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Volumn 63, Issue 11, 2011, Pages 955-963

Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine

Author keywords

AAA+ unfoldase; Bacteria; ClpXP protease; Mitochondria; Unfolded protein response

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CASEIN LYTIC PROTEASE; CHAPERONE; MITOCHONDRIAL PROTEIN; PROTEASOME; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84055190893     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.526     Document Type: Review
Times cited : (28)

References (71)
  • 1
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • Hartl, F. U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858. (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 2
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • DOI 10.1101/gad.1657108
    • Morimoto, R. I. (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22, 1427-1438. (Pubitemid 351793077)
    • (2008) Genes and Development , vol.22 , Issue.11 , pp. 1427-1438
    • Morimoto, R.I.1
  • 4
    • 79952585579 scopus 로고    scopus 로고
    • Integration of clearance mechanisms: The proteasome and autophagy
    • Wong, E. and Cuervo, A. M. (2010) Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb. Perspect. Biol. 2, a006734.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Wong, E.1    Cuervo, A.M.2
  • 6
    • 65649123769 scopus 로고    scopus 로고
    • Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii
    • Zhang, F., Wu, Z., Zhang, P., Tian, G., Finley, D., and Shi, Y. (2009) Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol. Cell 34, 485-496.
    • (2009) Mol. Cell. , vol.34 , pp. 485-496
    • Zhang, F.1    Wu, Z.2    Zhang, P.3    Tian, G.4    Finley, D.5    Shi, Y.6
  • 7
    • 57749102552 scopus 로고    scopus 로고
    • Substrate selection by the proteasome during degradation of protein complexes
    • Prakash, S., Inobe, T., Hatch, A. J., and Matouschek, A. (2009) Substrate selection by the proteasome during degradation of protein complexes. Nat. Chem. Biol. 5, 29-36.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 29-36
    • Prakash, S.1    Inobe, T.2    Hatch, A.J.3    Matouschek, A.4
  • 8
    • 67651208925 scopus 로고    scopus 로고
    • Adapting the machine: Adaptor proteins for Hsp100/Clp and AAA+ proteases
    • Kirstein, J., Moliere, N., Dougan, D. A., and Turgay, K. (2009) Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases. Nat. Rev. Micro. 7, 589-599.
    • (2009) Nat. Rev. Micro. , vol.7 , pp. 589-599
    • Kirstein, J.1    Moliere, N.2    Dougan, D.A.3    Turgay, K.4
  • 9
    • 79958140971 scopus 로고    scopus 로고
    • The Clp protease system; a central component of the chloroplast protease network
    • Olinares, P. D., Kim, J., and van Wijk, K. J. (2011) The Clp protease system; a central component of the chloroplast protease network. Biochim. Biophys. Acta. 1807, 999-1011.
    • (2011) Biochim. Biophys. Acta. , vol.1807 , pp. 999-1011
    • Olinares, P.D.1    Kim, J.2    Van Wijk, K.J.3
  • 10
    • 75349107775 scopus 로고    scopus 로고
    • Diverse functions of mitochondrial AAA+ proteins: Protein activation, disaggregation, and degradation
    • Truscott, K. N., Lowth, B. R., Strack, P. R., and Dougan, D. A. (2010) Diverse functions of mitochondrial AAA+ proteins: protein activation, disaggregation, and degradation. Biochem. Cell. Biol. 88, 97-108.
    • (2010) Biochem. Cell. Biol. , vol.88 , pp. 97-108
    • Truscott, K.N.1    Lowth, B.R.2    Strack, P.R.3    Dougan, D.A.4
  • 11
    • 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., and Flanagan, J. M. (1997) The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91, 447-456. (Pubitemid 27508234)
    • (1997) Cell , vol.91 , Issue.4 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 12
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • DOI 10.1016/j.cell.2005.04.012, PII S0092867405003922
    • Hinnerwisch, J., Fenton, W. A., Furtak, K. J., Farr, G. W., and Horwich, A. L. (2005) Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041. (Pubitemid 40894633)
    • (2005) Cell , vol.121 , Issue.7 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 13
    • 77951567636 scopus 로고    scopus 로고
    • The bacterial N-end rule pathway: Expect the unexpected
    • Dougan, D. A., Truscott, K. N., and Zeth, K. (2010) The bacterial N-end rule pathway: expect the unexpected. Mol. Microbiol. 76, 545-558.
    • (2010) Mol. Microbiol. , vol.76 , pp. 545-558
    • Dougan, D.A.1    Truscott, K.N.2    Zeth, K.3
  • 14
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • Moore, S. D. and Sauer, R. T. (2007) The tmRNA system for translational surveillance and ribosome rescue. Annu. Rev. Biochem. 76, 101-124.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 15
    • 0034596991 scopus 로고    scopus 로고
    • Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: The role of trans recognition in UmuD0 stability
    • Gonzalez, M., Rasulova, F., Maurizi, M. R., and Woodgate, R. (2000) Subunit-specific degradation of the UmuD/D' heterodimer by the ClpXP protease: the role of trans recognition in UmuD0 stability. EMBO J. 19, 5251-5258.
    • (2000) EMBO J. , vol.19 , pp. 5251-5258
    • Gonzalez, M.1    Rasulova, F.2    Maurizi, M.R.3    Woodgate, R.4
  • 16
    • 0037740010 scopus 로고    scopus 로고
    • Latent ClpX-recognition signals ensure LexA destruction after DNA damage
    • DOI 10.1101/gad.1078003
    • Neher, S. B., Flynn, J. M., Sauer, R. T., and Baker, T. A. (2003) Latent ClpX-recognition signals ensure LexA destruction after DNA damage. Genes Dev. 17, 1084-1089. (Pubitemid 36534983)
    • (2003) Genes and Development , vol.17 , Issue.9 , pp. 1084-1089
    • Neher, S.B.1    Flynn, J.M.2    Sauer, R.T.3    Baker, T.A.4
  • 17
    • 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., and Sauer, R. T. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12, 1338-1347. (Pubitemid 28213409)
    • (1998) Genes and Development , vol.12 , Issue.9 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 18
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition, it all depends on their partner in crime
    • DOI 10.1016/S0014-5793(02)03179-4, PII S0014579302031794
    • Dougan, D. A., Mogk, A., Zeth, K., Turgay, K., and Bukau, B. (2002) AAA+ proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett. 529, 6-10. (Pubitemid 35283903)
    • (2002) FEBS Letters , vol.529 , Issue.1 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 19
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • DOI 10.1016/S1097-2765(02)00485-9
    • Dougan, D. A., Reid, B. G., Horwich, A. L., and Bukau, B. (2002) ClpS, a substrate modulator of the ClpAP machine. Mol. Cell 9, 673-683. (Pubitemid 34273796)
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 20
    • 0141957392 scopus 로고    scopus 로고
    • Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX
    • DOI 10.1016/j.molcel.2003.08.012
    • Dougan, D. A., Weber-Ban, E., and Bukau, B. (2003) Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX. Mol. Cell 12, 373-380. (Pubitemid 37238924)
    • (2003) Molecular Cell , vol.12 , Issue.2 , pp. 373-380
    • Dougan, D.A.1    Weber-Ban, E.2    Bukau, B.3
  • 21
    • 67649552963 scopus 로고    scopus 로고
    • Modification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli
    • Ninnis, R. L., Spall, S. K., Talbo, G. H., Truscott, K. N., and Dougan, D. A. (2009) Modification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli. EMBO J. 28, 1732-1744.
    • (2009) EMBO J. , vol.28 , pp. 1732-1744
    • Ninnis, R.L.1    Spall, S.K.2    Talbo, G.H.3    Truscott, K.N.4    Dougan, D.A.5
  • 22
    • 0037195961 scopus 로고    scopus 로고
    • + chaperone, ClpA
    • DOI 10.1074/jbc.M208104200
    • Guo, F., Esser, L., Singh, S. K., Maurizi, M. R., and Xia, D. (2002) Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. J. Biol. Chem. 277, 46753-46762. (Pubitemid 35417678)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46753-46762
    • Guo, F.1    Esser, L.2    Singh, S.K.3    Maurizi, M.R.4    Xia, D.5
  • 23
    • 0036896886 scopus 로고    scopus 로고
    • Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA
    • DOI 10.1038/nsb869
    • Zeth, K., Ravelli, R. B., Paal, K., Cusack, S., Bukau, B., and Dougan, D. A. (2002) Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Nat. Struct. Biol. 9, 906-911. (Pubitemid 35417058)
    • (2002) Nature Structural Biology , vol.9 , Issue.12 , pp. 906-911
    • Zeth, K.1    Ravelli, R.B.2    Paal, K.3    Cusack, S.4    Bukau, B.5    Dougan, D.A.6
  • 24
    • 40949141846 scopus 로고    scopus 로고
    • Distinct structural elements of the adaptor ClpS are required for regulating degradation by ClpAP
    • DOI 10.1038/nsmb.1392, PII NSMB1392
    • Hou, J. Y., Sauer, R. T., and Baker, T. A. (2008) Distinct structural elements of the adaptor ClpS are required for regulating degradation by ClpAP. Nat. Struct. Mol. Biol. 15, 288-294. (Pubitemid 351654046)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.3 , pp. 288-294
    • Hou, J.Y.1    Sauer, R.T.2    Baker, T.A.3
  • 25
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • DOI 10.1016/S1097-2765(03)00060-1
    • Flynn, J. M., Neher, S. B., Kim, Y. I., Sauer, R. T., and Baker, T. A. (2003) Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11, 671-683. (Pubitemid 36388762)
    • (2003) Molecular Cell , vol.11 , Issue.3 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.-I.3    Sauer, R.T.4    Baker, T.A.5
  • 26
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • DOI 10.1046/j.1365-2958.2001.02383.x
    • Tomoyasu, T., Mogk, A., Langen, H., Goloubinoff, P., and Bukau, B. (2001) Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microbiol. 40, 397-413. (Pubitemid 32391634)
    • (2001) Molecular Microbiology , vol.40 , Issue.2 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 27
    • 0141992126 scopus 로고    scopus 로고
    • Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag
    • DOI 10.1016/j.molcel.2003.08.014
    • Levchenko, I., Grant, R. A., Wah, D. A., Sauer, R. T., and Baker, T. A. (2003) Structure of a delivery protein for an AAA+ protease in complex with a peptide degradation tag. Mol. Cell 12, 365-372. (Pubitemid 37238923)
    • (2003) Molecular Cell , vol.12 , Issue.2 , pp. 365-372
    • Levchenko, I.1    Grant, R.A.2    Wah, D.A.3    Sauer, R.T.4    Baker, T.A.5
  • 28
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko, I., Seidel, M., Sauer, R. T., and Baker, T. A. (2000) A specificity-enhancing factor for the ClpXP degradation machine. Science 289, 2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 29
    • 0043128700 scopus 로고    scopus 로고
    • Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine
    • DOI 10.1016/S1097-2765(03)00271-5
    • Song, H. K. and Eck, M. J. (2003) Structural basis of degradation signal recognition by SspB, a specificity-enhancing factor for the ClpXP proteolytic machine. Mol. Cell 12, 75-86. (Pubitemid 36957833)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 75-86
    • Song, H.K.1    Eck, M.J.2
  • 30
    • 71749093772 scopus 로고    scopus 로고
    • Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli
    • Hengge, R. (2009) Proteolysis of sigmaS (RpoS) and the general stress response in Escherichia coli. Res. Microbiol. 160, 667-676.
    • (2009) Res. Microbiol. , vol.160 , pp. 667-676
    • Hengge, R.1
  • 31
    • 0029990928 scopus 로고    scopus 로고
    • The response regulator RssB controls stability of the sigma (S) subunit of RNA polymerase in Escherichia coli
    • Muffler, A., Fischer, D., Altuvia, S., Storz, G., and Hengge-Aronis, R. (1996) The response regulator RssB controls stability of the sigma (S) subunit of RNA polymerase in Escherichia coli. EMBO J. 15, 1333-1339.
    • (1996) EMBO J. , vol.15 , pp. 1333-1339
    • Muffler, A.1    Fischer, D.2    Altuvia, S.3    Storz, G.4    Hengge-Aronis, R.5
  • 33
    • 41049111259 scopus 로고    scopus 로고
    • S (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors
    • DOI 10.1111/j.1365-2958.2008.06146.x
    • Bougdour, A., Cunning, C., Baptiste, P. J., Elliott, T., and Gottesman, S. (2008) Multiple pathways for regulation of sigmaS (RpoS) stability in Escherichia coli via the action of multiple anti-adaptors. Mol. Microbiol. 68, 298-313. (Pubitemid 351422952)
    • (2008) Molecular Microbiology , vol.68 , Issue.2 , pp. 298-313
    • Bougdour, A.1    Cunning, C.2    Baptiste, P.J.3    Elliott, T.4    Gottesman, S.5
  • 35
    • 33645522854 scopus 로고    scopus 로고
    • Modulating RssB activity: IraP, a novel regulator of sigma (S) stability in Escherichia coli
    • Bougdour, A., Wickner, S., and Gottesman, S. (2006) Modulating RssB activity: IraP, a novel regulator of sigma (S) stability in Escherichia coli. Genes Dev. 20, 884-897.
    • (2006) Genes Dev. , vol.20 , pp. 884-897
    • Bougdour, A.1    Wickner, S.2    Gottesman, S.3
  • 36
    • 0033568606 scopus 로고    scopus 로고
    • The Escherichia coli σ;(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ; factor
    • DOI 10.1101/gad.13.18.2449
    • Ades, S. E., Connolly, L. E., Alba, B. M., and Gross, C. A. (1999) The Escherichia coli sigma (E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Genes Dev. 13, 2449-2461. (Pubitemid 29453615)
    • (1999) Genes and Development , vol.13 , Issue.18 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 37
    • 0030998321 scopus 로고    scopus 로고
    • The σ;(E) and the Cpx signal transduction systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • Danese, P. N. and Silhavy, T. J. (1997) The sigma (E) and the Cpx signal transduction systems control the synthesis of periplasmic proteinfolding enzymes in Escherichia coli. Genes Dev. 11, 1183-1193. (Pubitemid 27225226)
    • (1997) Genes and Development , vol.11 , Issue.9 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 38
    • 0027787823 scopus 로고
    • The activity of sigmaE, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins
    • Mecsas, J., Rouviere, P. E., Erickson, J. W., Donohue, T. J., and Gross, C. A. (1993) The activity of sigmaE, an Escherichia coli heat-inducible sigma-factor, is modulated by expression of outer membrane proteins. Genes Dev. 7, 2618-2628.
    • (1993) Genes Dev. , vol.7 , pp. 2618-2628
    • Mecsas, J.1    Rouviere, P.E.2    Erickson, J.W.3    Donohue, T.J.4    Gross, C.A.5
  • 39
    • 56949096401 scopus 로고    scopus 로고
    • Regulation by destruction, design of the sigmaE envelope stress response
    • Ades, S. E. (2008) Regulation by destruction, design of the sigmaE envelope stress response. Curr. Opin. Microbiol. 11, 535-540.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 535-540
    • Ades, S.E.1
  • 40
    • 31144454629 scopus 로고    scopus 로고
    • Conserved and variable functions of the sigmaE stress response in related genomes
    • Rhodius, V. A., Suh, W. C., Nonaka, G., West, J., and Gross, C. A. (2006) Conserved and variable functions of the sigmaE stress response in related genomes. PLoS Biol. 4, e2.
    • (2006) PLoS Biol. , vol.4
    • Rhodius, V.A.1    Suh, W.C.2    Nonaka, G.3    West, J.4    Gross, C.A.5
  • 41
    • 34249807616 scopus 로고    scopus 로고
    • E regulates and is regulated by a small RNA in Escherichia coli
    • DOI 10.1128/JB.00020-07
    • Thompson, K. M., Rhodius, V. A., and Gottesman, S. (2007) SigmaE regulates and is regulated by a small RNA in Escherichia coli. J. Bacteriol. 189, 4243-4256. (Pubitemid 46847373)
    • (2007) Journal of Bacteriology , vol.189 , Issue.11 , pp. 4243-4256
    • Thompson, K.M.1    Rhodius, V.A.2    Gottesman, S.3
  • 42
    • 50149107174 scopus 로고    scopus 로고
    • Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
    • Jiang, J., Zhang, X., Chen, Y., Wu, Y., Zhou, Z. H., Chang, Z., and Sui, S. F. (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
  • 43
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • DOI 10.1038/nature07004, PII NATURE07004
    • Krojer, T., Sawa, J., Schafer, E., Saibil, H. R., Ehrmann, M., and Clausen, T. (2008) Structural basis for the regulated protease and chaperone function of DegP. Nature 453, 885-890. (Pubitemid 351832567)
    • (2008) Nature , vol.453 , Issue.7197 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 44
    • 0012837562 scopus 로고    scopus 로고
    • E with the cytoplasmic domain of its anti-σ; RseA
    • DOI 10.1016/S1097-2765(03)00148-5
    • Campbell, E. A., Tupy, J. L., Gruber, T. M., Wang, S., Sharp, M. M., Gross, C. A., and Darst, S. A. (2003) Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA. Mol. Cell 11, 1067-1078. (Pubitemid 36566327)
    • (2003) Molecular Cell , vol.11 , Issue.4 , pp. 1067-1078
    • Campbell, E.A.1    Tupy, J.L.2    Gruber, T.M.3    Wang, S.4    Sharp, M.M.5    Gross, C.A.6    Darst, S.A.7
  • 45
    • 33846134757 scopus 로고    scopus 로고
    • E-mediated envelope stress response in Escherichia coli: Keys to graded, buffered, and rapid signal transduction
    • DOI 10.1101/gad.1496707
    • Chaba, R., Grigorova, I. L., Flynn, J. M., Baker, T. A., and Gross, C. A. (2007) Design principles of the proteolytic cascade governing the sigmaE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction. Genes Dev. 21, 124-136. (Pubitemid 46089713)
    • (2007) Genes and Development , vol.21 , Issue.1 , pp. 124-136
    • Chaba, R.1    Grigorova, I.L.2    Flynn, J.M.3    Baker, T.A.4    Gross, C.A.5
  • 46
    • 0030611694 scopus 로고    scopus 로고
    • σ;(E) is an essential sigma factor in Escherichia coli
    • De Las Penas, A., Connolly, L., and Gross, C. A. (1997) SigmaE is an essential sigma factor in Escherichia coli. J. Bacteriol. 179, 6862-6864. (Pubitemid 27465327)
    • (1997) Journal of Bacteriology , vol.179 , Issue.21 , pp. 6862-6864
    • De Las Penas, A.1    Connolly, L.2    Gross, C.A.3
  • 47
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli σ;(E) (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
    • Missiakas, D., Mayer, M. P., Lemaire, M., Georgopoulos, C., and Raina, S. (1997) Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol. Microbiol. 24, 355-371. (Pubitemid 27223866)
    • (1997) Molecular Microbiology , vol.24 , Issue.2 , pp. 355-371
    • Missiakas, D.1    Mayer, M.P.2    Lemaire, M.3    Georgopoulos, C.4    Raina, S.5
  • 48
    • 0037102509 scopus 로고    scopus 로고
    • DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma (E)-dependent extracytoplasmic stress response
    • Alba, B. M., Leeds, J. A., Onufryk, C., Lu, C. Z., and Gross, C. A. (2002) DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma (E)-dependent extracytoplasmic stress response. Genes Dev. 16, 2156-2168.
    • (2002) Genes Dev. , vol.16 , pp. 2156-2168
    • Alba, B.M.1    Leeds, J.A.2    Onufryk, C.3    Lu, C.Z.4    Gross, C.A.5
  • 49
    • 0034933064 scopus 로고    scopus 로고
    • E activity
    • DOI 10.1046/j.1365-2958.2001.02475.x
    • Alba, B. M., Zhong, H. J., Pelayo, J. C., and Gross, C. A. (2001) degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity. Mol. Microbiol. 40, 1323-1333. (Pubitemid 32635301)
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1323-1333
    • Alba, B.M.1    Zhong, H.J.2    Pelayo, J.C.3    Gross, C.A.4
  • 50
    • 4444377383 scopus 로고    scopus 로고
    • Modulating substrate choice: The SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation
    • DOI 10.1101/gad.1240104
    • Flynn, J. M., Levchenko, I., Sauer, R. T., and Baker, T. A. (2004) Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradation. Genes Dev. 18, 2292-2301. (Pubitemid 39209577)
    • (2004) Genes and Development , vol.18 , Issue.18 , pp. 2292-2301
    • Flynn, J.M.1    Levchenko, I.2    Sauer, R.T.3    Baker, T.A.4
  • 51
    • 0037102458 scopus 로고    scopus 로고
    • YaeL (EcfE) activates the sigma (E) pathway of stress response through a site-2 cleavage of anti-sigma (E), RseA
    • Kanehara, K., Ito, K., and Akiyama, Y. (2002) YaeL (EcfE) activates the sigma (E) pathway of stress response through a site-2 cleavage of anti-sigma (E), RseA. Genes Dev. 16, 2147-2155.
    • (2002) Genes Dev. , vol.16 , pp. 2147-2155
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 53
    • 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
    • DOI 10.1016/S0092-8674(03)00203-4
    • Walsh, N. P., Alba, B. M., Bose, B., Gross, C. A., and Sauer, R. T. (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. (Pubitemid 36411960)
    • (2003) Cell , vol.113 , Issue.1 , pp. 61-71
    • Walsh, N.P.1    Alba, B.M.2    Bose, B.3    Gross, C.A.4    Sauer, R.T.5
  • 56
    • 34548394160 scopus 로고    scopus 로고
    • The Structure of RseB: A Sensor in Periplasmic Stress Response of E. coli
    • DOI 10.1016/j.jmb.2007.06.039, PII S0022283607008339
    • Wollmann, P., and Zeth, K. (2007) The structure of RseB: a sensor in periplasmic stress response of E. coli. J. Mol. Biol. 372, 927-941. (Pubitemid 47368341)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.4 , pp. 927-941
    • Wollmann, P.1    Zeth, K.2
  • 58
    • 10044241602 scopus 로고    scopus 로고
    • RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences
    • DOI 10.1038/sj.emboj.7600449
    • Akiyama, Y., Kanehara, K., and Ito, K. (2004) RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences. EMBO J. 23, 4434-4442. (Pubitemid 39601968)
    • (2004) EMBO Journal , vol.23 , Issue.22 , pp. 4434-4442
    • Akiyama, Y.1    Kanehara, K.2    Ito, K.3
  • 59
    • 44349189894 scopus 로고    scopus 로고
    • Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease
    • Koide, K., Ito, K., and Akiyama, Y. (2008) Substrate recognition and binding by RseP, an Escherichia coli intramembrane protease. J. Biol. Chem. 283, 9562-9570.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9562-9570
    • Koide, K.1    Ito, K.2    Akiyama, Y.3
  • 61
    • 0037447049 scopus 로고    scopus 로고
    • Mechanisms of protein import into mitochondria
    • DOI 10.1016/S0960-9822(03)00239-2
    • Truscott, K. N., Brandner, K., and Pfanner, N. (2003) Mechanisms of protein import into mitochondria. Curr. Biol. 13, R326-337. (Pubitemid 36453308)
    • (2003) Current Biology , vol.13 , Issue.8
    • Truscott, K.N.1    Brandner, K.2    Pfanner, N.3
  • 62
    • 4944234936 scopus 로고    scopus 로고
    • Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones
    • DOI 10.1242/jcs.01275
    • Yoneda, T., Benedetti, C., Urano, F., Clark, S. G., Harding, H. P., and Ron, D. (2004) Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones. J. Cell. Sci. 117, 4055-4066. (Pubitemid 39328294)
    • (2004) Journal of Cell Science , vol.117 , Issue.18 , pp. 4055-4066
    • Yoneda, T.1    Benedetti, C.2    Urano, F.3    Clark, S.G.4    Harding, H.P.5    Ron, D.6
  • 63
    • 0037009521 scopus 로고    scopus 로고
    • A mitochondrial specific stress response in mammalian cells
    • DOI 10.1093/emboj/cdf445
    • Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., and Hoogenraad, N. J. (2002) A mitochondrial specific stress response in mammalian cells. EMBO J. 21, 4411-4419. (Pubitemid 34984328)
    • (2002) EMBO Journal , vol.21 , Issue.17 , pp. 4411-4419
    • Zhao, Q.1    Wang, J.2    Levichkin, I.V.3    Stasinopoulos, S.4    Ryan, M.T.5    Hoogenraad, N.J.6
  • 64
    • 33748901113 scopus 로고    scopus 로고
    • Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response
    • DOI 10.1534/genetics.106.061580
    • Benedetti, C., Haynes, C. M., Yang, Y., Harding, H. P., and Ron, D. (2006) Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response. Genetics 174, 229-239. (Pubitemid 44427668)
    • (2006) Genetics , vol.174 , Issue.1 , pp. 229-239
    • Benedetti, C.1    Haynes, C.M.2    Yang, Y.3    Harding, H.P.4    Ron, D.5
  • 65
    • 0029825891 scopus 로고    scopus 로고
    • Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome
    • Martinus, R. D., Garth, G. P., Webster, T. L., Cartwright, P., Naylor, D. J., Hoj, P. B., and Hoogenraad, N. J. (1996) Selective induction of mitochondrial chaperones in response to loss of the mitochondrial genome. Eur. J. Biochem. 240, 98-103. (Pubitemid 26276759)
    • (1996) European Journal of Biochemistry , vol.240 , Issue.1 , pp. 98-103
    • Hoogenraad, N.J.1
  • 66
    • 37849038317 scopus 로고    scopus 로고
    • The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response
    • Horibe, T. and Hoogenraad, N. J. (2007) The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. PLoS ONE 2, e835.
    • (2007) PLoS ONE , vol.2
    • Horibe, T.1    Hoogenraad, N.J.2
  • 67
    • 37849048003 scopus 로고    scopus 로고
    • Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements
    • Aldridge, J. E., Horibe, T., and Hoogenraad, N. J. (2007) Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements. PLoS ONE 2, e874.
    • (2007) PLoS ONE , vol.2
    • Aldridge, J.E.1    Horibe, T.2    Hoogenraad, N.J.3
  • 68
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron, D. and Walter, P. (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell. Biol. 8, 519-529. (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 69
    • 34848861368 scopus 로고    scopus 로고
    • ClpP Mediates Activation of a Mitochondrial Unfolded Protein Response in C. elegans
    • DOI 10.1016/j.devcel.2007.07.016, PII S1534580707002778
    • Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y., and Ron, D. (2007) ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell 13, 467-480. (Pubitemid 47500805)
    • (2007) Developmental Cell , vol.13 , Issue.4 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 70
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C
    • Haynes, C. M., Yang, Y., Blais, S. P., Neubert, T. A., and Ron, D. (2010) The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol. Cell 37, 529-540.
    • (2010) Elegans. Mol. Cell. , vol.37 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4    Ron, D.5
  • 71
    • 59449100177 scopus 로고    scopus 로고
    • Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex
    • Dunn, C. D., Tamura, Y., Sesaki, H., and Jensen, R. E. (2008) Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex. Mol. Biol. Cell 19, 5387-5397.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 5387-5397
    • Dunn, C.D.1    Tamura, Y.2    Sesaki, H.3    Jensen, R.E.4


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