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Volumn 3, Issue 5, 1999, Pages 584-591

Structure and mechanism of ATP-dependent proteases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; PROTEINASE;

EID: 0032859319     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)00013-7     Document Type: Review
Times cited : (66)

References (51)
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zühl F, Seemuller E The proteasome: paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemuller, E.4
  • 4
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Löwe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science. 268:1995;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
  • 6
    • 0030925223 scopus 로고    scopus 로고
    • Crystal structure of heat shock locus V (HslV) from Escherichia coli
    • Bochtler M, Ditzel L, Groll M, Huber R Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proc Natl Acad Sci USA. 94:1997;6070-6074.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6070-6074
    • Bochtler, M.1    Ditzel, L.2    Groll, M.3    Huber, R.4
  • 7
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang J, Hartling JA, Flanagan JM The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell. 91:1997;447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 8
    • 0030772933 scopus 로고    scopus 로고
    • Targeting of substrates to the 26S proteasome
    • Pickart CM Targeting of substrates to the 26S proteasome. FASEB J. 11:1997;1055-1066.
    • (1997) FASEB J , vol.11 , pp. 1055-1066
    • Pickart, C.M.1
  • 9
    • 0002981018 scopus 로고    scopus 로고
    • The 20S proteasome
    • J-M Peters, J.R. Harris, & D. Finley. New York: Plenum Press
    • Lupas A, Baumeister W The 20S proteasome. Peters J-M, Harris JR, Finley D Ubiquitin and the Biology of the Cell. 1998;127-143 Plenum Press, New York.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 127-143
    • Lupas, A.1    Baumeister, W.2
  • 11
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • Cryoelectron micrographs of ClpAP were used to characterize the symmetry mismatch between the heptameric ClpP cylinder and the hexameric ClpA ring. A cylindrical three-dimensional reconstruction reveals three internal cavities of the holocomplex: the central proteolytic chamber, a cavity within the ATPase ring and a connecting channel between these two chambers
    • Beuron F, Maurizi MR, Belnap DM, Kocsis E, Booy FP, Kessel M, Steven AC At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J Struct Biol. 123:1998;248-259. Cryoelectron micrographs of ClpAP were used to characterize the symmetry mismatch between the heptameric ClpP cylinder and the hexameric ClpA ring. A cylindrical three-dimensional reconstruction reveals three internal cavities of the holocomplex: the central proteolytic chamber, a cavity within the ATPase ring and a connecting channel between these two chambers.
    • (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
  • 12
    • 0031927996 scopus 로고    scopus 로고
    • 26S proteasome structure revealed by three-dimensional electron microscopy
    • The first three-dimensional reconstruction of 26S proteasomes, based on electron microscopic analysis, reveals a complex overall shape of the eukaryotic regulatory particle. A flexible linkage of the regulatory particle and the core particle is documented in addition to movements within the regulatory particle
    • Walz J, Erdmann A, Kania M, Typke D, Koster AJ, Baumeister W 26S proteasome structure revealed by three-dimensional electron microscopy. J Struct Biol. 121:1998;19-29. The first three-dimensional reconstruction of 26S proteasomes, based on electron microscopic analysis, reveals a complex overall shape of the eukaryotic regulatory particle. A flexible linkage of the regulatory particle and the core particle is documented in addition to movements within the regulatory particle.
    • (1998) J Struct Biol , vol.121 , pp. 19-29
    • Walz, J.1    Erdmann, A.2    Kania, M.3    Typke, D.4    Koster, A.J.5    Baumeister, W.6
  • 14
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud R, Kessel M, Beuron F, Steven AC, Maurizi MR Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J Biol Chem. 273:1998;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
  • 15
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26S proteasome, activates protein breakdown by 20S proteasomes
    • in press
    • Zwickl P, Ng D, Woo KM, Klenk H-P, Goldberg AL An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26S proteasome, activates protein breakdown by 20S proteasomes. J Biol Chem. 1999;. in press.
    • (1999) J Biol Chem
    • Zwickl, P.1    Ng, D.2    Woo, K.M.3    Klenk, H.-P.4    Goldberg, A.L.5
  • 16
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman MH, Rubin DM, Fried VA, Finley D The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol. 18:1998;3149-3162.
    • (1998) Mol Cell Biol , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 17
    • 0032577938 scopus 로고    scopus 로고
    • Molecular biology of the proteasome
    • Tanaka K Molecular biology of the proteasome. Biochem Biophys Res Commun. 247:1998;537-541.
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 537-541
    • Tanaka, K.1
  • 18
    • 0001730460 scopus 로고    scopus 로고
    • The 26S proteasome
    • J-M Peters, J.R. Harris, & D. Finley. New York: Plenum Press
    • Rechsteiner M The 26S proteasome. Peters J-M, Harris JR, Finley D. Ubiquitin and the Biology of the Cell. 1998;147-181 Plenum Press, New York.
    • (1998) Ubiquitin and the Biology of the Cell , pp. 147-181
    • Rechsteiner, M.1
  • 19
    • 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
    • Upon deletion of Rpn10, a non-ATPase subunit of the proteasome, the regulatory particle can be dissociated into two distinct subcomplexes. Whereas the lid contains eight non-ATPase subunits and is required for ubiquitin-dependent degradation of proteasomal substrates, the base complex is composed of the six ATPase subunits plus two non-ATPase subunits and is able to activate the peptidase activity of the proteolytic core particle in the presence of ATP
    • Glickman MH, Rubin DM, Coux O, Wefes I, Pfeifer G, Cjeka Z, Baumeister W, Fried VA, Finley D A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell. 94:1998;615-623. Upon deletion of Rpn10, a non-ATPase subunit of the proteasome, the regulatory particle can be dissociated into two distinct subcomplexes. Whereas the lid contains eight non-ATPase subunits and is required for ubiquitin-dependent degradation of proteasomal substrates, the base complex is composed of the six ATPase subunits plus two non-ATPase subunits and is able to activate the peptidase activity of the proteolytic core particle in the presence of ATP.
    • (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
  • 21
    • 13144305043 scopus 로고    scopus 로고
    • The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex
    • Wei N, Tsuge T, Serino G, Dohmae N, Takio K, Matsui M, Deng XW The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex. Curr Biol. 8:1998;919-922.
    • (1998) Curr Biol , vol.8 , pp. 919-922
    • Wei, N.1    Tsuge, T.2    Serino, G.3    Dohmae, N.4    Takio, K.5    Matsui, M.6    Deng, X.W.7
  • 22
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • In this study, the six proteasomal ATPases were shown to be functionally differentiated. Despite a high degree of sequence conservation among this subset of proteasomal subunits, individual inactivation results in distinct phenotypes from subunit to subunit. An Rpt2 mutant exhibited an inhibition of proteasomal peptidase activity, suggesting a possible role for Rpt2 in gating of the proteasome channel
    • Rubin DM, Glickman MH, Larsen CN, Dhruvakumar S, Finley D Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 17:1998;4909-4919. In this study, the six proteasomal ATPases were shown to be functionally differentiated. Despite a high degree of sequence conservation among this subset of proteasomal subunits, individual inactivation results in distinct phenotypes from subunit to subunit. An Rpt2 mutant exhibited an inhibition of proteasomal peptidase activity, suggesting a possible role for Rpt2 in gating of the proteasome channel.
    • (1998) EMBO J , vol.17 , pp. 4909-4919
    • Rubin, D.M.1    Glickman, M.H.2    Larsen, C.N.3    Dhruvakumar, S.4    Finley, D.5
  • 23
    • 0028840312 scopus 로고
    • FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli
    • Akiyama Y, Yoshihisa T, Ito K FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli. J Biol Chem. 270:1995;23485-23490.
    • (1995) J Biol Chem , vol.270 , pp. 23485-23490
    • Akiyama, Y.1    Yoshihisa, T.2    Ito, K.3
  • 24
    • 0029775087 scopus 로고    scopus 로고
    • AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • Leonhard K, Herrmann JM, Stuart RA, Mannhaupt G, Neupert W, Langer T AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15:1996;4218-4229.
    • (1996) EMBO J , vol.15 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, J.M.2    Stuart, R.A.3    Mannhaupt, G.4    Neupert, W.5    Langer, T.6
  • 25
    • 0032104477 scopus 로고    scopus 로고
    • How far divergent evolution goes in proteins
    • Murzin AG How far divergent evolution goes in proteins. Curr Opin Struct Biol. 8:1998;380-387.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 380-387
    • Murzin, A.G.1
  • 27
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF, Aravind L, Spouge JL, Koonin EV AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:1999;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
  • 28
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta′ subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J Crystal structure of the delta′ subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell. 91:1997;335-345.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 29
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • •] in the presence of AMP-PNP and ATP, respectively, provided insight into the subunit interactions of AAA+ proteins and into the nature of the nucleotide-binding pocket. In conjunction with the sequence conservation pattern of this protein family [2], it suggested a model for the coupling of ATP hydrolysis to conformational changes within the ring structure
    • •] in the presence of AMP-PNP and ATP, respectively, provided insight into the subunit interactions of AAA+ proteins and into the nature of the nucleotide-binding pocket. In conjunction with the sequence conservation pattern of this protein family [2], it suggested a model for the coupling of ATP hydrolysis to conformational changes within the ring structure.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 31
    • 0033535955 scopus 로고    scopus 로고
    • Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
    • The putative substrate-binding domains of various Clp ATPases and of Lon were analyzed for their ability to bind to in vivo substrates of the corresponding protease. They were shown to display distinct but overlapping substrate binding specificities
    • Smith CK, Baker TA, Sauer RT Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proc Natl Acad Sci USA. 96:1999;6678-6682. The putative substrate-binding domains of various Clp ATPases and of Lon were analyzed for their ability to bind to in vivo substrates of the corresponding protease. They were shown to display distinct but overlapping substrate binding specificities.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6678-6682
    • Smith, C.K.1    Baker, T.A.2    Sauer, R.T.3
  • 32
    • 0031457264 scopus 로고    scopus 로고
    • PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
    • Levchenko I, Smith CK, Walsh NP, Sauer RT, Baker TA PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell. 91:1997;939-947.
    • (1997) Cell , vol.91 , pp. 939-947
    • Levchenko, I.1    Smith, C.K.2    Walsh, N.P.3    Sauer, R.T.4    Baker, T.A.5
  • 33
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • The authors present the first evidence for a chaperone-like activity of an isolated ATPase domain of a eukaryotic energy-dependent protease, the AAA domain of the yeast mitochondrial membrane protease Yme1. Substrate binding by Yme1 is proposed to be guided by specific recognition of unfolded solvent exposed domains of integral membrane proteins
    • Leonhard K, Stiegler A, Neupert W, Langer T Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature. 398:1999;348-351. The authors present the first evidence for a chaperone-like activity of an isolated ATPase domain of a eukaryotic energy-dependent protease, the AAA domain of the yeast mitochondrial membrane protease Yme1. Substrate binding by Yme1 is proposed to be guided by specific recognition of unfolded solvent exposed domains of integral membrane proteins.
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 34
    • 0031231083 scopus 로고    scopus 로고
    • Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
    • Ahmadian MR, Stege P, Scheffzek K, Wittinghofer A Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras. Nat Struct Biol. 4:1997;686-689.
    • (1997) Nat Struct Biol , vol.4 , pp. 686-689
    • Ahmadian, M.R.1    Stege, P.2    Scheffzek, K.3    Wittinghofer, A.4
  • 35
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of the highly conserved second region of homology (SRH) in AAA family proteins: Site-directed mutagenesis of Escherichia coli FtsH
    • in press
    • Karata K, Inagawa T, Wilkinson AJ, Tatsuta T, Ogura T Dissecting the role of the highly conserved second region of homology (SRH) in AAA family proteins: site-directed mutagenesis of Escherichia coli FtsH. J Biol Chem. 1999;. in press.
    • (1999) J Biol Chem
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 37
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 94:1998;73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 38
    • 0028359550 scopus 로고
    • A new component of bacteriophage Mu replicative transposition machinery: The ClpX protein
    • Mhammedi-Alaoui A, Pato M, Gama MJ, Toussaint A A new component of bacteriophage Mu replicative transposition machinery: the ClpX protein. Mol Microbiol. 11:1994;1109-1116.
    • (1994) Mol Microbiol , vol.11 , pp. 1109-1116
    • Mhammedi-Alaoui, A.1    Pato, M.2    Gama, M.J.3    Toussaint, A.4
  • 39
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko I, Luo L, Baker TA Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9:1995;2399-2408.
    • (1995) Genes Dev , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 40
    • 0031961776 scopus 로고    scopus 로고
    • Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition
    • ClpXP exerts a dual function during bacteriophage Mu DNA replication. Its proteolytic activity is required to deactivate the repressor for Mu transposition, while the chaperone activity remodels MuA transposase, a step that is necessary for the transition to replisome assembly. Interestingly MuA is not degraded by ClpX during this process
    • Jones JM, Welty DJ, Nakai H Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition. J Biol Chem. 273:1998;459-465. ClpXP exerts a dual function during bacteriophage Mu DNA replication. Its proteolytic activity is required to deactivate the repressor for Mu transposition, while the chaperone activity remodels MuA transposase, a step that is necessary for the transition to replisome assembly. Interestingly MuA is not degraded by ClpX during this process.
    • (1998) J Biol Chem , vol.273 , pp. 459-465
    • Jones, J.M.1    Welty, D.J.2    Nakai, H.3
  • 42
    • 0032514746 scopus 로고    scopus 로고
    • The role of the ClpA chaperone in proteolysis by ClpAP
    • The individual steps of ClpAP mediated protein degradation were analyzed. It was shown that a protein bound to ClpA can be translocated to ClpP in the presence of ATP. While the assembly of the ClpAP holocomplex is achieved in the presence of non-hydrolyzable ATP analogs, substrate translocation requires ATP hydrolysis
    • Hoskins JR, Pak M, Maurizi MR, Wickner S The role of the ClpA chaperone in proteolysis by ClpAP. Proc Natl Acad Sci USA. 95:1998;12135-12140. The individual steps of ClpAP mediated protein degradation were analyzed. It was shown that a protein bound to ClpA can be translocated to ClpP in the presence of ATP. While the assembly of the ClpAP holocomplex is achieved in the presence of non-hydrolyzable ATP analogs, substrate translocation requires ATP hydrolysis.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12135-12140
    • Hoskins, J.R.1    Pak, M.2    Maurizi, M.R.3    Wickner, S.4
  • 43
    • 0033516473 scopus 로고    scopus 로고
    • Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity
    • By employing a chaperone-defective ClpA molecule, which is able to exert this activity only upon association with ClpP, the authors present evidence that the ClpAP holocomplex is able to exert both a proteolytic and protein-remodeling function
    • Pak M, Hoskins JR, Singh SK, Maurizi MR, Wickner S Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity. J Biol Chem. 274:1999;19316-19322. By employing a chaperone-defective ClpA molecule, which is able to exert this activity only upon association with ClpP, the authors present evidence that the ClpAP holocomplex is able to exert both a proteolytic and protein-remodeling function.
    • (1999) J Biol Chem , vol.274 , pp. 19316-19322
    • Pak, M.1    Hoskins, J.R.2    Singh, S.K.3    Maurizi, M.R.4    Wickner, S.5
  • 44
    • 0033176770 scopus 로고    scopus 로고
    • The base of the proteasome regulatory particle exhibits chaperone-like activity
    • In this study, a chaperone-like activity of the eukaryotic proteasome was demonstrated for the model substrate citrate synthase. The non-native molecule binds to the base subassembly. It is released in a folding-competent state in an ATP-stimulated process
    • Braun B, Glickman M, Kraft R, Dahlmann B, Kloetzel P-M, Finley D, Schmidt M The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat Cell Biol. 1:1999;221-226. In this study, a chaperone-like activity of the eukaryotic proteasome was demonstrated for the model substrate citrate synthase. The non-native molecule binds to the base subassembly. It is released in a folding-competent state in an ATP-stimulated process.
    • (1999) Nat Cell Biol , vol.1 , pp. 221-226
    • Braun, B.1    Glickman, M.2    Kraft, R.3    Dahlmann, B.4    Kloetzel, P.-M.5    Finley, D.6    Schmidt, M.7
  • 45
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • Rad 23 is a mediator of nucleotide excision repair that was previously demonstrated to associate with the proteasome via a ubiquitin-like domain at its amino-terminus. This paper shows that the Rad23-proteasome interaction is important for nucleotide excision repair in vitro. The data also suggest for the first time a non-proteolytic activity of the proteasome, which is suggested to be a chaperone activity
    • Russell SJ, Reed SH, Huang W, Friedberg EC, Johnston SA The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Molec Cell. 3:1999;687-695. Rad 23 is a mediator of nucleotide excision repair that was previously demonstrated to associate with the proteasome via a ubiquitin-like domain at its amino-terminus. This paper shows that the Rad23-proteasome interaction is important for nucleotide excision repair in vitro. The data also suggest for the first time a non-proteolytic activity of the proteasome, which is suggested to be a chaperone activity.
    • (1999) Molec Cell , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 47
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • This study provides the first direct evidence for an active unfolding event in a chaperone-mediated refolding system. By analyzing the velocity of hydrogen exchange of tritium-labeled protein, it was demonstrated that protected protons become accessible to the surrounding medium during Rubisco refolding in the presence of the complete chaperonin system
    • Shtilerman M, Lorimer GH, Englander SW Chaperonin function: folding by forced unfolding. Science. 284:1999;822-825. This study provides the first direct evidence for an active unfolding event in a chaperone-mediated refolding system. By analyzing the velocity of hydrogen exchange of tritium-labeled protein, it was demonstrated that protected protons become accessible to the surrounding medium during Rubisco refolding in the presence of the complete chaperonin system.
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 48
    • 0033153237 scopus 로고    scopus 로고
    • Dislocation of membrane proteins in FtsH-mediated proteolysis
    • FtsH is a membrane-inserted ATP-dependent protease with its functional domains facing the cytoplasm. Despite this topology, FtsH is able to degrade a membrane-bound protein that is exposed to the periplasmic space. Complete degradation by FtsH is only possible if disulfide bond formation in the periplasm is prevented. Presumably the disulfide bonds impose a steric block to the unfolding and pulling forces imposed by FtsH during the degradation process
    • Kihara A, Akiyama Y, Ito K Dislocation of membrane proteins in FtsH-mediated proteolysis. EMBO J. 18:1999;2970-2981. FtsH is a membrane-inserted ATP-dependent protease with its functional domains facing the cytoplasm. Despite this topology, FtsH is able to degrade a membrane-bound protein that is exposed to the periplasmic space. Complete degradation by FtsH is only possible if disulfide bond formation in the periplasm is prevented. Presumably the disulfide bonds impose a steric block to the unfolding and pulling forces imposed by FtsH during the degradation process.
    • (1999) EMBO J , vol.18 , pp. 2970-2981
    • Kihara, A.1    Akiyama, Y.2    Ito, K.3
  • 49
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer T, Wolf DH Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J. 11:1997;1227-1233.
    • (1997) FASEB J , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 50
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein
    • The authors show that the proteasome plays a key role in the extraction of membrane proteins from the ER membrane prior to their degradation. Data obtained with proteasome mutants suggest that the driving force for retrograde protein transport from the ER may be generated by the proteasome
    • Mayer TU, Braun T, Jentsch S Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J. 17:1998;3251-3257. The authors show that the proteasome plays a key role in the extraction of membrane proteins from the ER membrane prior to their degradation. Data obtained with proteasome mutants suggest that the driving force for retrograde protein transport from the ER may be generated by the proteasome.
    • (1998) EMBO J , vol.17 , pp. 3251-3257
    • Mayer, T.U.1    Braun, T.2    Jentsch, S.3
  • 51
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz EJH, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 384:1996;432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.