메뉴 건너뛰기




Volumn 292, Issue 4, 1999, Pages 819-825

Mitochondrial localization and oligomeric structure of HClpP, the human homologue of E. coli ClpP

Author keywords

ClpP; Mammalian; Mitochondria; Protease; Rotational symmetry

Indexed keywords

CELL PROTEIN; MUTANT PROTEIN; OLIGOMER; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 0033214148     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3121     Document Type: Article
Times cited : (39)

References (28)
  • 1
    • 0027707099 scopus 로고
    • Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing
    • Arizti P., Arribas J., Casta ñ J. G. Modulation of the multicatalytic proteinase complex by lipids, interconversion and proteolytic processing. Enzyme Protein. 47:1993;285-295.
    • (1993) Enzyme Protein , vol.47 , pp. 285-295
    • Arizti, P.1    Arribas, J.2    Casta Ñ., J.G.3
  • 2
    • 0027382271 scopus 로고
    • A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP fromEscherichia coli
    • Arribas J., Casta ñ J. G. A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP fromEscherichia coli. J. Biol. Chem. 268:1993;21165-21171.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21165-21171
    • Arribas, J.1    Casta Ñ., J.G.2
  • 3
    • 0026011789 scopus 로고
    • Autoantibodies against the multicatalytic proteinase in patients with systemic lupus erythematosus
    • Arribas J., Luz-Rodriguez M., Alvarez-Do-Forno R., Casta ñ J. G. Autoantibodies against the multicatalytic proteinase in patients with systemic lupus erythematosus. J. Exp. Med. 173:1991;423-427.
    • (1991) J. Exp. Med. , vol.173 , pp. 423-427
    • Arribas, J.1    Luz-Rodriguez, M.2    Alvarez-Do-Forno, R.3    Casta Ñ., J.G.4
  • 4
    • 0028287522 scopus 로고
    • Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex
    • Arribas J., Arizti P., Casta ñ J. G. Antibodies against the C2 COOH-terminal region discriminate the active and latent forms of the multicatalytic proteinase complex. J. Biol. Chem. 269:1994;12858-12864.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12858-12864
    • Arribas, J.1    Arizti, P.2    Casta Ñ., J.G.3
  • 5
    • 0029620843 scopus 로고
    • Human ClpP protease: CDNA sequence, tissue-specific expression and chromosomal assignment of the gene
    • Bross P., Andresen B. S., Knudsen L., Kruse T. A., Gregersen N. Human ClpP protease: CDNA sequence, tissue-specific expression and chromosomal assignment of the gene. FEBS Letters. 377:1995;249-252.
    • (1995) FEBS Letters , vol.377 , pp. 249-252
    • Bross, P.1    Andresen, B.S.2    Knudsen, L.3    Kruse, T.A.4    Gregersen, N.5
  • 6
    • 0029876795 scopus 로고    scopus 로고
    • Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis
    • Casta ñ J. G., Mahillo E., Arizti P., Arribas J. Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis. Biochemistry. 35:1996;3782-3789.
    • (1996) Biochemistry , vol.35 , pp. 3782-3789
    • Casta Ñ., J.G.1    Mahillo, E.2    Arizti, P.3    Arribas, J.4
  • 7
    • 0028535305 scopus 로고
    • Identification and expression of the chloroplast ClpP gene in the conifer Pinus contorta
    • Clarke A. K., Gustafsson P., Lidholm J. A. Identification and expression of the chloroplast ClpP gene in the conifer Pinus contorta. Plant. Mol Biol. 26:1994;851-862.
    • (1994) Plant. Mol Biol. , vol.26 , pp. 851-862
    • Clarke, A.K.1    Gustafsson, P.2    Lidholm, J.A.3
  • 8
    • 0032055408 scopus 로고    scopus 로고
    • A human homologue of Escherichia coli ClpP caseinolytic protease: Recombinant expression, intracellular processing and subcellular localization
    • Corydon T. J., Bross P., Holst H. U., Neve S., Kristiansen K., Gregersen N., Bolund L. A human homologue of Escherichia coli ClpP caseinolytic protease: recombinant expression, intracellular processing and subcellular localization. Biochem. J. 331:1998;309-316.
    • (1998) Biochem. J. , vol.331 , pp. 309-316
    • Corydon, T.J.1    Bross, P.2    Holst, H.U.3    Neve, S.4    Kristiansen, K.5    Gregersen, N.6    Bolund, L.7
  • 9
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:1996;465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 10
    • 0027364289 scopus 로고
    • ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities
    • Gottesman S., Clark W. P., de-Crecy-Lagard V., Maurizi M. R. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J. Biol. Chem. 268:1993;22618-22626.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22618-22626
    • Gottesman, S.1    Clark, W.P.2    De-Crecy-Lagard, V.3    Maurizi, M.R.4
  • 11
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman S., Maurizi M. R., Wickner S. Regulatory subunits of energy-dependent proteases. Cell. 91:1997a;435-438.
    • (1997) Cell , vol.91 , pp. 435-438
    • Gottesman, S.1    Maurizi, M.R.2    Wickner, S.3
  • 12
    • 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. 11:1997b;815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 13
    • 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
  • 14
    • 0023752052 scopus 로고
    • The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component
    • Katayama Y., Gottesman S., Pumphrey J., Rudikoff S., Clark W. P., Maurizi M. R. The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J. Biol. Chem. 263:1988;15226-15236.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15226-15236
    • Katayama, Y.1    Gottesman, S.2    Pumphrey, J.3    Rudikoff, S.4    Clark, W.P.5    Maurizi, M.R.6
  • 15
    • 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
  • 16
    • 0030726159 scopus 로고    scopus 로고
    • Protein translocation channels in the proteasome and other proteases
    • Larsen C. N., Finley D. Protein translocation channels in the proteasome and other proteases. Cell. 91:1997;431-434.
    • (1997) Cell , vol.91 , pp. 431-434
    • Larsen, C.N.1    Finley, D.2
  • 18
    • 0025323156 scopus 로고
    • ClpP represents a unique family of serine proteases
    • Maurizi M. R., Clark W. P., Kim S. H., Gottesman S. ClpP 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
  • 19
    • 0025215224 scopus 로고
    • Transcriptional regulation of rat liver protein disulphide- isomerase gene by insulin and in diabetes
    • Nieto A., Mira E., Casta ñ J. G. Transcriptional regulation of rat liver protein disulphide- isomerase gene by insulin and in diabetes. Biochem. J. 267:1990;317-323.
    • (1990) Biochem. J. , vol.267 , pp. 317-323
    • Nieto, A.1    Mira, E.2    Casta Ñ., J.G.3
  • 21
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of particles embedded in ice
    • Penczek P., Radermacher M., Frank J. Three-dimensional reconstruction of particles embedded in ice. Ultramicroscopy. 40:1992;33-52.
    • (1992) Ultramicroscopy , vol.40 , pp. 33-52
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 22
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • Shanklin J., DeWitt N. D., Flanagan J. M. The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: an archetypal two-component ATP-dependent protease. Plant. Cell. 7:1995;1713-1722.
    • (1995) Plant. Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    Dewitt, N.D.2    Flanagan, J.M.3
  • 23
    • 0028305742 scopus 로고
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates
    • Thompson M. W., Maurizi M. R. 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
  • 24
    • 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
  • 25
    • 0023067967 scopus 로고
    • A new resolution criterion based on the spectral signal-to-noise method ratios
    • Unser M., Trus B. L., Steven A. A new resolution criterion based on the spectral signal-to-noise method ratios. Ultramicroscopy. 23:1987;39-52.
    • (1987) Ultramicroscopy , vol.23 , pp. 39-52
    • Unser, M.1    Trus, B.L.2    Steven, A.3
  • 26
    • 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
  • 27
    • 0032469437 scopus 로고    scopus 로고
    • Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask
    • Wang J., Hartling J. A., Flanagan J. M. Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J. Struct. Biol. 124:1998;151-163.
    • (1998) J. Struct. Biol. , vol.124 , pp. 151-163
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 28
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.