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Volumn 12, Issue 1, 2011, Pages

Assembly and proteolytic processing of mycobacterial ClpP1 and ClpP2

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALANINE; ARGININE; BACTERIAL PROTEIN; PEPTIDASE; PROTEIN CLPP1; PROTEIN CLPP2; RECOMBINANT PROTEIN; SERINE; UNCLASSIFIED DRUG; SERINE PROTEINASE;

EID: 82355182598     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-61     Document Type: Article
Times cited : (24)

References (32)
  • 1
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in Bacterial Regulatory Circuits
    • DOI 10.1146/annurev.cellbio.19.110701.153228
    • Proteolysis in bacterial regulatory circuits. Gottesman S, Annu Rev Cell Dev Biol 2003 19 565 587 (Pubitemid 37487361)
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 2
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • DOI 10.1038/nature02263
    • Protein degradation and protection against misfolded or damaged proteins. Goldberg AL, Nature 2003 426 6968 895 899 (Pubitemid 38056882)
    • (2003) Nature , vol.426 , Issue.6968 , pp. 895-899
    • Goldberg, A.L.1
  • 3
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 A resolution suggests a model for ATP- dependent proteolysis
    • The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Wang J, Hartling JA, Flanagan JM, Cell 1997 91 4 447 456 (Pubitemid 27508234)
    • (1997) Cell , vol.91 , Issue.4 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 4
    • 0028305742 scopus 로고
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates. Thompson MW, Maurizi MR, J Biol Chem 1994 269 27 18201 18208 (Pubitemid 24206221)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.27 , pp. 18201-18208
    • Thompson, M.W.1    Maurizi, M.R.2
  • 5
    • 0024552829 scopus 로고
    • Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides
    • Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides. Woo KM, Chung WJ, Ha DB, Goldberg AL, Chung CH, J Biol Chem 1989 264 4 2088 2091 (Pubitemid 19057677)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.4 , pp. 2088-2091
    • Woo, K.M.1    Chung, W.J.2    Ha, D.B.3    Goldberg, A.L.4    Chung, C.H.5
  • 6
    • 71749085013 scopus 로고    scopus 로고
    • Clp chaperone-proteases: Structure and function
    • Clp chaperone-proteases: structure and function. Kress W, Maglica Z, Weber-Ban E, Res Microbiol 2009 160 9 618 628
    • (2009) Res Microbiol , vol.160 , Issue.9 , pp. 618-628
    • Kress, W.1    Maglica, Z.2    Weber-Ban, E.3
  • 8
    • 0031939281 scopus 로고    scopus 로고
    • Mechanisms of latency in Mycobacterium tuberculosis
    • DOI 10.1016/S0966-842X(98)01216-5, PII S0966842X98012165
    • Mechanisms of latency in Mycobacterium tuberculosis. Parrish NM, Dick JD, Bishai WR, Trends Microbiol 1998 6 3 107 112 (Pubitemid 28123330)
    • (1998) Trends in Microbiology , vol.6 , Issue.3 , pp. 107-112
    • Parrish, N.M.1    Dick, J.D.2    Bishai, W.R.3
  • 9
    • 0036165063 scopus 로고    scopus 로고
    • A phagosome of one's own: A microbial guide to life in the macrophage
    • DOI 10.1016/S1369-5274(02)00286-2
    • A phagosome of one's own: a microbial guide to life in the macrophage. Amer AO, Swanson MS, Curr Opin Microbiol 2002 5 1 56 61 (Pubitemid 34118158)
    • (2002) Current Opinion in Microbiology , vol.5 , Issue.1 , pp. 56-61
    • Amer, A.O.1    Swanson, M.S.2
  • 11
    • 0032870794 scopus 로고    scopus 로고
    • Effects of DksA and ClpP protease on sigma S production and virulence in Salmonella typhimurium
    • DOI 10.1046/j.1365-2958.1999.01581.x
    • Effects of DksA and ClpP protease on sigma S production and virulence in Salmonella typhimurium. Webb C, Moreno M, Wilmes-Riesenberg M, Curtiss R, Foster JW, Mol Microbiol 1999 34 1 112 123 (Pubitemid 29460490)
    • (1999) Molecular Microbiology , vol.34 , Issue.1 , pp. 112-123
    • Webb, C.1    Moreno, M.2    Wilmes-Riesenberg, M.3    Curtiss III, R.4    Foster, J.W.5
  • 12
    • 0034103357 scopus 로고    scopus 로고
    • The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes
    • DOI 10.1046/j.1365-2958.2000.01773.x
    • The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes. Gaillot O, Pellegrini E, Bregenholt S, Nair S, Berche P, Mol Microbiol 2000 35 6 1286 1294 (Pubitemid 30175506)
    • (2000) Molecular Microbiology , vol.35 , Issue.6 , pp. 1286-1294
    • Gaillot, O.1    Pellegrini, E.2    Bregenholt, S.3    Nair, S.4    Berche, P.5
  • 13
    • 0036279922 scopus 로고    scopus 로고
    • Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence
    • DOI 10.1128/JB.184.13.3508-3520.2002
    • Global transcriptional analysis of clpP mutations of type 2 Streptococcus pneumoniae and their effects on physiology and virulence. Robertson GT, Ng WL, Foley J, Gilmour R, Winkler ME, J Bacteriol 2002 184 13 3508 3520 (Pubitemid 34625659)
    • (2002) Journal of Bacteriology , vol.184 , Issue.13 , pp. 3508-3520
    • Robertson, G.T.1    Ng, W.-L.2    Foley, J.3    Gilmour, R.4    Winkler, M.E.5
  • 14
    • 0038236437 scopus 로고    scopus 로고
    • Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
    • DOI 10.1046/j.1365-2958.2003.03524.x
    • Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence. Frees D, Qazi SN, Hill PJ, Ingmer H, Mol Microbiol 2003 48 6 1565 1578 (Pubitemid 36751062)
    • (2003) Molecular Microbiology , vol.48 , Issue.6 , pp. 1565-1578
    • Frees, D.1    Qazi, S.N.A.2    Hill, P.J.3    Ingmer, H.4
  • 15
    • 58049114070 scopus 로고    scopus 로고
    • Helicobacter pylori mutants defective in the clpP ATP-dependant protease and the chaperone clpA display reduced macrophage and murine survival
    • Helicobacter pylori mutants defective in the clpP ATP-dependant protease and the chaperone clpA display reduced macrophage and murine survival. Loughlin MF, Arandhara V, Okolie C, Aldsworth TG, Jenks PJ, Microb Pathog 2009 46 1 53 57
    • (2009) Microb Pathog , vol.46 , Issue.1 , pp. 53-57
    • Loughlin, M.F.1    Arandhara, V.2    Okolie, C.3    Aldsworth, T.G.4    Jenks, P.J.5
  • 16
    • 77955343540 scopus 로고    scopus 로고
    • Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis
    • Characterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosis. Sherrid AM, Rustad TR, Cangelosi GA, Sherman DR, PLoS One 2010 5 7 11622
    • (2010) PLoS One , vol.5 , Issue.7 , pp. 511622
    • Sherrid, A.M.1    Rustad, T.R.2    Cangelosi, G.A.3    Sherman, D.R.4
  • 17
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • Genes required for mycobacterial growth defined by high density mutagenesis. Sassetti CM, Boyd DH, Rubin EJ, Mol Microbiol 2003 48 1 77 84 (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 19
    • 0025358672 scopus 로고
    • Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli
    • Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. Maurizi MR, Clark WP, Katayama Y, Rudikoff S, Pumphrey J, Bowers B, Gottesman S, J Biol Chem 1990 265 21 12536 12545
    • (1990) J Biol Chem , vol.265 , Issue.21 , 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
  • 20
    • 0025323156 scopus 로고
    • Clp P represents a unique family of serine proteases
    • Clp P represents a unique family of serine proteases. Maurizi MR, Clark WP, Kim SH, Gottesman S, J Biol Chem 1990 265 21 12546 12552
    • (1990) J Biol Chem , vol.265 , Issue.21 , pp. 12546-12552
    • Maurizi, M.R.1    Clark, W.P.2    Kim, S.H.3    Gottesman, S.4
  • 22
    • 0036093755 scopus 로고    scopus 로고
    • ClpP-dependent degradation of PopR allows tightly regulated expression of the clpP3 clpP4 operon in Streptomyces lividans
    • DOI 10.1046/j.1365-2958.2002.02907.x
    • ClpP-dependent degradation of PopR allows tightly regulated expression of the clpP3 clpP4 operon in Streptomyces lividans. Viala J, Mazodier P, Mol Microbiol 2002 44 3 633 643 (Pubitemid 34526576)
    • (2002) Molecular Microbiology , vol.44 , Issue.3 , pp. 633-643
    • Viala, J.1    Mazodier, P.2
  • 23
    • 31344467469 scopus 로고    scopus 로고
    • The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes
    • DOI 10.1016/j.jsb.2005.09.011, PII S1047847705001917
    • The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes. Bewley MC, Graziano V, Griffin K, Flanagan JM, J Struct Biol 2006 153 2 113 128 (Pubitemid 43139692)
    • (2006) Journal of Structural Biology , vol.153 , Issue.2 , pp. 113-128
    • Bewley, M.C.1    Graziano, V.2    Griffin, K.3    Flanagan, J.M.4
  • 24
    • 58349103347 scopus 로고    scopus 로고
    • Turned on for degradation: ATPase-independent degradation by ClpP
    • Turned on for degradation: ATPase-independent degradation by ClpP. Bewley MC, Graziano V, Griffin K, Flanagan JM, J Struct Biol 2009 165 2 118 125
    • (2009) J Struct Biol , vol.165 , Issue.2 , pp. 118-125
    • Bewley, M.C.1    Graziano, V.2    Griffin, K.3    Flanagan, J.M.4
  • 25
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • DOI 10.1016/S1097-2765(01)00274-X
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Kohler A, Cascio P, Leggett DS, Woo KM, Goldberg AL, Finley D, Mol Cell 2001 7 6 1143 1152 (Pubitemid 32607349)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1143-1152
    • Kohler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 26
    • 27444440627 scopus 로고    scopus 로고
    • Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX
    • DOI 10.1074/jbc.M507240200
    • Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX. Kang SG, Dimitrova MN, Ortega J, Ginsburg A, Maurizi MR, J Biol Chem 2005 280 42 35424 35432 (Pubitemid 41532732)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35424-35432
    • Kang, S.G.1    Dimitrova, M.N.2    Ortega, J.3    Ginsburg, A.4    Maurizi, M.R.5
  • 27
    • 77954636793 scopus 로고    scopus 로고
    • Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations
    • Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Kimber MS, Yu AY, Borg M, Leung E, Chan HS, Houry WA, Structure 2010 18 7 798 808
    • (2010) Structure , vol.18 , Issue.7 , pp. 798-808
    • Kimber, M.S.1    Yu, A.Y.2    Borg, M.3    Leung, E.4    Chan, H.S.5    Houry, W.A.6
  • 28
    • 0027382271 scopus 로고
    • A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli
    • A comparative study of the chymotrypsin-like activity of the rat liver multicatalytic proteinase and the ClpP from Escherichia coli. Arribas J, Castano JG, J Biol Chem 1993 268 28 21165 21171 (Pubitemid 23292303)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.28 , pp. 21165-21171
    • Arribas, J.1    Castano, J.G.2
  • 29
    • 70350238220 scopus 로고    scopus 로고
    • Atypical caseinolytic protease homolog from Plasmodium falciparum possesses unusual substrate preference and a functional nuclear localization signal
    • Atypical caseinolytic protease homolog from Plasmodium falciparum possesses unusual substrate preference and a functional nuclear localization signal. Lin W, Chan M, Sim TS, Parasitol Res 2009 105 6 1715 1722
    • (2009) Parasitol Res , vol.105 , Issue.6 , pp. 1715-1722
    • Lin, W.1    Chan, M.2    Sim, T.S.3
  • 31
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • DOI 10.1016/0076-6879(90)85008-C
    • Use of T7 RNA polymerase to direct expression of cloned genes. Studier FW, Rosenberg AH, Dunn JJ, Dubendorff JW, Methods Enzymol 1990 185 60 89 (Pubitemid 20219811)
    • (1990) Methods in Enzymology , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 32
    • 77349122288 scopus 로고    scopus 로고
    • Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the Bordetella pertussis adenylate cyclase toxin
    • Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the Bordetella pertussis adenylate cyclase toxin. Sotomayor Perez AC, Karst JC, Davi M, Guijarro JI, Ladant D, Chenal A, J Mol Biol 2010 397 2 534 549
    • (2010) J Mol Biol , vol.397 , Issue.2 , pp. 534-549
    • Sotomayor Perez, A.C.1    Karst, J.C.2    Davi, M.3    Guijarro, J.I.4    Ladant, D.5    Chenal, A.6


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