메뉴 건너뛰기




Volumn 10, Issue 2, 2000, Pages 242-250

Dis-assembly lines: The proteasome and related ATPase-assisted proteases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; PROTEASOME; PROTEINASE;

EID: 0034076210     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00075-0     Document Type: Review
Times cited : (78)

References (94)
  • 2
    • 0032549642 scopus 로고    scopus 로고
    • Proteasome function is dispensable under normal but not under heat-shock conditions in Thermoplasma acidophilum
    • Ruepp A., Eckerskorn C., Bogyo M., Baumeister W. Proteasome function is dispensable under normal but not under heat-shock conditions in Thermoplasma acidophilum. FEBS Lett. 425:1998;87-90.
    • (1998) FEBS Lett , vol.425 , pp. 87-90
    • Ruepp, A.1    Eckerskorn, C.2    Bogyo, M.3    Baumeister, W.4
  • 3
    • 0030877378 scopus 로고    scopus 로고
    • Inactivation of the 20S proteasome in Mycobacterium smegmatis
    • Knipfer N., Shrader T.E. Inactivation of the 20S proteasome in Mycobacterium smegmatis. Mol Microbiol. 25:1997;375-383.
    • (1997) Mol Microbiol , vol.25 , pp. 375-383
    • Knipfer, N.1    Shrader, T.E.2
  • 4
    • 0033083967 scopus 로고    scopus 로고
    • Proteasomes and other self-compartmentalizing proteases in prokaryotes
    • De Mot R., Nagy I., Walz J., Baumeister W. Proteasomes and other self-compartmentalizing proteases in prokaryotes. Trends Microbiol. 7:1999;88-92.
    • (1999) Trends Microbiol , vol.7 , pp. 88-92
    • De Mot, R.1    Nagy, I.2    Walz, J.3    Baumeister, W.4
  • 5
    • 0032836107 scopus 로고    scopus 로고
    • Halophilic 20S proteasomes of the archaeon Haloferax volcanii: Purification, characterization, and gene sequence analysis
    • Wilson H.L., Aldrich H.C., Maupin-Furlow J. Halophilic 20S proteasomes of the archaeon Haloferax volcanii: purification, characterization, and gene sequence analysis. J Bacteriol. 181:1999;5814-5824.
    • (1999) J Bacteriol , vol.181 , pp. 5814-5824
    • Wilson, H.L.1    Aldrich, H.C.2    Maupin-Furlow, J.3
  • 7
    • 0033959311 scopus 로고    scopus 로고
    • Characterization of the 20S proteasome from the actinomycete Frankia
    • Pouch M.-N., Cournoyer B., Baumeister W. Characterization of the 20S proteasome from the actinomycete Frankia. Mol Microbiol. 35:2000;368-377.
    • (2000) Mol Microbiol , vol.35 , pp. 368-377
    • Pouch, M.-N.1    Cournoyer, B.2    Baumeister, W.3
  • 9
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: Cooperative incorporation of interferon γ (IFN-γ)-inducible subunits
    • Griffin T.A., Nandi D., Cruz M., Fehling H.J., Vankaer L., Monaco J.J., Colbert R.A. Immunoproteasome assembly. cooperative incorporation of interferon γ (IFN-γ)-inducible subunits J Exp Med. 187:1998;97-104.
    • (1998) J Exp Med , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3    Fehling, H.J.4    Vankaer, L.5    Monaco, J.J.6    Colbert, R.A.7
  • 10
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • A comprehensive overview of proteasome research, with the main focus on 26S proteasomes.
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem. 68:1999;1015-1068. A comprehensive overview of proteasome research, with the main focus on 26S proteasomes.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 11
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zühl F., Seemüller 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    Seemüller, E.4
  • 13
    • 0029789918 scopus 로고    scopus 로고
    • Autocatalytic processing of the 20S proteasome
    • Seemüller E., Lupas A., Baumeister W. Autocatalytic processing of the 20S proteasome. Nature. 382:1996;468-470.
    • (1996) Nature , vol.382 , pp. 468-470
    • Seemüller, E.1    Lupas, A.2    Baumeister, W.3
  • 16
    • 0032476030 scopus 로고    scopus 로고
    • Contribution of proteasomal β-subunits to the cleavage of peptide-substrates analyzed with yeast mutants
    • Mutational and biochemical analyses of the specificity of the proteasomal β subunits are presented. All proteolytic activities could be assigned to subunits β1, β2 and β5, excluding the existence of additional active sites.
    • Dick T.P., Nussbaum A.K., Deeg M., Heinemeyer W., Groll M., Schirle M., Keilholz W., Stevanovic S., Wolf D.H., Huber R.et al. Contribution of proteasomal β-subunits to the cleavage of peptide-substrates analyzed with yeast mutants. J Biol Chem. 273:1998;25637-25646. Mutational and biochemical analyses of the specificity of the proteasomal β subunits are presented. All proteolytic activities could be assigned to subunits β1, β2 and β5, excluding the existence of additional active sites.
    • (1998) J Biol Chem , vol.273 , pp. 25637-25646
    • Dick, T.P.1    Nussbaum, A.K.2    Deeg, M.3    Heinemeyer, W.4    Groll, M.5    Schirle, M.6    Keilholz, W.7    Stevanovic, S.8    Wolf, D.H.9    Huber, R.10
  • 17
    • 0032514684 scopus 로고    scopus 로고
    • Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1
    • The authors describe the analysis of the cleavage products of enolase degraded by yeast proteasomes. A comparison of the fragments generated by wild-type and mutant proteasomes demonstrated that the product length is not dependent on the number of active sites.
    • Nussbaum A.K., Dick T.P., Keilholz W., Schirle M., Stevanovic S., Dietz K., Heinemeyer W., Groll M., Wolf D.H., Huber R.et al. Cleavage motifs of the yeast 20S proteasome β subunits deduced from digests of enolase 1. Proc Natl Acad Sci USA. 95:1998;12504-12509. The authors describe the analysis of the cleavage products of enolase degraded by yeast proteasomes. A comparison of the fragments generated by wild-type and mutant proteasomes demonstrated that the product length is not dependent on the number of active sites.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12504-12509
    • Nussbaum, A.K.1    Dick, T.P.2    Keilholz, W.3    Schirle, M.4    Stevanovic, S.5    Dietz, K.6    Heinemeyer, W.7    Groll, M.8    Wolf, D.H.9    Huber, R.10
  • 18
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • A cyclical bite-chew mechanism for protein breakdown by proteasomes is proposed, based on the finding of allosteric regulation of active sites.
    • Kisselev A.F., Akopian T.N., Castillo V., Goldberg A.L. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol Cell. 4:1999;395-402. A cyclical bite-chew mechanism for protein breakdown by proteasomes is proposed, based on the finding of allosteric regulation of active sites.
    • (1999) Mol Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 19
    • 0039660001 scopus 로고    scopus 로고
    • Dissecting the assembly pathway of the 20S proteasome
    • Zühl F., Seemüller E., Golbik R., Baumeister W. Dissecting the assembly pathway of the 20S proteasome. FEBS Lett. 418:1997;189-194.
    • (1997) FEBS Lett , vol.418 , pp. 189-194
    • Zühl, F.1    Seemüller, E.2    Golbik, R.3    Baumeister, W.4
  • 23
    • 0033597273 scopus 로고    scopus 로고
    • Sequence information within proteasomal prosequences mediates efficient integration of β-subunits into the 20 S proteasome complex
    • Schmidt M., Zantopf D., Kraft R., Kostka S., Preissner R., Kloetzel P.M. Sequence information within proteasomal prosequences mediates efficient integration of β-subunits into the 20 S proteasome complex. J Mol Biol. 288:1999;117-128.
    • (1999) J Mol Biol , vol.288 , pp. 117-128
    • Schmidt, M.1    Zantopf, D.2    Kraft, R.3    Kostka, S.4    Preissner, R.5    Kloetzel, P.M.6
  • 24
    • 0040008534 scopus 로고    scopus 로고
    • Proteasome β-type subunits: Unequal roles of propeptides in core particle maturation and a hierarchy of active site function
    • Jäger S., Groll M., Huber R., Wolf D.H., Heinemeyer W. Proteasome β-type subunits: unequal roles of propeptides in core particle maturation and a hierarchy of active site function. J Mol Biol. 291:1999;997-1013.
    • (1999) J Mol Biol , vol.291 , pp. 997-1013
    • Jäger, S.1    Groll, M.2    Huber, R.3    Wolf, D.H.4    Heinemeyer, W.5
  • 25
    • 0030880547 scopus 로고    scopus 로고
    • Intermediates in the formation of mouse 20S proteasomes - Implications for the assembly of precursor β-subunits
    • Nandi D., Woodward E., Ginsburg D.B., Monaco J.J. Intermediates in the formation of mouse 20S proteasomes - implications for the assembly of precursor β-subunits. EMBO J. 16:1997;5363-5375.
    • (1997) EMBO J , vol.16 , pp. 5363-5375
    • Nandi, D.1    Woodward, E.2    Ginsburg, D.B.3    Monaco, J.J.4
  • 26
    • 0031585998 scopus 로고    scopus 로고
    • Maturation of mammalian 20S proteasome: Purification and characterization of 13 S and 16 S proteasome precursor complexes
    • Schmidtke G., Schmidt M., Kloetzel P.M. Maturation of mammalian 20S proteasome: purification and characterization of 13 S and 16 S proteasome precursor complexes. J Mol Biol. 268:1997;95-106.
    • (1997) J Mol Biol , vol.268 , pp. 95-106
    • Schmidtke, G.1    Schmidt, M.2    Kloetzel, P.M.3
  • 27
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • The authors report the discovery of the short-lived chaperone Ump1p, which is required for the correct maturation of the yeast 20S proteasome.
    • Ramos P.C., H.öckendorff J., Johnson E.S., Varshavsky A., Dohmen R.J. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell. 92:1998;489-499. The authors report the discovery of the short-lived chaperone Ump1p, which is required for the correct maturation of the yeast 20S proteasome.
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    H.öckendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 28
    • 0033168717 scopus 로고    scopus 로고
    • Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly
    • α-acetylation.
    • α-acetylation.
    • (1999) EMBO J , vol.18 , pp. 3575-3585
    • Arendt, C.S.1    Hochstrasser, M.2
  • 29
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev A.F., Akopian T.N., Goldberg A.L. Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J Biol Chem. 273:1998;1982-1989.
    • (1998) J Biol Chem , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 30
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes - Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev A.F., Akopian T.N., Woo K.M., Goldberg A.L. The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes - implications for understanding the degradative mechanism and antigen presentation. J Biol Chem. 274:1999;3363-3371.
    • (1999) J Biol Chem , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 31
    • 0344527769 scopus 로고    scopus 로고
    • Decelerated degradation of short peptides by the 20S proteasome
    • Dolenc I., Seemüller E., Baumeister W. Decelerated degradation of short peptides by the 20S proteasome. FEBS Lett. 434:1998;357-361.
    • (1998) FEBS Lett , vol.434 , pp. 357-361
    • Dolenc, I.1    Seemüller, E.2    Baumeister, W.3
  • 32
    • 0031927996 scopus 로고    scopus 로고
    • 26S proteasome structure revealed by three-dimensional electron microscopy
    • Single-particle three-dimensional electron microscopy provided the first insights into the structural organization of the 19S regulatory complex. Image analysis reveals a weak flexible linkage between the regulatory complex and the proteolytic core.
    • Walz J., Erdmann A., Kania M., Typke D., Koster A.J., Baumeister W. 26S proteasome structure revealed by three-dimensional electron microscopy. J Struct Biol. 121:1998;19-29. Single-particle three-dimensional electron microscopy provided the first insights into the structural organization of the 19S regulatory complex. Image analysis reveals a weak flexible linkage between the regulatory complex and the proteolytic core.
    • (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
  • 33
    • 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
    • The dissection of the 19S regulator of the yeast 26S proteasome into 'lid' and 'base' subcomplexes using functional and structural analyses. The lid is essential for the degradation of ubiquitinated substrates, whereas the base is responsible for ATP-dependent degradation.
    • Glickman M.H., Rubin D.M., Coux O., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V.A., 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. The dissection of the 19S regulator of the yeast 26S proteasome into 'lid' and 'base' subcomplexes using functional and structural analyses. The lid is essential for the degradation of ubiquitinated substrates, whereas the base is responsible for ATP-dependent degradation.
    • (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
  • 36
    • 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 X.W. 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
  • 37
    • 0032993486 scopus 로고    scopus 로고
    • Making sense of the COP9 signalosome
    • Wei N., Deng X-W. Making sense of the COP9 signalosome. Trends Genet. 15:1999;98-103.
    • (1999) Trends Genet , vol.15 , pp. 98-103
    • Wei, N.1    Deng, X.-W.2
  • 38
    • 0032168508 scopus 로고    scopus 로고
    • Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome
    • Mutational analysis in yeast revealed that the proteasomal ATPases function in a nonredundant manner.
    • Rubin D.M., Glickman M.H., Larsen C.N., 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. Mutational analysis in yeast revealed that the proteasomal ATPases function in a nonredundant manner.
    • (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
  • 39
    • 0033176770 scopus 로고    scopus 로고
    • The base of the proteasome regulatory particle exhibits chaperone-like activity
    • Surprisingly, the 19S regulator of the 26S proteasome is shown to refold denatured citrate synthase. This chaperone-like activity is mapped to the base subcomplex of the regulator. The refolding of a substrate protein is opposite to the assumed function of the 19S regulator in unfolding substrate proteins.
    • Braun B.C., 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. Surprisingly, the 19S regulator of the 26S proteasome is shown to refold denatured citrate synthase. This chaperone-like activity is mapped to the base subcomplex of the regulator. The refolding of a substrate protein is opposite to the assumed function of the 19S regulator in unfolding substrate proteins.
    • (1999) Nat Cell Biol , vol.1 , pp. 221-226
    • Braun, B.C.1    Glickman, M.2    Kraft, R.3    Dahlmann, B.4    Kloetzel, P.M.5    Finley, D.6    Schmidt, M.7
  • 42
    • 0032850746 scopus 로고    scopus 로고
    • ATP-dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation
    • Murakami Y., Matsufuji S., Hayashi S., Tanahashi N., Tanaka K. ATP-dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation. Mol Cell Biol. 19:1999;7216-7227.
    • (1999) Mol Cell Biol , vol.19 , pp. 7216-7227
    • Murakami, Y.1    Matsufuji, S.2    Hayashi, S.3    Tanahashi, N.4    Tanaka, K.5
  • 44
    • 0033520404 scopus 로고    scopus 로고
    • A 220-kDa activator complex of the 26S proteasome in insects and humans - A role in type II programmed insect muscle cell death and cross-activation of proteasomes from different species
    • Hastings R.A., Eyheralde I., Dawson S.P., Walker G., Reynolds S.E., Billett M.A., Mayer R.J. A 220-kDa activator complex of the 26S proteasome in insects and humans - a role in type II programmed insect muscle cell death and cross-activation of proteasomes from different species. J Biol Chem. 274:1999;25691-25700.
    • (1999) J Biol Chem , vol.274 , pp. 25691-25700
    • Hastings, R.A.1    Eyheralde, I.2    Dawson, S.P.3    Walker, G.4    Reynolds, S.E.5    Billett, M.A.6    Mayer, R.J.7
  • 45
    • 0032530241 scopus 로고    scopus 로고
    • Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity
    • Adams G.M., Crotchett B., Slaughter C.A., DeMartino G.N., Gogol E.P. Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity. Biochemistry. 37:1998;12927-12932.
    • (1998) Biochemistry , vol.37 , pp. 12927-12932
    • Adams, G.M.1    Crotchett, B.2    Slaughter, C.A.3    DeMartino, G.N.4    Gogol, E.P.5
  • 46
    • 0028985861 scopus 로고
    • Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel T., Baumeister W. Conformational constraints in protein degradation by the 20S proteasome. Nat Struct Biol. 2:1995;199-204.
    • (1995) Nat Struct Biol , vol.2 , pp. 199-204
    • Wenzel, T.1    Baumeister, W.2
  • 47
    • 0033543648 scopus 로고    scopus 로고
    • An archaebacterial ATPase, homologous to the ATPases in the eukaryotic 26S proteasome, activates protein breakdown by the 20S proteasome
    • The first characterization of an archaebacterial regulatory nucleotidase complex that stimulates protein breakdown by archaeal proteasomes.
    • Zwickl P., Ng D., Woo K.M., Klenk H-P., Goldberg A.L. An archaebacterial ATPase, homologous to the ATPases in the eukaryotic 26S proteasome, activates protein breakdown by the 20S proteasome. J Biol Chem. 274:1999;26008-26014. The first characterization of an archaebacterial regulatory nucleotidase complex that stimulates protein breakdown by archaeal proteasomes.
    • (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
  • 50
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst M., Wendland B., Estepa E.J., Emr S.D. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:1998;2982-2993.
    • (1998) EMBO J , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 51
    • 0033595814 scopus 로고    scopus 로고
    • Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin
    • Hartman J.J., Vale R.D. Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin. Science. 286:1999;782-785.
    • (1999) Science , vol.286 , pp. 782-785
    • Hartman, J.J.1    Vale, R.D.2
  • 52
    • 0032825282 scopus 로고    scopus 로고
    • The Janus face of the archaeal Cdc48/p97 homologue VAT: Protein folding versus unfolding
    • Golbik R., Lupas A.N., Koretke K.K., Baumeister W., Peters J. The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding. Biol Chem. 380:1999;1049-1062.
    • (1999) Biol Chem , vol.380 , pp. 1049-1062
    • Golbik, R.1    Lupas, A.N.2    Koretke, K.K.3    Baumeister, W.4    Peters, J.5
  • 53
    • 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., Roth R., Morisaki H., Jahn R., Heuser J.E. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:1997;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
  • 54
    • 0032909548 scopus 로고    scopus 로고
    • Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography
    • Rockel B., Walz J., Hegerl R., Peters J., Typke D., Baumeister W. Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography. FEBS Lett. 451:1999;27-32.
    • (1999) FEBS Lett , vol.451 , pp. 27-32
    • Rockel, B.1    Walz, J.2    Hegerl, R.3    Peters, J.4    Typke, D.5    Baumeister, W.6
  • 55
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • ••]. The fold of the protomers revealed a nucleotide-binding domain with a Rossmann fold and a helical domain.
    • ••]. The fold of the protomers revealed a nucleotide-binding domain with a Rossmann fold and a helical domain.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 59
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman S., Wickner S., Maurizi M.R. Protein quality control. triage by chaperones and proteases Genes Dev. 11:1997;815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 60
    • 0033536010 scopus 로고    scopus 로고
    • Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits
    • This structural study of Lon protease from yeast by electron microscopy and analytical ultracentrifugation supports the view that this enzyme, with covalently linked protease and ATPase domains, forms a flexible heptameric ring.
    • Stahlberg H., Kutejova E., Suda K., Wolpensinger B., Lustig A., Schatz G., Engel A., Suzuki C.K. Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits. Proc Natl Acad Sci USA. 96:1999;6787-6790. This structural study of Lon protease from yeast by electron microscopy and analytical ultracentrifugation supports the view that this enzyme, with covalently linked protease and ATPase domains, forms a flexible heptameric ring.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6787-6790
    • Stahlberg, H.1    Kutejova, E.2    Suda, K.3    Wolpensinger, B.4    Lustig, A.5    Schatz, G.6    Engel, A.7    Suzuki, C.K.8
  • 61
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome
    • Kessel M., Maurizi M.R., Kim B., Kocsis E., Trus B.L., Singh S.K., Steven A.C. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome. J Mol Biol. 250:1995;587-594.
    • (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, S.K.6    Steven, A.C.7
  • 62
    • 0029147711 scopus 로고
    • Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore
    • Flanagan J.M., Wall J.S., Capel M.S., Schneider D.K., Shanklin J. Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore. Biochemistry. 34:1995;10910-10917.
    • (1995) Biochemistry , vol.34 , pp. 10910-10917
    • Flanagan, J.M.1    Wall, J.S.2    Capel, M.S.3    Schneider, D.K.4    Shanklin, J.5
  • 64
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang J., Hartling J.A., Flanagan J.M. 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
  • 65
    • 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
  • 66
    • 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 ClpP but not ATP hydrolysis
    • Thompson M.W., Singh S.K., Maurizi M.R. Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli- requirement for the multiple array of active-sites in ClpP but not ATP hydrolysis. J Biol Chem. 269:1994;18209-18215.
    • (1994) J Biol Chem , vol.269 , pp. 18209-18215
    • Thompson, M.W.1    Singh, S.K.2    Maurizi, M.R.3
  • 67
    • 0033178790 scopus 로고    scopus 로고
    • Comparative sequence analysis of the DNA packaging, head, and tail morphogenesis modules in the temperate cos-site Streptococcus thermophilus bacteriophage Sfi21
    • Desiere F., Lucchini S., Brüssow H. Comparative sequence analysis of the DNA packaging, head, and tail morphogenesis modules in the temperate cos-site Streptococcus thermophilus bacteriophage Sfi21. Virology. 260:1999;244-253.
    • (1999) Virology , vol.260 , pp. 244-253
    • Desiere, F.1    Lucchini, S.2    Brüssow, H.3
  • 68
    • 0032725193 scopus 로고    scopus 로고
    • Cloning and analysis of the capsid morphogenesis genes of Pseudomonas aeruginosa bacteriophage D3: Another example of protein chain mail?
    • Gilakjan Z.A., Kropinski A.M. Cloning and analysis of the capsid morphogenesis genes of Pseudomonas aeruginosa bacteriophage D3: another example of protein chain mail? J Bacteriol. 181:1999;7221-7227.
    • (1999) J Bacteriol , vol.181 , pp. 7221-7227
    • Gilakjan, Z.A.1    Kropinski, A.M.2
  • 69
    • 0032958485 scopus 로고    scopus 로고
    • Alteration of the synthesis of the Clp ATP-dependent protease affects morphological and physiological differentiation in Streptomyces
    • de Crecy-Lagard V., Servant-Moisson P., Viala J., Grandvalet C., Mazodier P. Alteration of the synthesis of the Clp ATP-dependent protease affects morphological and physiological differentiation in Streptomyces. Mol Microbiol. 32:1999;505-517.
    • (1999) Mol Microbiol , vol.32 , pp. 505-517
    • De Crecy-Lagard, V.1    Servant-Moisson, P.2    Viala, J.3    Grandvalet, C.4    Mazodier, P.5
  • 71
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • This paper presents a cryo-electron microscopy reconstruction of ClpA, a two-domain ATPase, that reveals an internal compartment enclosed between two hexameric rings. It draws on the crystal structure of the double-heptamer protease ClpP [64] to determine their docking. A rotational model of processive substrate processing is suggested.
    • Beuron F., Maurizi M.R., Belnap D.M., Kocsis E., Booy F.P., Kessel M., Steven A.C. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J Struct Biol. 124:1998;179-188. This paper presents a cryo-electron microscopy reconstruction of ClpA, a two-domain ATPase, that reveals an internal compartment enclosed between two hexameric rings. It draws on the crystal structure of the double-heptamer protease ClpP [64] to determine their docking. A rotational model of processive substrate processing is suggested.
    • (1998) J Struct Biol , vol.124 , pp. 179-188
    • 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
  • 72
    • 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 A.C., Maurizi M.R. 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
  • 74
    • 0033535955 scopus 로고    scopus 로고
    • Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
    • The homologous SSD (sensor and substrate discrimination) sequences of five ATP-dependent bacterial proteases were expressed in E. coli. Three of them were demonstrated to assume compact folds, providing support for the hypothesis that SSD sequences correspond to discrete domains. The binding of ssrA-tagged substrates by these domains was found to be partially selective.
    • Smith C.K., Baker T.A., Sauer R.T. Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proc Natl Acad Sci USA. 96:1999;6678-6682. The homologous SSD (sensor and substrate discrimination) sequences of five ATP-dependent bacterial proteases were expressed in E. coli. Three of them were demonstrated to assume compact folds, providing support for the hypothesis that SSD sequences correspond to discrete domains. The binding of ssrA-tagged substrates by these domains was found to be partially selective.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6678-6682
    • Smith, C.K.1    Baker, T.A.2    Sauer, R.T.3
  • 75
    • 0032431025 scopus 로고    scopus 로고
    • Formation of the preprimosome protects λ O from RNA transcription-dependent proteolysis by ClpP/ClpX
    • Zylicz M., Liberek K., Wawrzynow A., Georgopoulos C. Formation of the preprimosome protects λ O from RNA transcription-dependent proteolysis by ClpP/ClpX. Proc Natl Acad Sci USA. 95:1998;15259-15263.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15259-15263
    • Zylicz, M.1    Liberek, K.2    Wawrzynow, A.3    Georgopoulos, C.4
  • 77
    • 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
    • The authors exploited specific point mutations in the ATPase ClpA to study its interaction with the model substrate RepA, distinguishing the roles of its two ATPase domains in substrate binding and the dual roles of ClpA in either unfolding alone or unfolding as an activity in protein degradation.
    • Pak M., Hoskins J.R., Singh S.K., Maurizi M.R., 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. The authors exploited specific point mutations in the ATPase ClpA to study its interaction with the model substrate RepA, distinguishing the roles of its two ATPase domains in substrate binding and the dual roles of ClpA in either unfolding alone or unfolding as an activity in protein degradation.
    • (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
  • 78
    • 0033539690 scopus 로고    scopus 로고
    • ClpA and ClpP remain associated during multiple rounds of ATP dependent protein degradation by ClpAP protease
    • Singh S.K., Guo F.S., Maurizi M.R. ClpA and ClpP remain associated during multiple rounds of ATP dependent protein degradation by ClpAP protease. Biochemistry. 38:1999;14906-14915.
    • (1999) Biochemistry , vol.38 , pp. 14906-14915
    • Singh, S.K.1    Guo, F.S.2    Maurizi, M.R.3
  • 79
    • 0031961776 scopus 로고    scopus 로고
    • Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition
    • Jones J.M., Welty D.J., Nakai H. Versatile action of Escherichia coli ClpXP as protease or molecular chaperone for bacteriophage Mu transposition. J Biol Chem. 273:1998;459-465.
    • (1998) J Biol Chem , vol.273 , pp. 459-465
    • Jones, J.M.1    Welty, D.J.2    Nakai, H.3
  • 80
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • The unfolding of substrates by ClpA in the absence of proteolysis was demonstrated in a fluorescence assay using ssrA-tagged green fluorescent protein as a substrate. The substrate was stabilized in the unfolded state by being subsequently bound to a modified chaperone.
    • Weber-Ban E.U., Reid B.G., Miranker A.D., Horwich A.L. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 401:1999;90-93. The unfolding of substrates by ClpA in the absence of proteolysis was demonstrated in a fluorescence assay using ssrA-tagged green fluorescent protein as a substrate. The substrate was stabilized in the unfolded state by being subsequently bound to a modified chaperone.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 81
    • 0343811707 scopus 로고    scopus 로고
    • The bacteriophage φ29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution
    • Müller D.J., Engel A., Carrascosa J.L., Velez M. The bacteriophage φ29 head-tail connector imaged at high resolution with the atomic force microscope in buffer solution. EMBO J. 16:1997;2547-2553.
    • (1997) EMBO J , vol.16 , pp. 2547-2553
    • Müller, D.J.1    Engel, A.2    Carrascosa, J.L.3    Velez, M.4
  • 82
    • 0032516784 scopus 로고    scopus 로고
    • Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage φ29 connector particle
    • Guasch A., Pous J., Parraga A., Valpuesta J.M., Carrascosa J.L., Coll M. Crystallographic analysis reveals the 12-fold symmetry of the bacteriophage φ29 connector particle. J Mol Biol. 281:1998;219-225.
    • (1998) J Mol Biol , vol.281 , pp. 219-225
    • Guasch, A.1    Pous, J.2    Parraga, A.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Coll, M.6
  • 83
    • 0027418576 scopus 로고
    • The portal protein of bacteriophage SPP1: A DNA pump with 13-fold symmetry
    • Dube P., Tavares P., Lurz R., van Heel M. The portal protein of bacteriophage SPP1. a DNA pump with 13-fold symmetry EMBO J. 12:1993;1303-1309.
    • (1993) EMBO J , vol.12 , pp. 1303-1309
    • Dube, P.1    Tavares, P.2    Lurz, R.3    Van Heel, M.4
  • 84
    • 0029360470 scopus 로고
    • Improved methods for determination of rotational symmetries in macromolecules
    • Kocsis E., Cerritelli M.E., Trus B.L., Cheng N., Steven A.C. Improved methods for determination of rotational symmetries in macromolecules. Ultramicroscopy. 60:1995;219-228.
    • (1995) Ultramicroscopy , vol.60 , pp. 219-228
    • Kocsis, E.1    Cerritelli, M.E.2    Trus, B.L.3    Cheng, N.4    Steven, A.C.5
  • 85
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 370:1994;621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 86
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • Rastogi V.K., Girvin M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 402:1999;263-268.
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 87
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D., Leslie A.G.W., Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science. 286:1999;1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 88
    • 0016853664 scopus 로고
    • A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport
    • Boyer P.D. A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport. FEBS Lett. 58:1975;1-6.
    • (1975) FEBS Lett , vol.58 , pp. 1-6
    • Boyer, P.D.1
  • 89
    • 0039538633 scopus 로고
    • Symmetry mismatch and DNA packaging in large bacteriophages
    • Hendrix R.W. Symmetry mismatch and DNA packaging in large bacteriophages. Proc Natl Acad Sci USA. 75:1978;4779-4783.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4779-4783
    • Hendrix, R.W.1
  • 90
    • 0030934380 scopus 로고    scopus 로고
    • Direct, observation of the rotation of F1-ATPase.
    • Noji H., Yasuda R., Yoshida M., Kinosita K. Jr. Direct, observation of the rotation of F1-ATPase., Nature. 386:1997;299-302.
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita K., Jr.4
  • 93
    • 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
  • 94
    • 0034677361 scopus 로고    scopus 로고
    • The structures of HslU and the ATP-dependent protease HslU-HslV
    • Crystal structures of the HslU ATPase in its free form and in complex with the HslV protease were determined. In both structures, the HslU ATPase has a sixfold symmetry, as does the HslV protease, suggesting that a symmetry mismatch is nonexistent in the HslUV protease.
    • Bochtler M., Hartmann C., Song H.K., Bourenkov G.P., Bartunik H.D., Huber R. The structures of HslU and the ATP-dependent protease HslU-HslV. Nature. 403:2000;800-806. Crystal structures of the HslU ATPase in its free form and in complex with the HslV protease were determined. In both structures, the HslU ATPase has a sixfold symmetry, as does the HslV protease, suggesting that a symmetry mismatch is nonexistent in the HslUV protease.
    • (2000) Nature , vol.403 , pp. 800-806
    • Bochtler, M.1    Hartmann, C.2    Song, H.K.3    Bourenkov, G.P.4    Bartunik, H.D.5    Huber, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.