메뉴 건너뛰기




Volumn 9, Issue 2, 2013, Pages 90-96

Allosteric regulation of DegS protease subunits through a shared energy landscape

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DEGS PROTEASE; OUTER MEMBRANE PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84872683928     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1135     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 81755174173 scopus 로고    scopus 로고
    • The structural basis of mode of activation and functional diversity: A case study with HtrA family of serine proteases
    • Singh, N., Kuppili, R.R. & Bose, K. 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).
    • (2011) Arch. Biochem. Biophys , vol.516 , pp. 1-96
    • Singh, N.1    Kuppili, R.R.2    Bose, K.3
  • 2
    • 20944444077 scopus 로고    scopus 로고
    • Implications of the serine protease HtrA1 in amyloid precursor protein processing
    • USA
    • Grau, S. et al. Implications of the serine protease HtrA1 in amyloid precursor protein processing. Proc. Natl. Acad. Sci. USA 102, 6021-6026 (2005).
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 6021-6026
    • Grau, S.1
  • 3
  • 4
    • 57349169295 scopus 로고    scopus 로고
    • Emerging roles of serine proteinases in tissue turnover in arthritis
    • Milner, J.M., Patel, A. & Rowan, A.D. Emerging roles of serine proteinases in tissue turnover in arthritis. Arthritis Rheum. 58, 3644-3656 (2008).
    • (2008) Arthritis Rheum , vol.58 , pp. 3644-3656
    • Milner, J.M.1    Patel, A.2    Rowan, A.D.3
  • 5
    • 39449115415 scopus 로고    scopus 로고
    • The mitochondrial serine protease HtrA2/Omi: An overview
    • Vande Walle, L., Lamkanfi, M. & Vandenabeele, P. The mitochondrial serine protease HtrA2/Omi: an overview. Cell Death Differ. 15, 453-460 (2008).
    • (2008) Cell Death Differ , vol.15 , pp. 453-460
    • Vande Walle, L.1    Lamkanfi, M.2    Vandenabeele, P.3
  • 6
    • 67649305413 scopus 로고    scopus 로고
    • HtrA serine proteases as potential therapeutic targets in cancer
    • Chien, J., Campioni, M., Shridhar, V. & Baldi, A. HtrA serine proteases as potential therapeutic targets in cancer. Curr. Cancer Drug Targets 9, 451-468 (2009).
    • (2009) Curr. Cancer Drug Targets , vol.9 , pp. 451-468
    • Chien, J.1    Campioni, M.2    Shridhar, V.3    Baldi, A.4
  • 7
    • 65949097072 scopus 로고    scopus 로고
    • Association of HTRA1 mutations and familial ischemic cerebral small-vessel disease
    • Hara, K. et al. Association of HTRA1 mutations and familial ischemic cerebral small-vessel disease. N. Engl. J. Med. 360, 1729-1739 (2009).
    • (2009) N. Engl. J. Med , vol.360 , pp. 1729-1739
    • Hara, K.1
  • 8
    • 77955421829 scopus 로고    scopus 로고
    • High-temperature requirement factor A3 (Htra3): A novel serine protease and its potential role in ovarian function and ovarian cancers
    • Bowden, M.A. et al. High-temperature requirement factor A3 (Htra3): a novel serine protease and its potential role in ovarian function and ovarian cancers. Mol. Cell. Endocrinol. 327, 13-18 (2010).
    • (2010) Mol. Cell. Endocrinol , vol.327 , pp. 1-18
    • Bowden, M.A.1
  • 9
    • 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
    • Walsh, N.P., Alba, B.M., Bose, B., Gross, C.A. & Sauer, R.T. 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).
    • (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
  • 10
    • 2442563573 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli σe-dependent envelope stress response
    • Alba, B.M. & Gross, C.A. Regulation of the Escherichia coli σE-dependent envelope stress response. Mol. Microbiol. 52, 613-619 (2004).
    • (2004) Mol. Microbiol , vol.52 , pp. 613-619
    • Alba, B.M.1    Gross, C.A.2
  • 11
    • 0030066650 scopus 로고    scopus 로고
    • Characterization of degQ and degS Escherichia coli genes encoding homologs of the DegP protease
    • Waller, P.R. & Sauer, R.T. Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease. J. Bacteriol. 178, 1146-1153 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 1146-1153
    • Waller, P.R.1    Sauer, R.T.2
  • 12
    • 0030611303 scopus 로고    scopus 로고
    • The σe-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of σe
    • De Las Peñas, A., Connolly, L. & Gross, C.A. The σE-mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of σE. Mol. Microbiol. 24, 373-385 (1997).
    • (1997) Mol. Microbiol , vol.24 , pp. 373-385
    • De Las Peñas, A.1    Connolly, L.2    Gross, C.A.3
  • 13
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli σe (RpoE) heat-shock transcription-factor activity by the RseA RseB and RseC proteins
    • Missiakas, D., Mayer, M.P., Lemaire, M., Georgopoulos, C. & Raina, S. Modulation of the Escherichia coli σE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol. Microbiol. 24, 355-371 (1997).
    • (1997) Mol. Microbiol , vol.24 , pp. 355-371
    • Missiakas, D.1    Mayer, M.P.2    Lemaire, M.3    Georgopoulos, C.4    Raina, S.5
  • 14
    • 0012837562 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli σe with the cytoplasmic domain of its anti-σ RseA
    • Campbell, E.A. et al. Crystal structure of Escherichia coli σE with the cytoplasmic domain of its anti-σ RseA. Mol. Cell 11, 1067-1078 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1067-1078
    • Campbell, E.A.1
  • 15
    • 0344453810 scopus 로고    scopus 로고
    • Regulation of the alternative σ factor σe during initiation, adaptation, and shutoff of the extracytoplasmic heat shock response in Escherichia coli
    • Ades, S.E., Grigorova, I.L. & Gross, C.A. Regulation of the alternative σ factor σE during initiation, adaptation, and shutoff of the extracytoplasmic heat shock response in Escherichia coli. J. Bacteriol. 185, 2512-2519 (2003).
    • (2003) J. Bacteriol , vol.185 , pp. 2512-2519
    • Ades, S.E.1    Grigorova, I.L.2    Gross, C.A.3
  • 16
    • 0037102458 scopus 로고    scopus 로고
    • YaeL (EcfE) activates the σe pathway of stress response through a site-2 cleavage of anti-σE RseA
    • Kanehara, K., Ito, K. & Akiyama, Y. YaeL (EcfE) activates the σE pathway of stress response through a site-2 cleavage of anti-σE, RseA. Genes Dev. 16, 2147-2155 (2002).
    • (2002) Genes Dev , vol.16 , pp. 2147-2155
    • Kanehara, K.1    Ito, K.2    Akiyama, Y.3
  • 17
    • 10044241602 scopus 로고    scopus 로고
    • RseP (YaeL) an Escherichia coli RIP protease, cleaves transmembrane sequences
    • Akiyama, Y., Kanehara, K. & Ito, K. RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences. EMBO J. 23, 4434-4442 (2004).
    • (2004) EMBO J , vol.23 , pp. 4434-4442
    • Akiyama, Y.1    Kanehara, K.2    Ito, K.3
  • 18
    • 70349299921 scopus 로고    scopus 로고
    • Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage
    • USA
    • Li, X. et al. Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage. Proc. Natl. Acad. Sci. USA 106, 14837-14842 (2009).
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 14837-14842
    • Li, X.1
  • 19
    • 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
    • Flynn, J.M., Levchenko, I., Sauer, R.T. & Baker, T.A. 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 (2004).
    • (2004) Genes Dev , vol.18 , pp. 2292-2301
    • Flynn, J.M.1    Levchenko, I.2    Sauer, R.T.3    Baker, T.A.4
  • 20
    • 33846134757 scopus 로고    scopus 로고
    • Design principles of the proteolytic cascade governing the σe-mediated envelope stress response in Escherichia coli: Keys to graded, buffered, and rapid signal transduction
    • Chaba, R., Grigorova, I.L., Flynn, J.M., Baker, T.A. & Gross, C.A. Design principles of the proteolytic cascade governing the σE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transduction. Genes Dev. 21, 124-136 (2007).
    • (2007) Genes Dev , vol.21 , pp. 124-136
    • Chaba, R.1    Grigorova, I.L.2    Flynn, J.M.3    Baker, T.A.4    Gross, C.A.5
  • 21
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • Wilken, C., Kitzing, K., Kurzbauer, R., Ehrmann, M. & Clausen, T. Crystal structure of the DegS stress sensor: how a PDZ domain recognizes misfolded protein and activates a protease. Cell 117, 483-494 (2004).
    • (2004) Cell , vol.117 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 22
    • 3042644567 scopus 로고    scopus 로고
    • Structural analysis of DegS, a stress sensor of the bacterial periplasm
    • Zeth, K. Structural analysis of DegS, a stress sensor of the bacterial periplasm. FEBS Lett. 569, 351-358 (2004).
    • (2004) FEBS Lett , vol.569 , pp. 351-358
    • Zeth, K.1
  • 23
    • 35548973933 scopus 로고    scopus 로고
    • Allosteric activation of DegS, a stress sensor PDZ protease
    • Sohn, J., Grant, R.A. & Sauer, R.T. Allosteric activation of DegS, a stress sensor PDZ protease. Cell 131, 572-583 (2007).
    • (2007) Cell , vol.131 , pp. 572-583
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 24
    • 77958563467 scopus 로고    scopus 로고
    • Allostery is an intrinsic property of the protease domain of DegS: Implications for enzyme function and evolution
    • Sohn, J., Grant, R.A. & Sauer, R.T. Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution. J. Biol. Chem. 285, 34039-34047 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 1-34047
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 25
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. & Changeux, J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12, 88-118 (1965).
    • (1965) J. Mol. Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 26
    • 58149287846 scopus 로고    scopus 로고
    • OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations
    • Sohn, J. & Sauer, R.T. OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations. Mol. Cell 33, 64-74 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 64-74
    • Sohn, J.1    Sauer, R.T.2
  • 27
    • 70349779534 scopus 로고    scopus 로고
    • OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism
    • Sohn, J., Grant, R.A. & Sauer, R.T. OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism. Structure 17, 1411-1421 (2009).
    • (2009) Structure , vol.17 , pp. 1411-1421
    • Sohn, J.1    Grant, R.A.2    Sauer, R.T.3
  • 28
    • 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
    • Hasselblatt, H. et al. 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).
    • (2007) Genes Dev , vol.21 , pp. 2659-2670
    • Hasselblatt, H.1
  • 29
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui, Q. & Karplus, M. Allostery and cooperativity revisited. Protein Sci. 17, 1295-1307 (2008).
    • (2008) Protein Sci , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 30
    • 68149157248 scopus 로고    scopus 로고
    • The origin of allosteric functional modulation: Multiple pre-existing pathways
    • del Sol, A., Tsai, C.J., Ma, B. & Nussinov, R. The origin of allosteric functional modulation: multiple pre-existing pathways. Structure 17, 1042-1050 (2009).
    • (2009) Structure , vol.17 , pp. 1042-1050
    • Del Sol, A.1    Tsai, C.J.2    Ma, B.3    Nussinov, R.4
  • 31
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: The serine hydrolases
    • USA
    • Liu, Y., Patricelli, M.P. & Cravatt, B.F. Activity-based protein profiling: the serine hydrolases. Proc. Natl. Acad. Sci. USA 96, 14694-14699 (1999).
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 32
    • 0035949616 scopus 로고    scopus 로고
    • Isolation of an individual allosteric interaction in tetrameric phosphofructokinase from Bacillus stearothermophilus
    • Kimmel, J.L. & Reinhart, G.D. Isolation of an individual allosteric interaction in tetrameric phosphofructokinase from Bacillus stearothermophilus. Biochemistry 40, 11623-11629 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11623-11629
    • Kimmel, J.L.1    Reinhart, G.D.2
  • 33
    • 0034919395 scopus 로고    scopus 로고
    • Transthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins
    • Schneider, F., Hammarström, P. & Kelly, J.W. Transthyretin slowly exchanges subunits under physiological conditions: a convenient chromatographic method to study subunit exchange in oligomeric proteins. Protein Sci. 10, 1606-1613 (2001).
    • (2001) Protein Sci , vol.10 , pp. 1606-1613
    • Schneider, F.1    Hammarström, P.2    Kelly, J.W.3
  • 34
    • 79951967246 scopus 로고    scopus 로고
    • HTRA proteases: Regulated proteolysis in protein quality control
    • Clausen, T., Kaiser, M., Huber, R. & Ehrmann, M. HTRA proteases: regulated proteolysis in protein quality control. Nat. Rev. Mol. Cell Biol. 12, 152-162 (2011).
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 1-162
    • Clausen, T.1    Kaiser, M.2    Huber, R.3    Ehrmann, M.4
  • 36
    • 0001163089 scopus 로고
    • Kinetics of reaction control and information transfer in enzymes and nucleic acids
    • Eigen, M. Kinetics of reaction control and information transfer in enzymes and nucleic acids. Nobel Symp. 5, 333-369 (1967).
    • (1967) Nobel Symp , vol.5 , pp. 333-369
    • Eigen, M.1
  • 37
    • 0015231037 scopus 로고
    • Regulation of enzyme activity the activity of enzymes can be controlled by a multiplicity of conformational equilibria
    • Hammes, G.G. & Wu, C.W. Regulation of enzyme activity. The activity of enzymes can be controlled by a multiplicity of conformational equilibria. Science 172, 1205-1211 (1971).
    • (1971) Science , vol.172 , pp. 1205-1211
    • Hammes, G.G.1    Wu, C.W.2
  • 38
    • 79959468179 scopus 로고    scopus 로고
    • β-Barrel membrane protein assembly by the Bam complex
    • Hagan, C.L., Silhavy, T.J. & Kahne, D. β-Barrel membrane protein assembly by the Bam complex. Annu. Rev. Biochem. 80, 189-210 (2011).
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 1-210
    • Hagan, C.L.1    Silhavy, T.J.2    Kahne, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.