메뉴 건너뛰기




Volumn 70, Issue 5, 2013, Pages 761-775

Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response

Author keywords

Molecular switch; Oligomerization; PDZ domain; Protein quality control; X ray crystallography

Indexed keywords

CHAPERONE; HIGH-TEMPERATURE REQUIREMENT A; HIGH-TEMPERATURE REQUIREMENT A2; OLIGOMER; PROTEIN DEGP; PROTEINASE; SERINE PROTEINASE; SERINE PROTEINASE OMI; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84873712940     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1076-4     Document Type: Review
Times cited : (104)

References (88)
  • 1
    • 57649165535 scopus 로고    scopus 로고
    • Evolution of peptidase diversity
    • 18768474 10.1074/jbc.M804650200 1:CAS:528:DC%2BD1cXht1ynt7bJ
    • Page MJ, Di Cera E (2008) Evolution of peptidase diversity. J Biol Chem 283:30010-30014
    • (2008) J Biol Chem , vol.283 , pp. 30010-30014
    • Page, M.J.1    Di Cera, E.2
  • 2
    • 79951967246 scopus 로고    scopus 로고
    • HtrA proteases: Regulated proteolysis in protein quality control
    • 21326199 10.1038/nrm3065 1:CAS:528:DC%2BC3MXhvFKltbk%3D
    • Clausen T, Kaiser M, Huber R, Ehrmann M (2011) HtrA proteases: regulated proteolysis in protein quality control. Nat Rev Mol Cell Biol 12:152-162
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 152-162
    • Clausen, T.1    Kaiser, M.2    Huber, R.3    Ehrmann, M.4
  • 4
    • 0032825302 scopus 로고    scopus 로고
    • The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress
    • 10517331 10.1007/s004380051092 1:CAS:528:DyaK1MXntFCktrc%3D
    • Skorko-Glonek J, Zurawa D, Kuczwara E, Wozniak M, Wypych Z, Lipinska B (1999) The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress. Mol Gen Genet 262:342-350
    • (1999) Mol Gen Genet , vol.262 , pp. 342-350
    • Skorko-Glonek, J.1    Zurawa, D.2    Kuczwara, E.3    Wozniak, M.4    Wypych, Z.5    Lipinska, B.6
  • 5
    • 43849099548 scopus 로고    scopus 로고
    • Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: Disulfide oxidoreductase DsbA
    • 18174153 10.1074/mcp.M700433-MCP200
    • Önder Ö, Turkarslan S, Sun D, Daldal F (2008) Overproduction or absence of the periplasmic protease DegP severely compromises bacterial growth in the absence of the dithiol: disulfide oxidoreductase DsbA. Mol Cell Proteomics 7:875-890
    • (2008) Mol Cell Proteomics , vol.7 , pp. 875-890
    • Önder, Ö.1    Turkarslan, S.2    Sun, D.3    Daldal, F.4
  • 6
    • 0029156237 scopus 로고
    • Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures
    • 7557477 10.1016/0378-1119(95)00406-V 1:CAS:528:DyaK2MXosVOhtbc%3D
    • Skorko-Glonek J, Wawrzynow A, Krzewski K, Kurpierz K, Lipinska B (1995) Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures. Gene 163:47-52
    • (1995) Gene , vol.163 , pp. 47-52
    • Skorko-Glonek, J.1    Wawrzynow, A.2    Krzewski, K.3    Kurpierz, K.4    Lipinska, B.5
  • 7
    • 2442563573 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli sigma-dependent envelope stress response
    • 15101969 10.1111/j.1365-2958.2003.03982.x 1:CAS:528:DC%2BD2cXktFCitL8%3D
    • Alba BM, Gross CA (2004) Regulation of the Escherichia coli sigma-dependent envelope stress response. Mol Microbiol 52:613-619
    • (2004) Mol Microbiol , vol.52 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 8
    • 71749086886 scopus 로고    scopus 로고
    • Proteases in bacterial pathogenesis
    • 19778606 10.1016/j.resmic.2009.08.017 1:CAS:528:DC%2BD1MXhsVens7fJ
    • Ingmer H, Brøndsted L (2009) Proteases in bacterial pathogenesis. Res Microbiol 160:704-710
    • (2009) Res Microbiol , vol.160 , pp. 704-710
    • Ingmer, H.1    Brøndsted, L.2
  • 9
    • 79960601819 scopus 로고    scopus 로고
    • The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies
    • 21670246 10.1073/pnas.1101084108 1:CAS:528:DC%2BC3MXovFentL8%3D
    • Wrase R, Scott H, Hilgenfeld R, Hansen G (2011) The Legionella HtrA homologue DegQ is a self-compartmentizing protease that forms large 12-meric assemblies. Proc Natl Acad Sci USA 108:10490-10495
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 10490-10495
    • Wrase, R.1    Scott, H.2    Hilgenfeld, R.3    Hansen, G.4
  • 10
    • 80052495133 scopus 로고    scopus 로고
    • Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins
    • 21893291 10.1016/j.str.2011.06.013 1:CAS:528:DC%2BC3MXhtFaqsr7O
    • Bai XC, Pan XJ, Wang XJ, Ye YY, Chang LF, Leng D, Lei J, Sui SF (2011) Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins. Structure 19:1328-1337
    • (2011) Structure , vol.19 , pp. 1328-1337
    • Bai, X.C.1    Pan, X.J.2    Wang, X.J.3    Ye, Y.Y.4    Chang, L.F.5    Leng, D.6    Lei, J.7    Sui, S.F.8
  • 11
    • 79953268481 scopus 로고    scopus 로고
    • Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages
    • 21458668 10.1016/j.cell.2011.02.024 1:CAS:528:DC%2BC3MXktF2hurk%3D
    • Kim S, Grant RA, Sauer RT (2011) Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages. Cell 145:67-78
    • (2011) Cell , vol.145 , pp. 67-78
    • Kim, S.1    Grant, R.A.2    Sauer, R.T.3
  • 13
    • 80052235693 scopus 로고    scopus 로고
    • Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope
    • 21685389 10.1074/jbc.M111.243832 1:CAS:528:DC%2BC3MXhtVOktL%2FO
    • Sawa J, Malet H, Krojer T, Canellas F, Ehrmann M, Clausen T (2011) Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope. J Biol Chem 286:30680-30690
    • (2011) J Biol Chem , vol.286 , pp. 30680-30690
    • Sawa, J.1    Malet, H.2    Krojer, T.3    Canellas, F.4    Ehrmann, M.5    Clausen, T.6
  • 14
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • 11919638 10.1038/416455a 1:CAS:528:DC%2BD38Xislamt7o%3D
    • Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416:455-459
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 15
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • 18496527 10.1038/nature07004 1:CAS:528:DC%2BD1cXntVCqurg%3D
    • Krojer T, Sawa J, Schäfer E, Saibil HR, Ehrmann M, Clausen T (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453:885-890
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schäfer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 16
    • 50149107174 scopus 로고    scopus 로고
    • Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
    • 18697939 10.1073/pnas.0805464105 1:CAS:528:DC%2BD1cXhtVCnurnM
    • Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, Chang Z, Sui SF (2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc Natl Acad Sci USA 105:11939-11944
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11939-11944
    • Jiang, J.1    Zhang, X.2    Chen, Y.3    Wu, Y.4    Zhou, Z.H.5    Chang, Z.6    Sui, S.F.7
  • 18
    • 63849240148 scopus 로고    scopus 로고
    • Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control
    • 19255437 10.1073/pnas.0811780106 1:CAS:528:DC%2BD1MXktFGqtbc%3D
    • Shen QT, Bai XC, Chang LF, Wu Y, Wang HW, Sui SF (2009) Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control. Proc Natl Acad Sci USA 106:4858-4863
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4858-4863
    • Shen, Q.T.1    Bai, X.C.2    Chang, L.F.3    Wu, Y.4    Wang, H.W.5    Sui, S.F.6
  • 19
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • 15137941 10.1016/S0092-8674(04)00454-4 1:CAS:528:DC%2BD2cXktlCqtrk%3D
    • Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T (2004) Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease. Cell 117:483-494
    • (2004) Cell , vol.117 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 22
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
    • 8576051 1:CAS:528:DyaK28XpvVansA%3D%3D
    • Waller PR, Sauer RT (1996) Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J Bacteriol 178:1146-1153
    • (1996) J Bacteriol , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 23
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • 10319814 10.1016/S0092-8674(00)80743-6 1:CAS:528:DyaK1MXjtVKltb4%3D
    • Spiess C, Beil A, Ehrmann M (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 24
    • 29644445406 scopus 로고    scopus 로고
    • Listeria monocytogenes 10403S HtrA is necessary for resistance to cellular stress and virulence
    • 16369036 10.1128/IAI.74.1.765-768.2006 1:CAS:528:DC%2BD28XitlOjtw%3D%3D
    • Wilson RL, Brown LL, Kirkwood-Watts D, Warren TK, Lund SA, King DS, Jones KF, Hruby DE (2006) Listeria monocytogenes 10403S HtrA is necessary for resistance to cellular stress and virulence. Infect Immun 74:765-768
    • (2006) Infect Immun , vol.74 , pp. 765-768
    • Wilson, R.L.1    Brown, L.L.2    Kirkwood-Watts, D.3    Warren, T.K.4    Lund, S.A.5    King, D.S.6    Jones, K.F.7    Hruby, D.E.8
  • 25
    • 23744437997 scopus 로고    scopus 로고
    • Role for HtrA in stress induction and virulence potential in Listeria monocytogenes
    • 16085809 10.1128/AEM.71.8.4241-4247.2005 1:CAS:528:DC%2BD2MXoslGitrc%3D
    • Stack HM, Sleator RD, Bowers M, Hill C, Gahan CG (2005) Role for HtrA in stress induction and virulence potential in Listeria monocytogenes. Appl Environ Microbiol 71:4241-4247
    • (2005) Appl Environ Microbiol , vol.71 , pp. 4241-4247
    • Stack, H.M.1    Sleator, R.D.2    Bowers, M.3    Hill, C.4    Gahan, C.G.5
  • 26
    • 11144298928 scopus 로고    scopus 로고
    • Effect of inactivation of degS on Salmonella enterica serovar typhimurium in vitro and in vivo
    • 15618185 10.1128/IAI.73.1.459-463.2005 1:CAS:528:DC%2BD2MXisFylsA%3D%3D
    • Rowley G, Stevenson A, Kormanec J, Roberts M (2005) Effect of inactivation of degS on Salmonella enterica serovar typhimurium in vitro and in vivo. Infect Immun 73:459-463
    • (2005) Infect Immun , vol.73 , pp. 459-463
    • Rowley, G.1    Stevenson, A.2    Kormanec, J.3    Roberts, M.4
  • 27
    • 34147144087 scopus 로고    scopus 로고
    • Burkholderia cenocepacia requires a periplasmic HtrA protease for growth under thermal and osmotic stress and for survival in vivo
    • 17220310 10.1128/IAI.01581-06 1:CAS:528:DC%2BD2sXkt1Ohs7Y%3D
    • Flannagan RS, Aubert D, Kooi C, Sokol PA, Valvano MA (2007) Burkholderia cenocepacia requires a periplasmic HtrA protease for growth under thermal and osmotic stress and for survival in vivo. Infect Immun 75:1679-1689
    • (2007) Infect Immun , vol.75 , pp. 1679-1689
    • Flannagan, R.S.1    Aubert, D.2    Kooi, C.3    Sokol, P.A.4    Valvano, M.A.5
  • 28
    • 9244252534 scopus 로고    scopus 로고
    • Effect of inactivation of the HtrA-like serine protease DegQ on the virulence of Salmonella enterica serovar typhimurium in mice
    • 15557668 10.1128/IAI.72.12.7357-7359.2004 1:CAS:528:DC%2BD2cXhtVGls7nL
    • Farn J, Roberts M (2004) Effect of inactivation of the HtrA-like serine protease DegQ on the virulence of Salmonella enterica serovar typhimurium in mice. Infect Immun 72:7357-7359
    • (2004) Infect Immun , vol.72 , pp. 7357-7359
    • Farn, J.1    Roberts, M.2
  • 29
    • 80052697246 scopus 로고    scopus 로고
    • HtrA is a major virulence determinant of Bacillus anthracis
    • 21801240 10.1111/j.1365-2958.2011.07790.x 1:CAS:528:DC%2BC3MXht1CgsLzK
    • Chitlaru T, Zaide G, Ehrlich S, Inbar I, Cohen O, Shafferman A (2011) HtrA is a major virulence determinant of Bacillus anthracis. Mol Microbiol 81:1542-1559
    • (2011) Mol Microbiol , vol.81 , pp. 1542-1559
    • Chitlaru, T.1    Zaide, G.2    Ehrlich, S.3    Inbar, I.4    Cohen, O.5    Shafferman, A.6
  • 30
    • 19944402536 scopus 로고    scopus 로고
    • Envelope stress responses and Gram-negative bacterial pathogenesis
    • 15882407 10.1111/j.1365-2958.2005.04625.x 1:CAS:528:DC%2BD2MXkslOlu78%3D
    • Raivio TL (2005) Envelope stress responses and Gram-negative bacterial pathogenesis. Mol Microbiol 56:1119-1128
    • (2005) Mol Microbiol , vol.56 , pp. 1119-1128
    • Raivio, T.L.1
  • 31
    • 0344953579 scopus 로고    scopus 로고
    • OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain
    • 12679035 10.1016/S0092-8674(03)00203-4 1:CAS:528:DC%2BD3sXjtVWqsLg%3D
    • Walsh NP, Alba BM, Bose B, Gross CA, Sauer RT (2003) OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain. Cell 113:61-71
    • (2003) Cell , vol.113 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 33
    • 35548973933 scopus 로고    scopus 로고
    • Allosteric activation of DegS, a stress sensor PDZ protease
    • 17981123 10.1016/j.cell.2007.08.044 1:CAS:528:DC%2BD2sXhtlWitrzI
    • Sohn J, Grant RA, Sauer RT (2007) Allosteric activation of DegS, a stress sensor PDZ protease. Cell 131:572-583
    • (2007) Cell , vol.131 , pp. 572-583
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 35
    • 3042644567 scopus 로고    scopus 로고
    • Structural analysis of DegS, a stress sensor of the bacterial periplasm
    • 15225661 10.1016/j.febslet.2004.06.012 1:CAS:528:DC%2BD2cXlt1alsr0%3D
    • Zeth K (2004) Structural analysis of DegS, a stress sensor of the bacterial periplasm. FEBS Lett 569:351-358
    • (2004) FEBS Lett , vol.569 , pp. 351-358
    • Zeth, K.1
  • 36
    • 77958563467 scopus 로고    scopus 로고
    • Allostery is an intrinsic property of the protease domain of DegS: Implications for enzyme function and evolution
    • 20739286 10.1074/jbc.M110.135541 1:CAS:528:DC%2BC3cXhtlWktrnI
    • Sohn J, Grant RA, Sauer RT (2010) Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. J Biol Chem 285:34039-34047
    • (2010) J Biol Chem , vol.285 , pp. 34039-34047
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 37
    • 70349779534 scopus 로고    scopus 로고
    • OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism
    • 19836340 10.1016/j.str.2009.07.017 1:CAS:528:DC%2BD1MXht1yms77K
    • Sohn J, Grant RA, Sauer RT (2009) OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure 17:1411-1421
    • (2009) Structure , vol.17 , pp. 1411-1421
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 38
    • 35348985928 scopus 로고    scopus 로고
    • Regulation of the σe stress response by DegS: How the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress
    • 17938245 10.1101/gad.445307 1:CAS:528:DC%2BD2sXht1WnsbnM
    • Hasselblatt H, Kurzbauer R, Wilken C, Krojer T, Sawa J, Kurt J, Kirk R, Hasenbein S, Ehrmann M, Clausen T (2007) Regulation of the σE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress. Genes Dev 21:2659-2670
    • (2007) Genes Dev , vol.21 , pp. 2659-2670
    • Hasselblatt, H.1    Kurzbauer, R.2    Wilken, C.3    Krojer, T.4    Sawa, J.5    Kurt, J.6    Kirk, R.7    Hasenbein, S.8    Ehrmann, M.9    Clausen, T.10
  • 39
    • 0023808092 scopus 로고
    • 32-independent mechanism of heat-inducible transcription
    • 3057437 10.1093/nar/16.21.10053 1:CAS:528:DyaL1MXktlCnsbY%3D
    • 32- independent mechanism of heat-inducible transcription. Nucleic Acids Res 16:10053-10067
    • (1988) Nucleic Acids Res , vol.16 , pp. 10053-10067
    • Lipinska, B.1    Sharma, S.2    Georgopoulos, C.3
  • 40
    • 77951298112 scopus 로고    scopus 로고
    • Molecular transformers in the cell: Lessons learned from the DegP protease-chaperone
    • 20188538 10.1016/j.sbi.2010.01.014 1:CAS:528:DC%2BC3cXks1Sjtrs%3D
    • Sawa J, Heuck A, Ehrmann M, Clausen T (2010) Molecular transformers in the cell: lessons learned from the DegP protease-chaperone. Curr Opin Struct Biol 20:253-258
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 253-258
    • Sawa, J.1    Heuck, A.2    Ehrmann, M.3    Clausen, T.4
  • 41
    • 0033579536 scopus 로고    scopus 로고
    • Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli
    • 10600391 10.1006/jmbi.1999.3320 1:CAS:528:DyaK1MXnvFaqs74%3D
    • Kim KI, Park SC, Kang SH, Cheong GW, Chung CH (1999) Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli. J Mol Biol 294:1363-1374
    • (1999) J Mol Biol , vol.294 , pp. 1363-1374
    • Kim, K.I.1    Park, S.C.2    Kang, S.H.3    Cheong, G.W.4    Chung, C.H.5
  • 42
    • 77954384306 scopus 로고    scopus 로고
    • HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues
    • 20581825 10.1038/nsmb.1840 1:CAS:528:DC%2BC3cXnvFyktrk%3D
    • Krojer T, Sawa J, Huber R, Clausen T (2010) HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues. Nat Struct Mol Biol 17:844-852
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 844-852
    • Krojer, T.1    Sawa, J.2    Huber, R.3    Clausen, T.4
  • 43
    • 84860816318 scopus 로고    scopus 로고
    • Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival
    • 22529381 10.1073/pnas.1204791109 1:CAS:528:DC%2BC38XnsVWks7c%3D
    • Kim S, Sauer RT (2012) Cage assembly of DegP protease is not required for substrate-dependent regulation of proteolytic activity or high-temperature cell survival. Proc Natl Acad Sci USA 109:7263-7268
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 7263-7268
    • Kim, S.1    Sauer, R.T.2
  • 44
    • 33846588852 scopus 로고    scopus 로고
    • The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity
    • 17122339 10.1128/JB.01334-06 1:CAS:528:DC%2BD2sXht1ehtr0%3D
    • Jomaa A, Damjanovic D, Leong V, Ghirlando R, Iwanczyk J, Ortega J (2007) The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity. J Bacteriol 189:706-716
    • (2007) J Bacteriol , vol.189 , pp. 706-716
    • Jomaa, A.1    Damjanovic, D.2    Leong, V.3    Ghirlando, R.4    Iwanczyk, J.5    Ortega, J.6
  • 45
    • 0029843213 scopus 로고    scopus 로고
    • The DegP and DegQ periplasmic endoproteases of Escherichia coli: Specificity for cleavage sites and substrate conformation
    • 8830688 1:CAS:528:DyaK28XmtFOks7s%3D
    • Kolmar H, Waller PR, Sauer RT (1996) The DegP and DegQ periplasmic endoproteases of Escherichia coli: specificity for cleavage sites and substrate conformation. J Bacteriol 178:5925-5929
    • (1996) J Bacteriol , vol.178 , pp. 5925-5929
    • Kolmar, H.1    Waller, P.R.2    Sauer, R.T.3
  • 46
    • 25444491980 scopus 로고    scopus 로고
    • Structure and function of HtrA family proteins, the key players in protein quality control
    • 15943900 10.5483/BMBRep.2005.38.3.266 1:CAS:528:DC%2BD2MXlt1ygsbo%3D
    • Kim DY, Kim KK (2005) Structure and function of HtrA family proteins, the key players in protein quality control. J Biochem Mol Biol 38:266-274
    • (2005) J Biochem Mol Biol , vol.38 , pp. 266-274
    • Kim, D.Y.1    Kim, K.K.2
  • 47
    • 0037458675 scopus 로고    scopus 로고
    • Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima
    • 12458220 10.1074/jbc.M208148200 1:CAS:528:DC%2BD3sXht1ejsb4%3D
    • Kim DY, Kim DR, Ha SC, Lokanath NK, Lee CJ, Hwang HY, Kim KK (2003) Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima. J Biol Chem 278:6543-6551
    • (2003) J Biol Chem , vol.278 , pp. 6543-6551
    • Kim, D.Y.1    Kim, D.R.2    Ha, S.C.3    Lokanath, N.K.4    Lee, C.J.5    Hwang, H.Y.6    Kim, K.K.7
  • 48
    • 40049107314 scopus 로고    scopus 로고
    • The mechanism of temperature-induced bacterial HtrA activation
    • 18272173 10.1016/j.jmb.2007.12.078 1:CAS:528:DC%2BD1cXjtVWlu78%3D
    • Kim DY, Kwon E, Shin YK, Kweon DH, Kim KK (2008) The mechanism of temperature-induced bacterial HtrA activation. J Mol Biol 377:410-420
    • (2008) J Mol Biol , vol.377 , pp. 410-420
    • Kim, D.Y.1    Kwon, E.2    Shin, Y.K.3    Kweon, D.H.4    Kim, K.K.5
  • 49
    • 0036397455 scopus 로고    scopus 로고
    • Is Mycobacterium tuberculosis a closer relative to Gram-positive or Gram-negative bacterial pathogens?
    • 10.1054/tube.2002.0328 1:STN:280:DC%2BD38vpsFyqsA%3D%3D
    • Fu LM, Fu-Liu CS (2002) Is Mycobacterium tuberculosis a closer relative to Gram-positive or Gram-negative bacterial pathogens? Tuberculosis (Edinb) 82:85-90
    • (2002) Tuberculosis (Edinb) , vol.82 , pp. 85-90
    • Fu, L.M.1    Fu-Liu, C.S.2
  • 50
    • 0032765127 scopus 로고    scopus 로고
    • Cloning, expression, and immunological evaluation of two putative secreted serine protease antigens of Mycobacterium tuberculosis
    • 10417166 1:CAS:528:DyaK1MXkvVKlsbw%3D
    • Skeiky YA, Lodes MJ, Guderian JA, Mohamath R, Bement T, Alderson MR, Reed SG (1999) Cloning, expression, and immunological evaluation of two putative secreted serine protease antigens of Mycobacterium tuberculosis. Infect Immun 67:3998-4007
    • (1999) Infect Immun , vol.67 , pp. 3998-4007
    • Skeiky, Y.A.1    Lodes, M.J.2    Guderian, J.A.3    Mohamath, R.4    Bement, T.5    Alderson, M.R.6    Reed, S.G.7
  • 51
    • 0036263973 scopus 로고    scopus 로고
    • Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
    • 11967569 10.1038/nsb795 1:CAS:528:DC%2BD38XjvFOms70%3D
    • Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y (2002) Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Nat Struct Biol 9:436-441
    • (2002) Nat Struct Biol , vol.9 , pp. 436-441
    • Li, W.1    Srinivasula, S.M.2    Chai, J.3    Li, P.4    Wu, J.W.5    Zhang, Z.6    Alnemri, E.S.7    Shi, Y.8
  • 53
    • 57849101491 scopus 로고    scopus 로고
    • D1-protein dynamics in photosystem II: The lingering enigma
    • 18709440 10.1007/s11120-008-9342-x 1:CAS:528:DC%2BD1cXhsVOgt7fN
    • Edelman M, Mattoo AK (2008) D1-protein dynamics in photosystem II: the lingering enigma. Photosynth Res 98:609-620
    • (2008) Photosynth Res , vol.98 , pp. 609-620
    • Edelman, M.1    Mattoo, A.K.2
  • 54
    • 71749101554 scopus 로고    scopus 로고
    • Deg/HtrA proteases as components of a network for photosystem II quality control in chloroplasts and cyanobacteria
    • 19732828 10.1016/j.resmic.2009.08.005 1:CAS:528:DC%2BD1MXhsVensL7N
    • Huesgen PF, Schuhmann H, Adamska I (2009) Deg/HtrA proteases as components of a network for photosystem II quality control in chloroplasts and cyanobacteria. Res Microbiol 160:726-732
    • (2009) Res Microbiol , vol.160 , pp. 726-732
    • Huesgen, P.F.1    Schuhmann, H.2    Adamska, I.3
  • 56
    • 23044491228 scopus 로고    scopus 로고
    • Expression and characterization of a serine protease that preferentially cleaves insulin-like growth factor binding protein-5
    • 15534875 10.1002/jcb.20328 1:CAS:528:DC%2BD2MXhtlaltLk%3D
    • Hou J, Clemmons DR, Smeekens S (2005) Expression and characterization of a serine protease that preferentially cleaves insulin-like growth factor binding protein-5. J Cell Biochem 94:470-484
    • (2005) J Cell Biochem , vol.94 , pp. 470-484
    • Hou, J.1    Clemmons, D.R.2    Smeekens, S.3
  • 61
    • 77955887363 scopus 로고    scopus 로고
    • Identification of novel substrates for the serine protease HTRA1 in the human RPE secretome
    • 10.1167/iovs.09-4853
    • An E, Sen S, Park SK, Gordish-Dressman H, Hathout Y (2010) Identification of novel substrates for the serine protease HTRA1 in the human RPE secretome. Investig Ophthalmol Vis Sci 51:3379-3386
    • (2010) Investig Ophthalmol Vis Sci , vol.51 , pp. 3379-3386
    • An, E.1    Sen, S.2    Park, S.K.3    Gordish-Dressman, H.4    Hathout, Y.5
  • 62
    • 23844487193 scopus 로고    scopus 로고
    • Expression of mouse HtrA1 serine protease in normal bone and cartilage and its upregulation in joint cartilage damaged by experimental arthritis
    • 15993670 10.1016/j.bone.2005.03.015 1:CAS:528:DC%2BD2MXos1agtb8%3D
    • Tsuchiya A, Yano M, Tocharus J, Kojima H, Fukumoto M, Kawaichi M, Oka C (2005) Expression of mouse HtrA1 serine protease in normal bone and cartilage and its upregulation in joint cartilage damaged by experimental arthritis. Bone 37:323-336
    • (2005) Bone , vol.37 , pp. 323-336
    • Tsuchiya, A.1    Yano, M.2    Tocharus, J.3    Kojima, H.4    Fukumoto, M.5    Kawaichi, M.6    Oka, C.7
  • 63
    • 67649305413 scopus 로고    scopus 로고
    • HtrA serine proteases as potential therapeutic targets in cancer
    • 19519315 10.2174/156800909788486704 1:CAS:528:DC%2BD1MXotlWku7c%3D
    • Chien J, Campioni M, Shridhar V, Baldi A (2009) HtrA serine proteases as potential therapeutic targets in cancer. Curr Cancer Drug Targets 9:451-468
    • (2009) Curr Cancer Drug Targets , vol.9 , pp. 451-468
    • Chien, J.1    Campioni, M.2    Shridhar, V.3    Baldi, A.4
  • 64
    • 56249140828 scopus 로고    scopus 로고
    • Age-related macular degeneration
    • 19027484 10.1016/S0140-6736(08)61759-6 1:CAS:528:DC%2BD1cXhsVWhtbjP
    • Coleman HR, Chan CC, Ferris FL 3rd, Chew EY (2008) Age-related macular degeneration. Lancet 372:1835-1845
    • (2008) Lancet , vol.372 , pp. 1835-1845
    • Coleman, H.R.1    Chan, C.C.2    Ferris III, F.L.3    Chew, E.Y.4
  • 66
    • 57349169295 scopus 로고    scopus 로고
    • Emerging roles of serine proteinases in tissue turnover in arthritis
    • 10.1002/art.24046 1:CAS:528:DC%2BD1MXmt1yntA%3D%3D
    • Milner JM, Patel A, Rowan AD (2008) Emerging roles of serine proteinases in tissue turnover in arthritis. Arthr Rheum 58:3644-3656
    • (2008) Arthr Rheum , vol.58 , pp. 3644-3656
    • Milner, J.M.1    Patel, A.2    Rowan, A.D.3
  • 67
    • 39449115415 scopus 로고    scopus 로고
    • The mitochondrial serine protease HtrA2/Omi: An overview
    • 18174901 10.1038/sj.cdd.4402291 1:CAS:528:DC%2BD1cXitVOlsbw%3D
    • Vande Walle L, Lamkanfi M, Vandenabeele P (2008) The mitochondrial serine protease HtrA2/Omi: an overview. Cell Death Differ 15:453-460
    • (2008) Cell Death Differ , vol.15 , pp. 453-460
    • Vande Walle, L.1    Lamkanfi, M.2    Vandenabeele, P.3
  • 69
    • 0037314409 scopus 로고    scopus 로고
    • CIAP1 and the serine protease HTRA2 are involved in a novel p53-dependent apoptosis pathway in mammals
    • 12569127 10.1101/gad.1047003 1:CAS:528:DC%2BD3sXhtF2mtLk%3D
    • Jin S, Kalkum M, Overholtzer M, Stoffel A, Chait BT, Levine AJ (2003) CIAP1 and the serine protease HTRA2 are involved in a novel p53-dependent apoptosis pathway in mammals. Genes Dev 17:359-367
    • (2003) Genes Dev , vol.17 , pp. 359-367
    • Jin, S.1    Kalkum, M.2    Overholtzer, M.3    Stoffel, A.4    Chait, B.T.5    Levine, A.J.6
  • 70
    • 1542571796 scopus 로고    scopus 로고
    • Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi
    • 14512424 10.1074/jbc.M308659200 1:CAS:528:DC%2BD3sXptlGrt74%3D
    • Martins LM, Turk BE, Cowling V, Borg A, Jarrell ET, Cantley LC, Downward J (2003) Binding specificity and regulation of the serine protease and PDZ domains of HtrA2/Omi. J Biol Chem 278:49417-49427
    • (2003) J Biol Chem , vol.278 , pp. 49417-49427
    • Martins, L.M.1    Turk, B.E.2    Cowling, V.3    Borg, A.4    Jarrell, E.T.5    Cantley, L.C.6    Downward, J.7
  • 72
    • 33749186806 scopus 로고    scopus 로고
    • Selection of neural differentiation-specific genes by comparing profiles of random differentiation
    • 16627687 10.1634/stemcells.2005-0325 1:CAS:528:DC%2BD28XhtFKiu77J
    • Lee MS, Jun DH, Hwang CI, Park SS, Kang JJ, Park HS, Kim J, Kim JH, Seo JS, Park WY (2006) Selection of neural differentiation-specific genes by comparing profiles of random differentiation. Stem Cells 24:1946-1955
    • (2006) Stem Cells , vol.24 , pp. 1946-1955
    • Lee, M.S.1    Jun, D.H.2    Hwang, C.I.3    Park, S.S.4    Kang, J.J.5    Park, H.S.6    Kim, J.7    Kim, J.H.8    Seo, J.S.9    Park, W.Y.10
  • 73
    • 34948867875 scopus 로고    scopus 로고
    • HtrA2 regulates beta-amyloid precursor protein (APP) metabolism through endoplasmic reticulum-associated degradation
    • 17684015 10.1074/jbc.M702951200 1:CAS:528:DC%2BD2sXhtVeisrfI
    • Huttunen HJ, Guenette SY, Peach C, Greco C, Xia W, Kim DY, Barren C, Tanzi RE, Kovacs DM (2007) HtrA2 regulates beta-amyloid precursor protein (APP) metabolism through endoplasmic reticulum-associated degradation. J Biol Chem 282:28285-28295
    • (2007) J Biol Chem , vol.282 , pp. 28285-28295
    • Huttunen, H.J.1    Guenette, S.Y.2    Peach, C.3    Greco, C.4    Xia, W.5    Kim, D.Y.6    Barren, C.7    Tanzi, R.E.8    Kovacs, D.M.9
  • 74
    • 81755174173 scopus 로고    scopus 로고
    • The structural basis of mode of activation and functional diversity: A case study with HtrA family of serine proteases
    • 22027029 10.1016/j.abb.2011.10.007 1:CAS:528:DC%2BC3MXhsV2kt7bF
    • Singh N, Kuppili RR, Bose K (2011) The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases. Arch Biochem Biophys 516:85-96
    • (2011) Arch Biochem Biophys , vol.516 , pp. 85-96
    • Singh, N.1    Kuppili, R.R.2    Bose, K.3
  • 75
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • 22053084 10.1093/nar/gkr931 1:CAS:528:DC%2BC3MXhs12hurzL
    • Letunic I, Doerks T, Bork P (2012) SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res 40:D302-D305
    • (2012) Nucleic Acids Res , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 76
    • 2342531574 scopus 로고    scopus 로고
    • PDZ domains-common players in the cell signaling
    • 14739991 1:CAS:528:DC%2BD2cXhtFGkt78%3D
    • Jelen F, Oleksy A, Smietana K, Otlewski J (2003) PDZ domains-common players in the cell signaling. Acta Biochim Pol 50:985-1017
    • (2003) Acta Biochim Pol , vol.50 , pp. 985-1017
    • Jelen, F.1    Oleksy, A.2    Smietana, K.3    Otlewski, J.4
  • 78
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: Structure, specificity, and modification
    • 20509869 10.1186/1478-811X-8-8
    • Lee HJ, Zheng JJ (2010) PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun Signal 8:8
    • (2010) Cell Commun Signal , vol.8 , pp. 8
    • Lee, H.J.1    Zheng, J.J.2
  • 79
    • 45549098563 scopus 로고    scopus 로고
    • Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins
    • 18505836 10.1073/pnas.0803392105 1:CAS:528:DC%2BD1cXnt1SrsLw%3D
    • Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K, Huber R, Ehrmann M, Clausen T (2008) Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins. Proc Natl Acad Sci USA 105:7702-7707
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7702-7707
    • Krojer, T.1    Pangerl, K.2    Kurt, J.3    Sawa, J.4    Stingl, C.5    Mechtler, K.6    Huber, R.7    Ehrmann, M.8    Clausen, T.9
  • 80
    • 79953153131 scopus 로고    scopus 로고
    • Extensions of PDZ domains as important structural and functional elements
    • 10.1007/s13238-010-0099-6
    • Wang CK, Pan L, Chen J, Zhang M (2011) Extensions of PDZ domains as important structural and functional elements. Protein Cell 1:737-751
    • (2011) Protein Cell , vol.1 , pp. 737-751
    • Wang, C.K.1    Pan, L.2    Chen, J.3    Zhang, M.4
  • 81
    • 80053161741 scopus 로고    scopus 로고
    • A systematic family-wide investigation reveals that ~ 30 % of mammalian PDZ domains engage in PDZ-PDZ interactions
    • 21944753 10.1016/j.chembiol.2011.06.013 1:CAS:528:DC%2BC3MXht1eisr7M
    • Chang BH, Gujral TS, Karp ES, BuKhalid R, Grantcharova VP, MacBeath G (2011) A systematic family-wide investigation reveals that ~ 30 % of mammalian PDZ domains engage in PDZ-PDZ interactions. Chem Biol 18:1143-1152
    • (2011) Chem Biol , vol.18 , pp. 1143-1152
    • Chang, B.H.1    Gujral, T.S.2    Karp, E.S.3    Bukhalid, R.4    Grantcharova, V.P.5    MacBeath, G.6
  • 82
    • 38049178969 scopus 로고    scopus 로고
    • Domain swapping within PDZ2 is responsible for dimerization of ZO proteins
    • 17928286 10.1074/jbc.M707255200 1:CAS:528:DC%2BD2sXhsVGjt7%2FO
    • Fanning AS, Lye MF, Anderson JM, Lavie A (2007) Domain swapping within PDZ2 is responsible for dimerization of ZO proteins. J Biol Chem 282:37710-37716
    • (2007) J Biol Chem , vol.282 , pp. 37710-37716
    • Fanning, A.S.1    Lye, M.F.2    Anderson, J.M.3    Lavie, A.4
  • 83
    • 34247238159 scopus 로고    scopus 로고
    • Crystal structures of autoinhibitory PDZ domain of Tamalin: Implications for metabotropic glutamate receptor trafficking regulation
    • 17396155 10.1038/sj.emboj.7601651 1:CAS:528:DC%2BD2sXktlSlu7g%3D
    • Sugi T, Oyama T, Muto T, Nakanishi S, Morikawa K, Jingami H (2007) Crystal structures of autoinhibitory PDZ domain of Tamalin: implications for metabotropic glutamate receptor trafficking regulation. EMBO J 26:2192-2205
    • (2007) EMBO J , vol.26 , pp. 2192-2205
    • Sugi, T.1    Oyama, T.2    Muto, T.3    Nakanishi, S.4    Morikawa, K.5    Jingami, H.6
  • 84
    • 0037424515 scopus 로고    scopus 로고
    • Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization
    • 12493751 10.1074/jbc.M212263200 1:CAS:528:DC%2BD3sXhsF2htro%3D
    • Im YJ, Park SH, Rho SH, Lee JH, Kang GB, Sheng M, Kim E, Eom SH (2003) Crystal structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization. J Biol Chem 278:8501-8507
    • (2003) J Biol Chem , vol.278 , pp. 8501-8507
    • Im, Y.J.1    Park, S.H.2    Rho, S.H.3    Lee, J.H.4    Kang, G.B.5    Sheng, M.6    Kim, E.7    Eom, S.H.8
  • 85
    • 0348111461 scopus 로고    scopus 로고
    • Crystal structure of the Shank PDZ-ligand complex reveals a class i PDZ interaction and a novel PDZ-PDZ dimerization
    • 12954649 10.1074/jbc.M306919200 1:CAS:528:DC%2BD3sXpt1GjsL0%3D
    • Im YJ, Lee JH, Park SH, Park SJ, Rho SH, Kang GB, Kim E, Eom SH (2003) Crystal structure of the Shank PDZ-ligand complex reveals a class I PDZ interaction and a novel PDZ-PDZ dimerization. J Biol Chem 278:48099-48104
    • (2003) J Biol Chem , vol.278 , pp. 48099-48104
    • Im, Y.J.1    Lee, J.H.2    Park, S.H.3    Park, S.J.4    Rho, S.H.5    Kang, G.B.6    Kim, E.7    Eom, S.H.8
  • 86
    • 25444479087 scopus 로고    scopus 로고
    • Role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans
    • 16177372 10.1128/IAI.73.10.6923-6934.2005 1:CAS:528:DC%2BD2MXhtVyhu7%2FN
    • Biswas S, Biswas I (2005) Role of HtrA in surface protein expression and biofilm formation by Streptococcus mutans. Infect Immun 73:6923-6934
    • (2005) Infect Immun , vol.73 , pp. 6923-6934
    • Biswas, S.1    Biswas, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.