muralidhar MG, Thomas JB: The Drosophila bendless gene encodes a neural protein related to ubiquitin-conjugating enzymes. Neuron 11: 253-266 (1993).
    • (1993) Neuron , vol.11 , pp. 253-266
    • Muralidhar, M.G.1    Thomas, J.B.2
  • 152
    • 0029051233 scopus 로고
    • Cyclin ubiquitination: The destructive end of mitosis
    • Murray A: Cyclin ubiquitination: the destructive end of mitosis. Cell 81: 149-152 (1995).
    • (1995) Cell , vol.81 , pp. 149-152
    • Murray, A.1
  • 154
    • 0029294012 scopus 로고
    • Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion
    • Nussaume L, Vincentz M, Meyer C, Boutin J-P, Caboche M: Post-transcriptional regulation of nitrate reductase by light is abolished by an N-terminal deletion. Plant Cell 7: 611-621 (1995).
    • (1995) Plant Cell , vol.7 , pp. 611-621
    • Nussaume, L.1    Vincentz, M.2    Meyer, C.3    Boutin, J.-P.4    Caboche, M.5
  • 155
    • 0026495086 scopus 로고
    • Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast
    • Oblong JE, Lamppa GK: Identification of two structurally related proteins involved in proteolytic processing of precursors targeted to the chloroplast. EMBO J 11: 4401-4409 (1992).
    • (1992) EMBO J , vol.11 , pp. 4401-4409
    • Oblong, J.E.1    Lamppa, G.K.2
  • 156
    • 0026794712 scopus 로고
    • Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea
    • Ozaki M, Fujinami K, Tanaka D, Amemiya Y, Sato T, Ogura N, Nakagawa H: Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea. J Biol Chem 267: 21678-21684 (1992).
    • (1992) J Biol Chem , vol.267 , pp. 21678-21684
    • Ozaki, M.1    Fujinami, K.2    Tanaka, D.3    Amemiya, Y.4    Sato, T.5    Ogura, N.6    Nakagawa, H.7
  • 158
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palmobella VJ, Rando OJ, Goldberg AL, Maniatis T: The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78: 773-785 (1994).
    • (1994) Cell , vol.78 , pp. 773-785
    • Palmobella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 159
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to the product of the human tre-2 oncogene
    • Papa FR, Hochstrasser M: The yeast DOA4 gene encodes a deubiquitinating enzyme related to the product of the human tre-2 oncogene. Nature 366: 313-319 (1993).
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 160
    • 0025886794 scopus 로고
    • A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins
    • Pearce G, Strydom D, Johnson S, Ryan CA: A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins. Science 253: 895-898 (1991).
    • (1991) Science , vol.253 , pp. 895-898
    • Pearce, G.1    Strydom, D.2    Johnson, S.3    Ryan, C.A.4
  • 161
    • 0027414074 scopus 로고
    • The multicatalytic and 26S proteases
    • Rechsteiner M, Hoffman L, Dubiel W: The multicatalytic and 26S proteases. J Biol Chem 268: 6065-6068 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 6065-6068
    • Rechsteiner, M.1    Hoffman, L.2    Dubiel, W.3
  • 163
    • 0029310466 scopus 로고
    • A nodule-specific gene encoding a subtilisin-like protease is expressed in early stages of actinorhizal nodule development
    • Ribeiro A, Akkermans AD, van Kammen A, Bisseling T, Pawlowski K: A nodule-specific gene encoding a subtilisin-like protease is expressed in early stages of actinorhizal nodule development. Plant Cell 7: 785-794 (1995).
    • (1995) Plant Cell , vol.7 , pp. 785-794
    • Ribeiro, A.1    Akkermans, A.D.2    Van Kammen, A.3    Bisseling, T.4    Pawlowski, K.5
  • 164
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett AJ: Proteasomes: multicatalytic proteinase complexes. Biochem J 291: 1-10 (1993).
    • (1993) Biochem J , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 165
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL: Inhibitors of the proteasome block degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78: 761-771 (1994).
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 166
    • 0001329109 scopus 로고
    • Proteolytic enzymes and their inhibitors in plants
    • Ryan CA: Proteolytic enzymes and their inhibitors in plants. Annu Rev Plant Physiol 24: 173-196 (1973).
    • (1973) Annu Rev Plant Physiol , vol.24 , pp. 173-196
    • Ryan, C.A.1
  • 167
    • 0027987123 scopus 로고
    • Identification of a 50 kDa systemin-binding protein in tomato plasma membranes having Kex2-like properties
    • Schaller A, Ryan CA: Identification of a 50 kDa systemin-binding protein in tomato plasma membranes having Kex2-like properties. Proc Natl Acad Sci USA 91: 11802-11806 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11802-11806
    • Schaller, A.1    Ryan, C.A.2
  • 168
    • 0029411655 scopus 로고
    • Induction of wound response genes in tomato leaves by bestatin, an inhibitor of amino peptidases
    • Schaller A, Bergey DR, Ryan CE: Induction of wound response genes in tomato leaves by bestatin, an inhibitor of amino peptidases. Plant Cell 7: 1893-1898 (1995).
    • (1995) Plant Cell , vol.7 , pp. 1893-1898
    • Schaller, A.1    Bergey, D.R.2    Ryan, C.E.3
  • 169
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in ubiquitination of p53
    • Scheffner M, Huibregtse JM, Vierstra RD, Howley PM: The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in ubiquitination of p53. Cell 75: 495-505 (1993).
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 170
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin-thioester cascade
    • Scheffner M, Nuber U, Hulbregtse JM: Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin-thioester cascade. Nature 363: 81-83 (1995).
    • (1995) Nature , vol.363 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Hulbregtse, J.M.3
  • 172
    • 18844480151 scopus 로고
    • Rapid degradation of unassembled ribulose 1,5-bisphosphate carboxylase small subunit in chloroplasts
    • Schmidt GW, Mishkind ML: Rapid degradation of unassembled ribulose 1,5-bisphosphate carboxylase small subunit in chloroplasts. Proc Natl Acad Sci USA 80: 2632-2636 (1983).
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2632-2636
    • Schmidt, G.W.1    Mishkind, M.L.2
  • 174
    • 0021354885 scopus 로고
    • Role of protein degradation in the regulation of cellular protein content and amino acid pools
    • Scornik OA: Role of protein degradation in the regulation of cellular protein content and amino acid pools. FASEB J 43: 1283-1288 (1984).
    • (1984) FASEB J , vol.43 , pp. 1283-1288
    • Scornik, O.A.1
  • 176
    • 0026708316 scopus 로고
    • In vivo function of the proteasome in the ubiquitin pathway
    • Seufert W, Jentsch S: In vivo function of the proteasome in the ubiquitin pathway. EMBO J 11: 3077-3080 (1992).
    • (1992) EMBO J , vol.11 , pp. 3077-3080
    • Seufert, W.1    Jentsch, S.2
  • 177
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- And M-phase cyclins
    • Seufert W, Futcher B, Jentsch S: Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 373: 78-81 (1995).
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 178
    • 0023154514 scopus 로고
    • Red light-induced formation of ubiquitin-phytochrome conjugates: Identification of possible intermediates of phytochrome degradation
    • Shanklin J, Jabben M, Vierstra RD: Red light-induced formation of ubiquitin-phytochrome conjugates: identification of possible intermediates of phytochrome degradation. Proc Natl Acad Sci USA 84: 359-363 (1987).
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 359-363
    • Shanklin, J.1    Jabben, M.2    Vierstra, R.D.3
  • 179
    • 0039932366 scopus 로고
    • Partial purification and peptide mapping of ubiquitin-phytochrome conjugates from oat
    • Shanklin J, Jabben M, Vierstra RD: Partial purification and peptide mapping of ubiquitin-phytochrome conjugates from oat. Biochemistry 28: 6028-6034 (1989).
    • (1989) Biochemistry , vol.28 , pp. 6028-6034
    • Shanklin, J.1    Jabben, M.2    Vierstra, R.D.3
  • 180
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain C1pP and C1pC, functional homologues of Escherichia coli C1pP and C1pA: An archetypal two component ATP-dependent protease
    • Shanklin J, DeWitt ND, Flanagan JM: The stroma of higher plant plastids contain C1pP and C1pC, functional homologues of Escherichia coli C1pP and C1pA: an archetypal two component ATP-dependent protease. Plant Cell 7: 1713-1722 (1995).
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3
  • 181
    • 0027136759 scopus 로고
    • An Arabidopsis gene homolgous to mammalian and insect genes encoding the largest proteasome subunit
    • Shirley BW, Goodman HM: An Arabidopsis gene homolgous to mammalian and insect genes encoding the largest proteasome subunit. Mol Gen Genet 241: 586-594 (1993).
    • (1993) Mol Gen Genet , vol.241 , pp. 586-594
    • Shirley, B.W.1    Goodman, H.M.2
  • 182
    • 0026513218 scopus 로고
    • Tsp: A tail-specific protease that selectively degrades proteins with non-polar C-termini
    • Silber KR, Keiler KC, Sauer RT: Tsp: a tail-specific protease that selectively degrades proteins with non-polar C-termini. Proc Natl Acad Sci USA 89: 295-299 (1992).
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 295-299
    • Silber, K.R.1    Keiler, K.C.2    Sauer, R.T.3
  • 183
    • 0028115642 scopus 로고
    • The apparent turnover of 1-aminocyclopropane-1-carboxylate synthase in tomato cells is regulated by protein phosphorylation and dephosphorylation
    • Spanu P, Grosskopf DG, Felix G, Boller T: The apparent turnover of 1-aminocyclopropane-1-carboxylate synthase in tomato cells is regulated by protein phosphorylation and dephosphorylation. Plant Physiol 106: 529-535 (1994).
    • (1994) Plant Physiol , vol.106 , pp. 529-535
    • Spanu, P.1    Grosskopf, D.G.2    Felix, G.3    Boller, T.4
  • 184
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
    • Spence J, Sadis S, Haas AL, Finley D: A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 15: 1265-1273 (1995).
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 186
    • 0028501449 scopus 로고
    • An Arabidopsis peptide transporter is a member of a new class of membrane transport proteins
    • Steiner H-Y, Song W, Zhang L, Naider F, Becker JM, Stacey G: An Arabidopsis peptide transporter is a member of a new class of membrane transport proteins. Plant Cell 6: 1289-1299 (1994).
    • (1994) Plant Cell , vol.6 , pp. 1289-1299
    • Steiner, H.-Y.1    Song, W.2    Zhang, L.3    Naider, F.4    Becker, J.M.5    Stacey, G.6
  • 187
    • 0024807033 scopus 로고
    • A ubiquitin carrier protein from wheat germ is structurally and functionally similar to the yeast DNA repair enzyme encoded by RAD6
    • Sullivan ML, Vierstra RD: A ubiquitin carrier protein from wheat germ is structurally and functionally similar to the yeast DNA repair enzyme encoded by RAD6. Proc Natl Acad Sci USA 86: 9861-9865 (1989).
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9861-9865
    • Sullivan, M.L.1    Vierstra, R.D.2
  • 188
    • 0006418264 scopus 로고
    • HPLC resolution of ubiquitin pathway from wheat germ
    • Sullivan ML, Callis J, Vierstra RD: HPLC resolution of ubiquitin pathway from wheat germ. Plant Physiol 94: 710-716 (1990).
    • (1990) Plant Physiol , vol.94 , pp. 710-716
    • Sullivan, M.L.1    Callis, J.2    Vierstra, R.D.3
  • 189
    • 0026325730 scopus 로고
    • Cloning of a 16 kDa ubiquitin carrier protein (E2) from wheat and Arabidopsis thaliana: Identification of functional domains by in vitro mutagenesis
    • Sullivan ML, Vierstra RD: Cloning of a 16 kDa ubiquitin carrier protein (E2) from wheat and Arabidopsis thaliana: identification of functional domains by in vitro mutagenesis. J Biol Chem 266: 23878-23885 (1991).
    • (1991) J Biol Chem , vol.266 , pp. 23878-23885
    • Sullivan, M.L.1    Vierstra, R.D.2
  • 190
    • 0028370795 scopus 로고
    • Homologues of wheat ubiquitin-conjugating enzymes TaUBC1 and roUBC4 are encoded by small multigene families in Arabidopsis thaliana
    • Sullivan ML, Carpenter T, Vierstra RD: Homologues of wheat ubiquitin-conjugating enzymes TaUBC1 and roUBC4 are encoded by small multigene families in Arabidopsis thaliana. Plant Mol Biol 24: 651-661 (1994).
    • (1994) Plant Mol Biol , vol.24 , pp. 651-661
    • Sullivan, M.L.1    Carpenter, T.2    Vierstra, R.D.3
  • 191
    • 0023991920 scopus 로고
    • The genomic organization and transcription of the ubiquitin genes of Trypanosoma cruzi
    • Swindle J, Ajioka J, Eisen H, Sanwal B, Jacquemot C, Browder Z, Buck G: The genomic organization and transcription of the ubiquitin genes of Trypanosoma cruzi. EMBO J 7: 1121-1127 (1988).
    • (1988) EMBO J , vol.7 , pp. 1121-1127
    • Swindle, J.1    Ajioka, J.2    Eisen, H.3    Sanwal, B.4    Jacquemot, C.5    Browder, Z.6    Buck, G.7
  • 194
    • 0024459376 scopus 로고
    • Lysosomal (Vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival
    • Teichert U, Mechlers B, Müller H, Wolf DH: Lysosomal (Vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. J Biol Chem 264: 16037-16045 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 16037-16045
    • Teichert, U.1    Mechlers, B.2    Müller, H.3    Wolf, D.H.4
  • 195
    • 26844577005 scopus 로고
    • Members of gene families encoding the ubiquitin-conjugating enzymes, AtUBC1-3 and AtUBC4-6, from Arabidopsis are differentially expressed
    • in press
    • Thoma S, Sullivan ML, Vierstra RD: Members of gene families encoding the ubiquitin-conjugating enzymes, AtUBC1-3 and AtUBC4-6, from Arabidopsis are differentially expressed. Plant Mol Biol, in press (1986).
    • (1986) Plant Mol Biol
    • Thoma, S.1    Sullivan, M.L.2    Vierstra, R.D.3
  • 198
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB that is still bound to NF-κB
    • Traenckner EB-M, Wilk S, Baeuerle PA: A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB that is still bound to NF-κB. EMBO J 13: 5433-5441 (1994).
    • (1994) EMBO J , vol.13 , pp. 5433-5441
    • Traenckner, E.B.-M.1    Wilk, S.2    Baeuerle, P.A.3
  • 199
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain
    • Treier M, Staszewski LM, Bohmann D: Ubiquitin-dependent c-jun degradation in vivo is mediated by the δ domain. Cell 78: 787-798 (1994).
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 200
    • 0025889016 scopus 로고
    • Cloning and characterization of a 20-kilodalton ubiquitin-carrier protein (E2) from wheat that catalyzes multi ubiquitin-chain formation in vitro
    • van Nocker S, Vierstra RD: Cloning and characterization of a 20-kilodalton ubiquitin-carrier protein (E2) from wheat that catalyzes multi ubiquitin-chain formation in vitro. Proc Natl Acad Sci USA 88: 10297-10301 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10297-10301
    • Van Nocker, S.1    Vierstra, R.D.2
  • 201
    • 0027428769 scopus 로고
    • Multiubiquitin chains linked through lysine-48 are abundant in vivo and competent inter-mediates in the ubiquitin-dependent proteolytic pathway
    • van Nocker S, Vierstra RD: Multiubiquitin chains linked through lysine-48 are abundant in vivo and competent inter-mediates in the ubiquitin-dependent proteolytic pathway. J Biol Chem 268: 24766-24773 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 24766-24773
    • Van Nocker, S.1    Vierstra, R.D.2
  • 202
    • 0030033982 scopus 로고    scopus 로고
    • Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome
    • van Nocker S, Deveraux Q, Rechsteiner M, Vierstra RD: Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc Natl Acad Sci USA 93: 856-860 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 856-860
    • Van Nocker, S.1    Deveraux, Q.2    Rechsteiner, M.3    Vierstra, R.D.4
  • 203
    • 26844498898 scopus 로고    scopus 로고
    • A multigene family in Arabidopsis thaliana encodes constitutively expressed E2s capable of forming multiubiquitin chains in vitro
    • in press
    • van Nocker S, Walker JM, Vierstra RD: A multigene family in Arabidopsis thaliana encodes constitutively expressed E2s capable of forming multiubiquitin chains in vitro. J Biol Chem, in press (1996).
    • (1996) J Biol Chem
    • Van Nocker, S.1    Walker, J.M.2    Vierstra, R.D.3
  • 204
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin chain-binding MCB1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential substrate-specific role in protein turnover
    • In press
    • van Nocker S, Saddis S, Rubin D, Glickman M, Fu H, Coux O, Wefes I, Finley D, Vierstra RD: The multiubiquitin chain-binding MCB1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential substrate-specific role in protein turnover. Mol Cell Biol, In press (1996).
    • (1996) Mol Cell Biol
    • Van Nocker, S.1    Saddis, S.2    Rubin, D.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 205
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky A: The N-end rule. Cell 69: 725-735 (1992).
    • (1992) Cell , vol.69 , pp. 725-735
    • Varshavsky, A.1
  • 206
    • 0010581992 scopus 로고
    • Demonstration of ATP-dependent, ubiquitin conjugating activities in higher plants
    • Vierstra RD: Demonstration of ATP-dependent, ubiquitin conjugating activities in higher plants. Plant Physiol 84: 332-336 (1987).
    • (1987) Plant Physiol , vol.84 , pp. 332-336
    • Vierstra, R.D.1
  • 208
    • 0001906410 scopus 로고
    • Phytochrome degradation
    • Kendrick RE, Kronenberg GHM (eds.) Martinus Nijhoff, Dordrecht, Netherlands
    • Vierstra RD: Phytochrome degradation. In: Kendrick RE, Kronenberg GHM (eds.) Photomorphogenesis in Plants, pp. 141-162. Martinus Nijhoff, Dordrecht, Netherlands (1994).
    • (1994) Photomorphogenesis in Plants , pp. 141-162
    • Vierstra, R.D.1
  • 209
    • 0022385458 scopus 로고
    • Purification and initial characterization of ubiquitin from the higher plant, Avena sativa
    • Vierstra RD, Langan SM, Haas AL: Purification and initial characterization of ubiquitin from the higher plant, Avena sativa. J Biol Chem 260:12015-12021 (1985).
    • (1985) J Biol Chem , vol.260 , pp. 12015-12021
    • Vierstra, R.D.1    Langan, S.M.2    Haas, A.L.3
  • 211
    • 0026782393 scopus 로고
    • The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes
    • Weibel FF, Kunau WH: The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes. Nature 359: 73-76 (1992).
    • (1992) Nature , vol.359 , pp. 73-76
    • Weibel, F.F.1    Kunau, W.H.2
  • 212
    • 0029007115 scopus 로고
    • From the cradle to the grave: Ring complexes in the life of a protein
    • Weissman JS, Sigler PB, Horwich AL: From the cradle to the grave: ring complexes in the life of a protein. Science 268: 523-524 (1995).
    • (1995) Science , vol.268 , pp. 523-524
    • Weissman, J.S.1    Sigler, P.B.2    Horwich, A.L.3
  • 213
    • 0028070376 scopus 로고
    • Existence of a molecular ruler in proteasomes suggested by analysis of degradation products
    • Wensel T, Eckerskorn C, Lottspeich F, Baumeister W: Existence of a molecular ruler in proteasomes suggested by analysis of degradation products. FEBS Lett 349: 205-209 (1994).
    • (1994) FEBS Lett , vol.349 , pp. 205-209
    • Wensel, T.1    Eckerskorn, C.2    Lottspeich, F.3    Baumeister, W.4
  • 216
    • 0002150829 scopus 로고
    • Role of proteolytic enzymes in the mobilization of protein reserves in the germinating dicot seed
    • Dalling MJ (ed) CRC Press, Boca Raton, FL
    • Wilson KA: Role of proteolytic enzymes in the mobilization of protein reserves in the germinating dicot seed. In: Dalling MJ (ed) Plant Proteolytic Enzymes, pp. 19-48. CRC Press, Boca Raton, FL (1986).
    • (1986) Plant Proteolytic Enzymes , pp. 19-48
    • Wilson, K.A.1
  • 217
    • 0027213027 scopus 로고
    • Ubiquitin found in the archaebacteria Thermoplasma acidophilum
    • Wolf S, Lottspeich F, Baumeister W: Ubiquitin found in the archaebacteria Thermoplasma acidophilum. FEBS Lett 326: 42-44 (1993).
    • (1993) FEBS Lett , vol.326 , pp. 42-44
    • Wolf, S.1    Lottspeich, F.2    Baumeister, W.3
  • 219
    • 0028587825 scopus 로고
    • Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a larger precursor
    • Yamagata H, Masuzawa T, Nagaoka Y, Ohnishi T, Iwasaki T: Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a larger precursor. J Biol Chem 169: 32725-32731 (1994).
    • (1994) J Biol Chem , vol.169 , pp. 32725-32731
    • Yamagata, H.1    Masuzawa, T.2    Nagaoka, Y.3    Ohnishi, T.4    Iwasaki, T.5
  • 220
    • 0027690079 scopus 로고
    • Gene expression patterns associated with in vitro tracheary element formation in isolated single mesophyll cells of Zinnia elegans
    • Ye Z-H, Varner J: Gene expression patterns associated with in vitro tracheary element formation in isolated single mesophyll cells of Zinnia elegans. Plant Physiol 103: 805-813 (1993).
    • (1993) Plant Physiol , vol.103 , pp. 805-813
    • Ye, Z.-H.1    Varner, J.2
  • 221
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally vacuolar compartments
    • Paris N, Stanley CM, Jones RL, Rogers JC: Plant cells contain two functionally vacuolar compartments. Cell 85: 563-572 (1996).
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4


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