메뉴 건너뛰기




Volumn 435, Issue 1, 2011, Pages 167-174

A new principle of oligomerization of plant DEG7 protease based on interactions of degenerated protease domains

Author keywords

Arabidopsis thaliana; Complex formation; DEG7; Degenerated protease domain; Serine protease; Taxonomic distribution

Indexed keywords

DEGRADATION OF PERIPLASMIC PROTEIN 7; PROTEINASE; RECOMBINANT PROTEIN; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 79952852360     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101613     Document Type: Article
Times cited : (15)

References (42)
  • 1
    • 25444491980 scopus 로고    scopus 로고
    • Structure and function of HtrA family proteins, the key players in protein quality control
    • Kim, D. Y. and Kim, K. K. (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
  • 2
    • 0036752926 scopus 로고    scopus 로고
    • The HtrA family of proteases: Implications for protein composition and cell fate
    • DOI 10.1016/S1097-2765(02)00658-5
    • Clausen, T., Southan, C. and Ehrmann, M. (2002) The HtrA family of proteases: implications for protein composition and cell fate. Mol. Cell 10, 443-455 (Pubitemid 35284166)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 443-455
    • Clausen, T.1    Southan, C.2    Ehrmann, M.3
  • 5
    • 57749091634 scopus 로고    scopus 로고
    • The DEG15 serine protease cleaves peroxisomal targeting signal 2-containing proteins in Arabidopsis
    • DOI 10.1104/pp.108.125377
    • Schuhmann, H., Huesgen, P. F., Gietl, C. and Adamska, I. (2008) The DEG15 serine protease cleaves peroxisomal targeting signal 2-containing proteins in Arabidopsis thaliana . Plant Physiol. 148, 1847-1856 (Pubitemid 352847459)
    • (2008) Plant Physiology , vol.148 , Issue.4 , pp. 1847-1856
    • Schuhmann, H.1    Huesgen, P.F.2    Gietl, C.3    Adamska, I.4
  • 6
    • 34250636225 scopus 로고    scopus 로고
    • Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis
    • DOI 10.1105/tpc.106.049510
    • Sun, X., Peng, L., Guo, J., Chi, W., Ma, J., Lu, C. and Zhang, L. (2007) Formation of DEG5 and DEG8 complexes and their involvement in the degradation of photodamaged photosystem II reaction center D1 protein in Arabidopsis. Plant Cell 19, 1347-1361 (Pubitemid 46941658)
    • (2007) Plant Cell , vol.19 , Issue.4 , pp. 1347-1361
    • Sun, X.1    Peng, L.2    Guo, J.3    Chi, W.4    Ma, J.5    Lu, C.6    Zhang, L.7
  • 7
    • 0036263973 scopus 로고    scopus 로고
    • Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
    • Li, W., Srinivasula, S. M., Chai, J., Li, P., Wu, J. W., Zhang, Z., Alnemri, E. S. and 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
  • 8
    • 2342659637 scopus 로고    scopus 로고
    • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
    • DOI 10.1016/S0092-8674(04)00454-4, PII S0092867404004544
    • Wilken, C., Kitzing, K., Kurzbauer, R., Ehrmann, M. and 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 (Pubitemid 38610233)
    • (2004) Cell , vol.117 , Issue.4 , pp. 483-494
    • Wilken, C.1    Kitzing, K.2    Kurzbauer, R.3    Ehrmann, M.4    Clausen, T.5
  • 9
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • DOI 10.1038/416455a
    • Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. and Clausen, T. (2002) Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416, 455-459 (Pubitemid 34272883)
    • (2002) Nature , vol.416 , Issue.6879 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 10
    • 33846588852 scopus 로고    scopus 로고
    • The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity
    • DOI 10.1128/JB.01334-06
    • Jomaa, A., Damjanovic, D., Leong, V., Ghirlando, R., Iwanczyk, J. and 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 (Pubitemid 46183845)
    • (2007) Journal of Bacteriology , vol.189 , Issue.3 , pp. 706-716
    • Jomaa, A.1    Damjanovic, D.2    Leong, V.3    Ghirlando, R.4    Iwanczyk, J.5    Ortega, J.6
  • 11
    • 0037458675 scopus 로고    scopus 로고
    • Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima
    • Kim, D. Y., Kim, D. R., Ha, S. C., Lokanath, N. K., Lee, C. J., Hwang, H. Y. and Kim, K. K. (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
  • 12
    • 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., Schäfer, 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
  • 13
    • 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. U.S.A. 105, 11939-11944
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 14
    • 0033568606 scopus 로고    scopus 로고
    • e-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ factor
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ factor. Genes Dev. 13, 2449-2461
    • (1999) Genes Dev. , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 16
    • 0024519269 scopus 로고
    • Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures
    • Lipinska, B., Fayet, O., Baird, L. and Georgopoulos, C. (1989) Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures. J. Bacteriol. 171, 1574-1584 (Pubitemid 19080799)
    • (1989) Journal of Bacteriology , vol.171 , Issue.3 , pp. 1574-1584
    • Lipinska, B.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 17
    • 0024673026 scopus 로고
    • Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature
    • Strauch, K. L., Johnson, K. and Beckwith, J. (1989) Characterization of degP , a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J. Bacteriol. 171, 2689-2696
    • (1989) J. Bacteriol. , vol.171 , pp. 2689-2696
    • Strauch, K.L.1    Johnson, K.2    Beckwith, J.3
  • 19
    • 33846949331 scopus 로고    scopus 로고
    • Novel peroxisomal protease Tysnd1 processes PTS1- And PTS2-containing enzymes involved in β-oxidation of fatty acids
    • Kurochkin, I. V., Mizuno, Y., Konagaya, A., Sakaki, Y., Schonbach, C. and Okazaki, Y. (2007) Novel peroxisomal protease Tysnd1 processes PTS1- and PTS2-containing enzymes involved in β-oxidation of fatty acids. EMBO J. 26, 835-845
    • (2007) EMBO J. , vol.26 , pp. 835-845
    • Kurochkin, I.V.1    Mizuno, Y.2    Konagaya, A.3    Sakaki, Y.4    Schonbach, C.5    Okazaki, Y.6
  • 20
    • 17444411552 scopus 로고    scopus 로고
    • The family of Deg proteases in cyanobacteria and chloroplasts of higher plants
    • Huesgen, P. F., Schuhmann, H. and Adamska, I. (2005) The family of Deg proteases in cyanobacteria and chloroplasts of higher plants. Physiol. Plant. 123, 413-420
    • (2005) Physiol. Plant. , vol.123 , pp. 413-420
    • Huesgen, P.F.1    Schuhmann, H.2    Adamska, I.3
  • 21
    • 63049132799 scopus 로고    scopus 로고
    • The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress
    • Padmanabhan, N., Fichtner, L., Dickmanns, A., Ficner, R., Schulz, J. B. and Braus, G. H. (2009) The yeast HtrA orthologue Ynm3 is a protease with chaperone activity that aids survival under heat stress. Mol. Biol. Cell 20, 68-77
    • (2009) Mol. Biol. Cell , vol.20 , pp. 68-77
    • Padmanabhan, N.1    Fichtner, L.2    Dickmanns, A.3    Ficner, R.4    Schulz, J.B.5    Braus, G.H.6
  • 22
    • 0347917233 scopus 로고    scopus 로고
    • The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis
    • DOI 10.1242/jcs.00848
    • Fahrenkrog, B., Sauder, U. and Aebi, U. (2004) The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis. J. Cell Sci. 117, 115-126 (Pubitemid 38072126)
    • (2004) Journal of Cell Science , vol.117 , Issue.1 , pp. 115-126
    • Fahrenkrog, B.1    Sauder, U.2    Aebi, U.3
  • 23
    • 33645825191 scopus 로고    scopus 로고
    • Direct interaction of Saccharomyces cerevisiae Faa1p with the Omi/HtrA protease orthologue Ynm3p alters lipid homeostasis
    • Tong, F., Black, P. N., Bivins, L., Quackenbush, S., Ctrnacta, V. and DiRusso, C. C. (2006) Direct interaction of Saccharomyces cerevisiae Faa1p with the Omi/HtrA protease orthologue Ynm3p alters lipid homeostasis. Mol. Genet. Genomics 275, 330-343
    • (2006) Mol. Genet. Genomics , vol.275 , pp. 330-343
    • Tong, F.1    Black, P.N.2    Bivins, L.3    Quackenbush, S.4    Ctrnacta, V.5    DiRusso, C.C.6
  • 24
    • 77949497673 scopus 로고    scopus 로고
    • The stromal chloroplast Deg7 protease participates in the repair of photosystem II after photoinhibition in Arabidopsis
    • Sun, X., Fu, T., Chen, N., Guo, J., Ma, J., Zou, M., Lu, C. and Zhang, L. (2010) The stromal chloroplast Deg7 protease participates in the repair of photosystem II after photoinhibition in Arabidopsis. Plant Physiol. 152, 1263-1273
    • (2010) Plant Physiol. , vol.152 , pp. 1263-1273
    • Sun, X.1    Fu, T.2    Chen, N.3    Guo, J.4    Ma, J.5    Zou, M.6    Lu, C.7    Zhang, L.8
  • 25
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • DOI 10.1093/nar/25.17.3389
    • Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (Pubitemid 27359211)
    • (1997) Nucleic Acids Research , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 26
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan - An integration platform for the signature-recognition methods in InterPro
    • Zdobnov, E. M. and Apweiler, R. (2001) InterProScan: an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17, 847-848 (Pubitemid 32970486)
    • (2001) Bioinformatics , vol.17 , Issue.9 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 27
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Soding, J., Biegert, A. and Lupas, A. N. (2005) The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244-W248
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 28
    • 34547571027 scopus 로고    scopus 로고
    • The M-Coffee web server: A meta-method for computing multiple sequence alignments by combining alternative alignment methods
    • Moretti, S., Armougom, F., Wallace, I. M., Higgins, D. G., Jongeneel, C. V. and Notredame, C. (2007) The M-Coffee web server: a meta-method for computing multiple sequence alignments by combining alternative alignment methods. Nucleic Acids Res. 35, W645-W648
    • (2007) Nucleic Acids Res. , vol.35
    • Moretti, S.1    Armougom, F.2    Wallace, I.M.3    Higgins, D.G.4    Jongeneel, C.V.5    Notredame, C.6
  • 31
    • 34547559252 scopus 로고    scopus 로고
    • Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain
    • Zhang, Y., Appleton, B. A., Wu, P., Wiesmann, C. and Sidhu, S. S. (2007) Structural and functional analysis of the ligand specificity of the HtrA2/Omi PDZ domain. Protein Sci. 16, 1738-1750
    • (2007) Protein Sci. , vol.16 , pp. 1738-1750
    • Zhang, Y.1    Appleton, B.A.2    Wu, P.3    Wiesmann, C.4    Sidhu, S.S.5
  • 34
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz, R. D. and Woods, R. A. (2002) Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350, 87-96
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 36
    • 3042644567 scopus 로고    scopus 로고
    • Structural analysis of DegS, a stress sensor of the bacterial periplasm
    • 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
  • 37
    • 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
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 38
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications
    • Peltier, J. B., Ripoll, D. R., Friso, G., Rudella, A., Cai, Y., Ytterberg, J., Giacomelli, L., Pillardy, J. and van Wijk, K. J. (2004) Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. J. Biol. Chem. 279, 4768-4781
    • (2004) J. Biol. Chem. , vol.279 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6    Giacomelli, L.7    Pillardy, J.8    Van Wijk, K.J.9
  • 41
    • 78049264771 scopus 로고    scopus 로고
    • The 26S proteasome: Assembly and function of a destructive machine
    • Gallastegui, N. and Groll, M. (2010) The 26S proteasome: assembly and function of a destructive machine. Trends Biochem. Sci. 35, 634-642
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 634-642
    • Gallastegui, N.1    Groll, M.2
  • 42
    • 21144447324 scopus 로고    scopus 로고
    • Molecular machines for protein degradation
    • DOI 10.1002/cbic.200400313
    • Groll, M., Bochtler, M., Brandstetter, H., Clausen, T. and Huber, R. (2005) Molecular machines for protein degradation. ChemBioChem 6, 222-256 (Pubitemid 40879733)
    • (2005) ChemBioChem , vol.6 , Issue.2 , pp. 222-256
    • Groll, M.1    Bochtler, M.2    Brandstetter, H.3    Clausen, T.4    Huber, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.