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Volumn 148, Issue 3, 2004, Pages 338-352

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP

Author keywords

ATP dependent protease; Clp Hsp100; Mitochondrial ClpP; X ray crystallography

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; CHAPERONE; ENDOPEPTIDASE CLP; PEPTIDE; PROTEIN SUBUNIT;

EID: 7444254844     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.07.004     Document Type: Article
Times cited : (93)

References (42)
  • 1
    • 0027412196 scopus 로고
    • ALSCRIPT-a tool to format multiple sequence alignments
    • G.J. Barton ALSCRIPT-a tool to format multiple sequence alignments Protein Eng. 6 1993 37 40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 2
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • F. Beuron, M.R. Maurizi, D.M. Belnap, E. Kocsis, F.P. Booy, and M. Kessel At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease J. Struct. Biol. 123 1998 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
  • 3
    • 0030925223 scopus 로고    scopus 로고
    • Crystal structure of heat shock locus V (HslV) from Escherichia coli
    • M. Bochtler, L. Ditzel, M. Groll, and R. Huber 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
  • 4
    • 0029620843 scopus 로고
    • Human ClpP protease: CDNA sequence, tissue-specific expression and chromosomal assignment of the gene
    • P. Bross, B.S. Andresen, I. Knudsen, T.A. Kruse, and N. Gregersen Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene FEBS Lett. 377 1995 249 252
    • (1995) FEBS Lett. , vol.377 , pp. 249-252
    • Bross, P.1    Andresen, B.S.2    Knudsen, I.3    Kruse, T.A.4    Gregersen, N.5
  • 6
    • 0037407940 scopus 로고    scopus 로고
    • Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing
    • R.E. Burton, T.A. Baker, and R.T. Sauer Energy-dependent degradation: linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing Protein Sci. 12 2003 893 902
    • (2003) Protein Sci. , vol.12 , pp. 893-902
    • Burton, R.E.1    Baker, T.A.2    Sauer, R.T.3
  • 7
    • 0035875890 scopus 로고    scopus 로고
    • Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
    • R.E. Burton, S.M. Siddiqui, Y.I. Kim, T.A. Baker, and R.T. Sauer Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine EMBO J. 20 2001 3092 3100
    • (2001) EMBO J. , vol.20 , pp. 3092-3100
    • Burton, R.E.1    Siddiqui, S.M.2    Kim, Y.I.3    Baker, T.A.4    Sauer, R.T.5
  • 8
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • CCP4, Collaborative Computing Project Number 4
    • CCP4, 1994. Collaborative Computing Project Number 4. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 10
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • S. Gottesman Proteolysis in bacterial regulatory circuits Annu. Rev. Cell Dev. Biol. 19 2003 565 587
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 11
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • S. Gottesman, S. Wickner, and M.R. Maurizi 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
  • 12
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • R. Grimaud, M. Kessel, F. Beuron, A.C. Steven, and M.R. Maurizi 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
  • 14
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • F. Guo, M.R. Maurizi, L. Esser, and D. Xia Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease J. Biol. Chem. 277 2002 46743 46752
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 15
    • 0035039711 scopus 로고    scopus 로고
    • Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease
    • T. Halperin, B. Zheng, H. Itzhaki, A.K. Clarke, and Z. Adam Plant mitochondria contain proteolytic and regulatory subunits of the ATP-dependent Clp protease Plant Mol. Biol. 45 2001 461 468
    • (2001) Plant Mol. Biol. , vol.45 , pp. 461-468
    • Halperin, T.1    Zheng, B.2    Itzhaki, H.3    Clarke, A.K.4    Adam, Z.5
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0037036431 scopus 로고    scopus 로고
    • Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP
    • S.G. Kang, J. Ortega, S.K. Singh, N. Wang, N.N. Huang, A.C. Steven, and M.R. Maurizi Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP J. Biol. Chem. 277 2002 21095 21102
    • (2002) J. Biol. Chem. , vol.277 , pp. 21095-21102
    • Kang, S.G.1    Ortega, J.2    Singh, S.K.3    Wang, N.4    Huang, N.N.5    Steven, A.C.6    Maurizi, M.R.7
  • 19
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • J.A. Kenniston, T.A. Baker, J.M. Fernandez, and R.T. Sauer Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine Cell 114 2003 511 520
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 20
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli ClpAP protease and the eukaryotic a26 S proteasome
    • M. Kessel, M.R. Maurizi, B. Kim, E. Kocsis, B.L. Trus, S.K. Singh, and A.C. Steven Homology in structural organization between E. coli ClpAP protease and the eukaryotic a26 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
  • 21
    • 0348010311 scopus 로고    scopus 로고
    • Crystal structure of ClpX molecular chaperone from Helicobacter pylori
    • D.Y. Kim, and K.K. Kim Crystal structure of ClpX molecular chaperone from Helicobacter pylori J. Biol. Chem. 278 2003 50664 50670
    • (2003) J. Biol. Chem. , vol.278 , pp. 50664-50670
    • Kim, D.Y.1    Kim, K.K.2
  • 22
    • 0030501419 scopus 로고    scopus 로고
    • Use of non-crystallographic symmetry in protein structure refinement
    • G.J. Kleywegt Use of non-crystallographic symmetry in protein structure refinement Acta Crystallogr. D 52 1996 842 857
    • (1996) Acta Crystallogr. D , vol.52 , pp. 842-857
    • Kleywegt, G.J.1
  • 23
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • G.J. Kleywegt, and R.J. Read Not your average density Structure 1997 1557 1569
    • (1997) Structure , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT-a program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT-a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 26
    • 0029042511 scopus 로고
    • Crystal structure of the a20S proteasome from the archaeon T. acidophilum at 3.4 a resolution
    • J. Lowe, D. Stock, B. Jap, P. Zwickl, W. Baumeister, and R. Huber Crystal structure of the a20S proteasome from the archaeon T. acidophilum at 3.4 A resolution Science 268 1995 533 539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 28
    • 0025358672 scopus 로고
    • Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli
    • M.R. Maurizi, W.P. Clark, Y. Katayama, S. Rudikoff, J. Pumphrey, B. Bowers, and S. Gottesman Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli J. Biol. Chem. 265 1990 12536 12545
    • (1990) J. Biol. Chem. , vol.265 , pp. 12536-12545
    • Maurizi, M.R.1    Clark, W.P.2    Katayama, Y.3    Rudikoff, S.4    Pumphrey, J.5    Bowers, B.6    Gottesman, S.7
  • 29
    • 0025323156 scopus 로고
    • Clp P represents a unique family of serine proteases
    • M.R. Maurizi, W.P. Clark, S.H. Kim, and S. Gottesman Clp P represents a unique family of serine proteases J. Biol. Chem. 265 1990 12546 12552
    • (1990) J. Biol. Chem. , vol.265 , pp. 12546-12552
    • Maurizi, M.R.1    Clark, W.P.2    Kim, S.H.3    Gottesman, S.4
  • 30
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 525
    • (1997) Methods Enzymol. , vol.277 , pp. 505-525
    • Merritt, E.A.1    Bacon, D.J.2
  • 31
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • J. Navaza, and P. Saludjian aMoRe: an automated molecular replacement program package Methods Enzymol. 276 1997 581 594
    • (1997) Methods Enzymol. , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 32
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • A.F. Neuwald, L. Aravind, J.L. Spouge, and E.V. Koonin 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
  • 33
    • 0026319199 scopus 로고
    • Protein folding association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Hoing Protein folding association: insights from the interfacial and thermodynamic properties of hydrocarbons Protein Eng. 11 1991 281 296
    • (1991) Protein Eng. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Hoing, B.3
  • 34
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • J. Ortega, S.K. Singh, T. Ishikawa, M.R. Maurizi, and A.C. Steven 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
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collecting in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collecting in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0036068418 scopus 로고    scopus 로고
    • The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus
    • J. Schelin, F. Lindmark, and A.K. Clarke The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus Microbiology 148 2002 2255 2265
    • (2002) Microbiology , vol.148 , pp. 2255-2265
    • Schelin, J.1    Lindmark, F.2    Clarke, A.K.3
  • 38
    • 0033539690 scopus 로고    scopus 로고
    • ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease
    • S.K. Singh, F. Guo, and M.R. Maurizi 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.2    Maurizi, M.R.3
  • 39
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HslUV protease-chaperone complex
    • M.C. Sousa, C.B. Trame, H. Tsuruta, S.M. Wilbanks, V.S. Reddy, and D. McKay Crystal and solution structures of an HslUV protease-chaperone complex Cell 103 2000 633 643
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1    Trame, C.B.2    Tsuruta, H.3    Wilbanks, S.M.4    Reddy, V.S.5    McKay, D.6
  • 40
    • 0028305742 scopus 로고
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates
    • M.W. Thompson, and M.R. Maurizi Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates J. Biol. Chem. 269 1994 18201 18208
    • (1994) J. Biol. Chem. , vol.269 , pp. 18201-18208
    • Thompson, M.W.1    Maurizi, M.R.2
  • 41
    • 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
    • M.W. Thompson, S.K. Singh, and M.R. Maurizi 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
  • 42
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 a resolution suggests a model for ATP-dependent proteolysis
    • J. Wang, J.A. Hartling, and J.M. Flanagan The structure of ClpP at 2.3 A 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


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