메뉴 건너뛰기




Volumn 182, Issue 6, 2000, Pages 1680-1692

Biochemical and physical properties of the Methanococcus jannaschii 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the eucaryal 26S proteasome

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINO ACID; BACTERIAL ENZYME; CYTIDINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; NUCLEOTIDASE; NUCLEOTIDE; PROTEASOME; URIDINE TRIPHOSPHATE;

EID: 0034100371     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.6.1680-1692.2000     Document Type: Article
Times cited : (75)

References (84)
  • 1
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum
    • Akopian, T. N., A. F. Kisselev, and A. L. Goldberg. 1997. Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272:1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 2
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., T. K. Sato, L. M. Banta, and S. D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831.
    • (1997) EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 3
    • 0031038205 scopus 로고    scopus 로고
    • Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus
    • Bauer, M. W., S. B. Halio, and R. M. Kelly. 1997. Purification and characterization of a proteasome from the hyperthermophilic archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 63:1160-1164.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1160-1164
    • Bauer, M.W.1    Halio, S.B.2    Kelly, R.M.3
  • 4
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., J. Walz, F. Zühl, and E. Seemüller. 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92:367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 5
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • Beuron, F., M. R. Maurizi, D. M. Belnap, E. Kocsis, F. P. Booy, M. Kessel, and A. C. Steven. 1998. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123: 248-259.
    • (1998) J. Struct. Biol. , vol.123 , pp. 248-259
    • Beuron, F.1    Maurizi, M.R.2    Belnap, D.M.3    Kocsis, E.4    Booy, F.P.5    Kessel, M.6    Steven, A.C.7
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0025212540 scopus 로고
    • A second consensus sequence of ATP-requiring proteins resides in the 21-kDa C-terminal segment of myosin subfragment 1
    • Burke, M., K. N. Rajasekharan, S. Maruta, and M. Ikebe. 1990. A second consensus sequence of ATP-requiring proteins resides in the 21-kDa C-terminal segment of myosin subfragment 1. FEBS Lett. 262:185-188.
    • (1990) FEBS Lett. , vol.262 , pp. 185-188
    • Burke, M.1    Rajasekharan, K.N.2    Maruta, S.3    Ikebe, M.4
  • 10
    • 0023790425 scopus 로고
    • Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La
    • Chin, D. T., S. A. Goff, T. Webster, T. Smith, and A. L. Goldberg. 1988. Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La. J. Biol. Chem. 263:11718-11728.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11718-11728
    • Chin, D.T.1    Goff, S.A.2    Webster, T.3    Smith, T.4    Goldberg, A.L.5
  • 12
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., K. Tanaka, and A. L. Goldberg. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 13
    • 0026746240 scopus 로고
    • Biochemical properties of the proteasome from Thermoplasma acidophilum
    • Dahlmann, B., L. Kuehn, A. Grizwa, P. Zwickl, and W. Baumeister. 1992. Biochemical properties of the proteasome from Thermoplasma acidophilum. Eur. J. Biochem. 208:789-797.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 789-797
    • Dahlmann, B.1    Kuehn, L.2    Grizwa, A.3    Zwickl, P.4    Baumeister, W.5
  • 14
    • 0024972956 scopus 로고
    • The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria
    • Dahlmann, B., F. Kopp, L. Kuehn, B. Niedel, G. Pfeifer, R. Hegerl, and W. Baumeister. 1989. The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Lett. 251:125-131.
    • (1989) FEBS Lett. , vol.251 , pp. 125-131
    • Dahlmann, B.1    Kopp, F.2    Kuehn, L.3    Niedel, B.4    Pfeifer, G.5    Hegerl, R.6    Baumeister, W.7
  • 15
    • 0023021180 scopus 로고
    • Role of ATP hydrolysis in the degradation of proteins by protease La from Escherichia coli
    • Edmunds, T., and A. L. Goldberg. 1986. Role of ATP hydrolysis in the degradation of proteins by protease La from Escherichia coli. J. Cell. Biochem. 32:187-191.
    • (1986) J. Cell. Biochem. , vol.32 , pp. 187-191
    • Edmunds, T.1    Goldberg, A.L.2
  • 17
    • 0028881024 scopus 로고
    • The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM
    • Fröhlich, K. U., H. W. Fries, J. M. Peters, and D. Mecke. 1995. The ATPase activity of purified CDC48p from Saccharomyces cerevisiae shows complex dependence on ATP-, ADP-, and NADH-concentrations and is completely inhibited by NEM. Biochim. Biophys. Acta 1253:25-32.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 25-32
    • Fröhlich, K.U.1    Fries, H.W.2    Peters, J.M.3    Mecke, D.4
  • 18
    • 0024210542 scopus 로고
    • A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation
    • Ganoth, D., E. Leshinsky, E. Eytan, and A. Hershko. 1988. A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation. J. Biol. Chem. 263:12412-12419.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12412-12419
    • Ganoth, D.1    Leshinsky, E.2    Eytan, E.3    Hershko, A.4
  • 19
    • 0032498229 scopus 로고    scopus 로고
    • The human proteasomal subunit HsC8 induces ring formation of other α-type subunits
    • Gerards, W. L., W. W. de Jong, H. Bloemendal, and W. Boelens. 1998. The human proteasomal subunit HsC8 induces ring formation of other α-type subunits. J. Mol. Biol. 275:113-121.
    • (1998) J. Mol. Biol. , vol.275 , pp. 113-121
    • Gerards, W.L.1    De Jong, W.W.2    Bloemendal, H.3    Boelens, W.4
  • 20
    • 0030950435 scopus 로고    scopus 로고
    • The human α-type proteasomal subunit HsC8 forms a double ringlike structure, but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26
    • Gerards, W. L., J. Enzlin, M. Haner, I. L. Hendriks, U. Aebi, H. Bloemendal, and W. Boelens. 1997. The human α-type proteasomal subunit HsC8 forms a double ringlike structure, but does not assemble into proteasome-like particles with the β-type subunits HsDelta or HsBPROS26. J. Biol. Chem. 272:10080-10086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10080-10086
    • Gerards, W.L.1    Enzlin, J.2    Haner, M.3    Hendriks, I.L.4    Aebi, U.5    Bloemendal, H.6    Boelens, W.7
  • 21
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M. H., D. M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V. A. Fried, and D. Finley. 1998. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94:615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 22
    • 0033118230 scopus 로고    scopus 로고
    • Regulation by proteolysis: Developmental switches
    • Gottesman, S. 1999. Regulation by proteolysis: developmental switches. Curr. Opin. Microbiol. 2:142-147.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 142-147
    • Gottesman, S.1
  • 23
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., S. Wickner, and M. R. Maurizi. 1997. Protein quality control: triage by chaperones and proteases. Genes Dev. 11:815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 24
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud, R., M. Kessel, F. Beuron, A. C. Steven, and M. R. Maurizi. 1998. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273:12476-12481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 25
    • 0025886124 scopus 로고
    • Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy
    • Grizwa, A., W. Baumeister, B. Dahlmann, and F. Kopp. 1991. Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy. FEBS Lett. 290:186-190.
    • (1991) FEBS Lett. , vol.290 , pp. 186-190
    • Grizwa, A.1    Baumeister, W.2    Dahlmann, B.3    Kopp, F.4
  • 26
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P. I., R. Roth, H. Morisaki, R. Jahn, and J. E. Heuser. 1997. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90:523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 27
    • 0003448569 scopus 로고    scopus 로고
    • Immunoblotting
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1999. Immunoblotting, p. 269-309. In Using antibodies:a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1999) Using Antibodies: A Laboratory Manual , pp. 269-309
    • Harlow, E.1    Lane, D.2
  • 28
    • 16944366641 scopus 로고    scopus 로고
    • Nucleotidase activities of the 26S proteasome and its regulatory complex
    • Hoffman, L., and M. Rechsteiner. 1996. Nucleotidase activities of the 26S proteasome and its regulatory complex. J. Biol. Chem. 271:32538-32545.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32538-32545
    • Hoffman, L.1    Rechsteiner, M.2
  • 30
    • 0023906054 scopus 로고
    • Protease Ti, a new ATP-dependent protease in Eschirichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits
    • Hwang, B. J., K. M. Woo, A. L. Goldberg, and C. H. Chung. 1988. Protease Ti, a new ATP-dependent protease in Eschirichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits. J. Biol. Chem. 263:8727-8734.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8727-8734
    • Hwang, B.J.1    Woo, K.M.2    Goldberg, A.L.3    Chung, C.H.4
  • 31
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata, K., T. Inagawa, A. J. Wilkinson, T. Tatsuta, and T. Ogura. 1999. Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem. 274:26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 35
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • Kodama, T., K. Fukui, and K. Kometani. 1986. The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J. Biochem. 99:1465-1472.
    • (1986) J. Biochem. , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 36
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P., L. Alvarez, P. Reinach, and O. Candia. 1979. An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100: 95-97.
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.1    Alvarez, L.2    Reinach, P.3    Candia, O.4
  • 37
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber. 1995. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268:533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 38
    • 0028899966 scopus 로고
    • Cloning and expression of a yeast gene encoding a protein with ATPase activity and high identity to the subunit 4 of the human 26S protease
    • Lucero, H., E. Chojnicki, S. Mandiyan, H. Nelson, and N. Nelson. 1995. Cloning and expression of a yeast gene encoding a protein with ATPase activity and high identity to the subunit 4 of the human 26S protease. J. Biol. Chem. 270:9178-9184.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9178-9184
    • Lucero, H.1    Chojnicki, E.2    Mandiyan, S.3    Nelson, H.4    Nelson, N.5
  • 40
    • 0343501897 scopus 로고    scopus 로고
    • Unpublished results
    • Maupin-Furlow, J. A. 1999. Unpublished results.
    • (1999)
    • Maupin-Furlow, J.A.1
  • 41
    • 0031918337 scopus 로고    scopus 로고
    • Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila
    • Maupin-Furlow, J. A., H. C. Aldrich, and J. G. Ferry. 1998. Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila. J. Bacteriol. 180:1480-1487.
    • (1998) J. Bacteriol. , vol.180 , pp. 1480-1487
    • Maupin-Furlow, J.A.1    Aldrich, H.C.2    Ferry, J.G.3
  • 42
    • 0028810102 scopus 로고
    • A proteasome from the methanogenic archaeon Methanosarcina thermophila
    • Maupin-Furlow, J. A., and J. G. Ferry. 1995. A proteasome from the methanogenic archaeon Methanosarcina thermophila. J. Biol. Chem. 270:28617-28622.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28617-28622
    • Maupin-Furlow, J.A.1    Ferry, J.G.2
  • 43
    • 0032568504 scopus 로고    scopus 로고
    • Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and ClpP
    • Maurizi, M. R., S. K. Singh, M. W. Thompson, M. Kessel, and A. Ginsburg. 1998. Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and ClpP. Biochemistry 37:7778-7786.
    • (1998) Biochemistry , vol.37 , pp. 7778-7786
    • Maurizi, M.R.1    Singh, S.K.2    Thompson, M.W.3    Kessel, M.4    Ginsburg, A.5
  • 44
    • 0028149757 scopus 로고
    • The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins
    • Morgan, A., R. Dimaline, and R. D. Burgoyne. 1994. The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins. J. Biol. Chem. 269:29347-29350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29347-29350
    • Morgan, A.1    Dimaline, R.2    Burgoyne, R.D.3
  • 46
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., L. Aravind, J. L. Spouge, and E. V. Koonin. 1999. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 48
    • 0031042544 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum
    • Pamnani, V., T. Tamura, A. Lupas, J. Peters, Z. Cejka, W. Ashraf, and W. Baumeister. 1997. Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum. FEBS Lett. 404:263-268.
    • (1997) FEBS Lett. , vol.404 , pp. 263-268
    • Pamnani, V.1    Tamura, T.2    Lupas, A.3    Peters, J.4    Cejka, Z.5    Ashraf, W.6    Baumeister, W.7
  • 50
    • 0025314878 scopus 로고
    • An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF
    • Peters, J. M., M. J. Walsh, and W. W. Franke. 1990. An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle related to the putative vesicle fusion proteins Sec18p and NSF. EMBO J. 9:1757-1767.
    • (1990) EMBO J. , vol.9 , pp. 1757-1767
    • Peters, J.M.1    Walsh, M.J.2    Franke, W.W.3
  • 51
    • 0031001763 scopus 로고    scopus 로고
    • Specific interactions between ATPase subunits of the 26 S protease
    • Richmond, C., C. Gorbea, and M. Rechsteiner. 1997. Specific interactions between ATPase subunits of the 26 S protease. J. Biol. Chem. 272:13403-13411.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13403-13411
    • Richmond, C.1    Gorbea, C.2    Rechsteiner, M.3
  • 52
    • 0027516156 scopus 로고
    • Proteasomes: Multicatalytic proteinase complexes
    • Rivett, A. J. 1993. Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291:1-10.
    • (1993) Biochem. J. , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 53
    • 0032905074 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of a VCP homolog in African trypanosomes
    • Roggy, J. L., and J. D. Bangs. 1999. Molecular cloning and biochemical characterization of a VCP homolog in African trypanosomes. Mol. Biochem. Parasitol. 98:1-15.
    • (1999) Mol. Biochem. Parasitol. , vol.98 , pp. 1-15
    • Roggy, J.L.1    Bangs, J.D.2
  • 54
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., P. R. Sibbald, and A. Wittinghofer. 1990. The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15:430-434.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 55
    • 0029789918 scopus 로고    scopus 로고
    • Autocatalytic processing of the 20S proteasome
    • Seemüller, E., A. Lupas, and W. Baumeister. 1996. Autocatalytic processing of the 20S proteasome. Nature 382:468-470.
    • (1996) Nature , vol.382 , pp. 468-470
    • Seemüller, E.1    Lupas, A.2    Baumeister, W.3
  • 56
    • 0029610391 scopus 로고
    • The 65-kDa protein derived from the internal translational start site of the clpA gene blocks autodegradation of ClpA by the ATP-dependent protease Ti in Escherichia coli
    • Seol, J. H., S. J. Yoo, M. S. Kang, D. B. Ha, and C. H. Chung. 1995. The 65-kDa protein derived from the internal translational start site of the clpA gene blocks autodegradation of ClpA by the ATP-dependent protease Ti in Escherichia coli. FEBS Lett. 377:41-43.
    • (1995) FEBS Lett. , vol.377 , pp. 41-43
    • Seol, J.H.1    Yoo, S.J.2    Kang, M.S.3    Ha, D.B.4    Chung, C.H.5
  • 61
    • 0027474007 scopus 로고
    • Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport
    • Tagaya, M., D. W. Wilson, M. Brunner, N. Arango, and J. E. Rothman. 1993. Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268:2662-2666.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2662-2666
    • Tagaya, M.1    Wilson, D.W.2    Brunner, M.3    Arango, N.4    Rothman, J.E.5
  • 63
    • 0028365133 scopus 로고
    • Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli: Requirement for the multiple array of active sites in ClpB but not ATP hydrolysis
    • Thompson, M. W., S. K. Singh, and M. R. Maurizi. 1994. Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli: requirement for the multiple array of active sites in ClpB but not ATP hydrolysis. J. Biol. Chem. 269:18209-18215.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18209-18215
    • Thompson, M.W.1    Singh, S.K.2    Maurizi, M.R.3
  • 65
    • 0033032942 scopus 로고    scopus 로고
    • Substrate sequestration by a proteolytically inactive lon mutant
    • Van Melderen, L., and S. Gottesman. 1999. Substrate sequestration by a proteolytically inactive lon mutant. Proc. Natl. Acad. Sci. USA 96:6064-6071.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6064-6071
    • Van Melderen, L.1    Gottesman, S.2
  • 66
    • 0001607723 scopus 로고
    • Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., M. Saraste, M. J. Runswick, and N. J. Gay. 1982. Distantly related sequences in the α- and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1:945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 67
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang, J., J. A. Hartling, and J. M. Flanagan. 1997. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91: 447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 68
    • 0029739021 scopus 로고    scopus 로고
    • Mammalian Sug1 and c-Fos in the nuclear 26S proteasome
    • Wang, W., P. M. Chevray, and D. Nathans. 1996. Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. Proc. Natl. Acad. Sci. USA 93:8236-8240.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8236-8240
    • Wang, W.1    Chevray, P.M.2    Nathans, D.3
  • 69
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., D. Wojtkowiak, J. Marszalek, B. Banecki, M. Jonsen, B. Graves, C. Georgopoulos, and M. Zylicz. 1995. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14:1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 70
    • 0020294051 scopus 로고
    • Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion
    • Waxman, L., and A. L. Goldberg. 1982. Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion. Proc. Natl. Acad. Sci. USA 79:4883-4887.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4883-4887
    • Waxman, L.1    Goldberg, A.L.2
  • 71
    • 0022413419 scopus 로고
    • Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction
    • Waxman, L., and A. L. Goldberg. 1985. Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction. J. Biol. Chem. 260:12022-12028.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12022-12028
    • Waxman, L.1    Goldberg, A.L.2
  • 72
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel, T., and W. Baumeister. 1995. Conformational constraints in protein degradation by the 20S proteasome. Nat. Struct. Biol. 2:199-204.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 73
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S. W., K. Rossnagel, S. A. Buhrow, M. Brunner, R. Jaenicke, and J. E. Rothman. 1994. N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126:945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 74
    • 0032836107 scopus 로고    scopus 로고
    • Halophilic 20S proteasomes of the archaeon Haloferax volcanii: Purification, characterization, and gene sequence analysis
    • Wilson, H. L., H. C. Aldrich, and J. A. Maupin-Furlow. 1999. Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis. J. Bacteriol. 181:5814-5824.
    • (1999) J. Bacteriol. , vol.181 , pp. 5814-5824
    • Wilson, H.L.1    Aldrich, H.C.2    Maupin-Furlow, J.A.3
  • 75
    • 0027519423 scopus 로고
    • Isolation and characterization of CLpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli
    • Wojtkowiak, D., C. Georgopoulos, and M. Zylicz. 1993. Isolation and characterization of CLpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli. J. Biol. Chem. 268:22609-22617.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22609-22617
    • Wojtkowiak, D.1    Georgopoulos, C.2    Zylicz, M.3
  • 77
    • 0001592716 scopus 로고
    • The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase
    • Woo, K. M., K. I. Kim, A. L. Goldberg, D. B. Ha, and C. H. Chung. 1992. The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J. Biol. Chem. 267:20429-20434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20429-20434
    • Woo, K.M.1    Kim, K.I.2    Goldberg, A.L.3    Ha, D.B.4    Chung, C.H.5
  • 78
    • 0033408417 scopus 로고    scopus 로고
    • α5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings
    • Yao, Y., C. R. Toth, L. Huang, M. L. Wong, P. Dias, A. L. Burlingame, P. Coffino, and C. C. Wang. 1999. α5 subunit in Trypanosoma brucei proteasome can self-assemble to form a cylinder of four stacked heptamer rings. Biochem. J. 344:349-358.
    • (1999) Biochem. J. , vol.344 , pp. 349-358
    • Yao, Y.1    Toth, C.R.2    Huang, L.3    Wong, M.L.4    Dias, P.5    Burlingame, A.L.6    Coffino, P.7    Wang, C.C.8
  • 79
    • 0007951626 scopus 로고    scopus 로고
    • Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis
    • Yoo, S. J., H. H. Kim, D. H. Shin, C. S. Lee, I. S. Seong, J. H. Seol, N. Shimbara, K. Tanaka, and C. H. Chung. 1998. Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis. J. Biol. Chem. 273: 22929-22935.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22929-22935
    • Yoo, S.J.1    Kim, H.H.2    Shin, D.H.3    Lee, C.S.4    Seong, I.S.5    Seol, J.H.6    Shimbara, N.7    Tanaka, K.8    Chung, C.H.9
  • 80
    • 0001588962 scopus 로고    scopus 로고
    • Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
    • Yoo, S. J., J. H. Seol, D. H. Shin, M. Rohrwild, M.-S. Kang, K. Tanaka, A. L. Goldberg, and C. H. Chung. 1996. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J. Biol. Chem. 271:14035-14040.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14035-14040
    • Yoo, S.J.1    Seol, J.H.2    Shin, D.H.3    Rohrwild, M.4    Kang, M.-S.5    Tanaka, K.6    Goldberg, A.L.7    Chung, C.H.8
  • 81
    • 0039660001 scopus 로고    scopus 로고
    • Dissecting the assembly pathway of the 20S proteasome
    • Zühl, F., E. Seemüller, R. Golbik, and W. Baumeister. 1997. Dissecting the assembly pathway of the 20S proteasome. FEBS Lett. 418:189-194.
    • (1997) FEBS Lett. , vol.418 , pp. 189-194
    • Zühl, F.1    Seemüller, E.2    Golbik, R.3    Baumeister, W.4
  • 84
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26S proteasome, activates protein breakdown by 20S proteasomes
    • Zwickl, P., D. Ng, K. M. Woo, H.-P. Klenk, and A. L. Goldberg. 1999. An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26S proteasome, activates protein breakdown by 20S proteasomes. J. Biol. Chem. 274:26008-26014.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26008-26014
    • Zwickl, P.1    Ng, D.2    Woo, K.M.3    Klenk, H.-P.4    Goldberg, A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.