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Volumn 12, Issue 2, 2003, Pages 365-372

Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALANYLALANYLASPARAGINYLASPARTYLGLUTAMYLASPARAGINYLTYROSYLALANYLLEUCYLALANYL ALANINE; AMINO ACID; BACTERIAL PROTEIN; CARRIER PROTEIN; CARRIER PROTEIN SSPB; DIMER; INTEGRASE; MONOMER; PROTEIN SUBUNIT; RIBONUCLEOPROTEIN; UNCLASSIFIED DRUG;

EID: 0141992126     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2003.08.014     Document Type: Article
Times cited : (83)

References (50)
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: (Collaborative Computational Project 4) programs for protein crystallography
    • CCP4 The CCP4 suite. (Collaborative Computational Project 4) programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 5
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • a
    • Dougan D.A., Mogk A., Zeth K., Turgay K., Bukau B. AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett. 529:2002;6-10. a.
    • (2002) FEBS Lett. , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 6
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • b
    • Dougan D.A., Reid B.G., Horwich A.L., Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell. 9:2002;673-683. b.
    • (2002) Mol. Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 8
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman S., Roche E., Zhou Y., Sauer R.T. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12:1998;1338-1347.
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 9
    • 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
  • 10
    • 0037195961 scopus 로고    scopus 로고
    • Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA
    • Guo F., Esser L., Singh S.K., Maurizi M.R., Xia D. Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. J. Biol. Chem. 277:2002;46753-46762.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46753-46762
    • Guo, F.1    Esser, L.2    Singh, S.K.3    Maurizi, M.R.4    Xia, D.5
  • 14
    • 0034255124 scopus 로고    scopus 로고
    • Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
    • Hoskins J.R., Singh S.K., Maurizi M.R., Wickner S. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. Proc. Natl. Acad. Sci. USA. 97:2000;8892-8897.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8892-8897
    • Hoskins, J.R.1    Singh, S.K.2    Maurizi, M.R.3    Wickner, S.4
  • 15
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones A.T., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystrallogr. A. 47:1991;110-119.
    • (1991) Acta Crystrallogr. A , vol.47 , pp. 110-119
    • Jones, A.T.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0034046020 scopus 로고    scopus 로고
    • The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue
    • Karzai A.W., Roche E.D., Sauer R.T. The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue. Nat. Struct. Biol. 7:2000;449-455.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 449-455
    • Karzai, A.W.1    Roche, E.D.2    Sauer, R.T.3
  • 17
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler K.C., Waller P.R., Sauer R.T. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science. 271:1996;990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 18
    • 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
  • 19
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim Y.I., Burton R.E., Burton B.M., Sauer R.T., Baker T.A. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell. 5:2000;639-648.
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 21
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko I., Luo L., Baker T.A. 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
  • 22
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko I., Seidel M., Sauer R.T., Baker T.A. A specificity-enhancing factor for the ClpXP degradation machine. Science. 289:2000;2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 24
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian Ufd1 and Npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G. A complex of mammalian Ufd1 and Npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19:2000;2181-2192.
    • (2000) EMBO J. , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 25
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An Automated Molecular Replacement Program Package
    • C.W. Carter, & R.M. Sweet. San Diego: Academic Press
    • Navaza J., Saludjian P. AMoRe. An Automated Molecular Replacement Program Package Carter C.W., Sweet R.M. Macromolecular Crystallography, Part A. 1997;Academic Press, San Diego., pp. 581-594.
    • (1997) Macromolecular Crystallography, Part A , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 26
    • 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., Aravind L., Spouge J.L., Koonin E.V. 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
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T., Wilkinson A.J. AAA+ superfamily ATPases. common structure-diverse function Genes Cells. 6:2001;575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 29
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega J., Singh S.K., Ishikawa T., Maurizi M.R., Steven A.C. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell. 6:2000;1515-1521.
    • (2000) Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 30
    • 0037119954 scopus 로고    scopus 로고
    • Alternating translocation of protein substrates from both ends of ClpXP protease
    • Ortega J., Lee H.S., Maurizi M.R., Steven A.C. Alternating translocation of protein substrates from both ends of ClpXP protease. EMBO J. 21:2002;4938-4949.
    • (2002) EMBO J. , vol.21 , pp. 4938-4949
    • Ortega, J.1    Lee, H.S.2    Maurizi, M.R.3    Steven, A.C.4
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray Diffraction Data Collected in Oscillation Mode
    • C.W. Carter, & R.M. Sweet. San Diego: Academic Press. 307-326.pp
    • Otwinowski Z., Minor W. Processing of X-ray Diffraction Data Collected in Oscillation Mode. Carter C.W., Sweet R.M. Macromolecular Crystallography, Part A. 1997;Academic Press, San Diego. 307-326.pp.
    • (1997) Macromolecular Crystallography, Part A
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0030804951 scopus 로고    scopus 로고
    • The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase
    • Seol J.H., Yoo S.J., Shin D.H., Shim Y.K., Kang M.S., Goldberg A.L., Chung C.H. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. Eur. J. Biochem. 247:1997;1143-1150.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1143-1150
    • Seol, J.H.1    Yoo, S.J.2    Shin, D.H.3    Shim, Y.K.4    Kang, M.S.5    Goldberg, A.L.6    Chung, C.H.7
  • 35
    • 0034698280 scopus 로고    scopus 로고
    • The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli
    • Seong I.S., Oh J.Y., Lee J.W., Tanaka K., Chung C.H. The HslU ATPase acts as a molecular chaperone in prevention of aggregation of SulA, an inhibitor of cell division in Escherichia coli. FEBS Lett. 477:2000;224-229.
    • (2000) FEBS Lett. , vol.477 , pp. 224-229
    • Seong, I.S.1    Oh, J.Y.2    Lee, J.W.3    Tanaka, K.4    Chung, C.H.5
  • 38
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome. a molecular machine designed for controlled proteolysis Annu. Rev. Biochem. 68:1999;1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 39
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah D.A., Levchenko I., Baker T.A., Sauer R.T. Characterization of a specificity factor for an AAA+ ATPase. assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer Chem. Biol. 9:2002;1237-1245.
    • (2002) Chem. Biol. , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 40
    • 0141888401 scopus 로고    scopus 로고
    • Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease
    • Wah D.A., Levchenko I., Rieckhof G.E., Bolon D.N., Baker T.A., Sauer R.T. Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. Mol. Cell. 12:2003;355-363., this issue.
    • (2003) Mol. Cell , vol.12 , Issue.THIS ISSUE , pp. 355-363
    • Wah, D.A.1    Levchenko, I.2    Rieckhof, G.E.3    Bolon, D.N.4    Baker, T.A.5    Sauer, R.T.6
  • 41
    • 0028922586 scopus 로고
    • Ligplot: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., Thornton J.M. Ligplot. a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8:1995;127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 42
    • 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., Wojtkowiak D., Marszalek J., Banecki B., Jonsen M., Graves B., Georgopoulos C., Zylicz M. 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. 14:1995;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
  • 43
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • 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.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 45
    • 0032968207 scopus 로고    scopus 로고
    • C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death
    • Wu D., Chen P.J., Chen S., Hu Y., Nunez G., Ellis R.E. C. elegans MAC-1, an essential member of the AAA family of ATPases, can bind CED-4 and prevent cell death. Development. 126:1999;2021-2031.
    • (1999) Development , vol.126 , pp. 2021-2031
    • Wu, D.1    Chen, P.J.2    Chen, S.3    Hu, Y.4    Nunez, G.5    Ellis, R.E.6
  • 46
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y., Meyer H.H., Rapoport T.A. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 414:2001;652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 47
    • 0036896886 scopus 로고    scopus 로고
    • Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
    • Zeth K., Ravelli R.B., Paal K., Cusack S., Bukau B., Dougan D.A. Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat. Struct. Biol. 9:2002;906-911.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 906-911
    • Zeth, K.1    Ravelli, R.B.2    Paal, K.3    Cusack, S.4    Bukau, B.5    Dougan, D.A.6
  • 48
    • 0031884182 scopus 로고    scopus 로고
    • Regulation of proteolysis of the stationary-phase sigma factor RpoS
    • Zhou Y., Gottesman S. Regulation of proteolysis of the stationary-phase sigma factor RpoS. J. Bacteriol. 180:1998;1154-1158.
    • (1998) J. Bacteriol. , vol.180 , pp. 1154-1158
    • Zhou, Y.1    Gottesman, S.2
  • 50
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 274:1999;28083-28086.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


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