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Volumn 72, Issue 1, 2009, Pages 26-40

The structural and biochemical characterizations of a novel TET peptidase complex from Pyrococcus horikoshii reveal an integrated peptide degradation system in hyperthermophilic Archaea

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE; COBALT; DIMER; MONOMER; TET PEPTIDASE; UNCLASSIFIED DRUG;

EID: 62949174473     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06600.x     Document Type: Article
Times cited : (32)

References (52)
  • 2
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N.A., Sept, D., Joseph, S., Holst, M.J. McCammon, J.A. (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc Natl Acad Sci USA 98 : 10037 10041.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz, J., Zühl, F. Seemüller, E. (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92 : 367 380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 4
    • 13844255627 scopus 로고    scopus 로고
    • Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes
    • Borissenko, L. Groll, M. (2005) Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes. J Mol Biol 346 : 1207 1219.
    • (2005) J Mol Biol , vol.346 , pp. 1207-1219
    • Borissenko, L.1    Groll, M.2
  • 6
    • 0037458547 scopus 로고    scopus 로고
    • PepN, the major Suc-LLVY-AMC-hydrolysing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and Eukarya
    • Chandu, D., Kumar, A. Nandi, D. (2003) PepN, the major Suc-LLVY-AMC-hydrolysing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and Eukarya. J Biol Chem 278 : 5548 5556.
    • (2003) J Biol Chem , vol.278 , pp. 5548-5556
    • Chandu, D.1    Kumar, A.2    Nandi, D.3
  • 7
    • 0032697046 scopus 로고    scopus 로고
    • Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Cheng, T.C., Ramakrishnan, V. Chan, S.I. (1999) Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. Protein Sci 8 : 2474 2486.
    • (1999) Protein Sci , vol.8 , pp. 2474-2486
    • Cheng, T.C.1    Ramakrishnan, V.2    Chan, S.I.3
  • 8
    • 0028773280 scopus 로고
    • Crystal structure of Aeromonas proteolytica aminopeptidase: A prototypical member of the co-catalytic zinc enzyme family
    • Chevrier, B., Schalk, C., D'Orchymont, H., Rondeau, J.M., Moras, D. Tarnus, C. (1994) Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family. Structure 2 : 283 291.
    • (1994) Structure , vol.2 , pp. 283-291
    • Chevrier, B.1    Schalk, C.2    D'Orchymont, H.3    Rondeau, J.M.4    Moras, D.5    Tarnus, C.6
  • 10
    • 0003845223 scopus 로고    scopus 로고
    • San Carlos, CA: DeLano Scientific. [WWW document]. URL
    • DeLano, W.L. (2002) The PyMOL Molecular Graphics System. San Carlos, CA : DeLano Scientific. [WWW document]. URL http://www.pymol.org
    • (2002) The PyMOL Molecular Graphics System.
    • Delano, W.L.1
  • 11
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T.J., Nielsen, J.E., McCammon, J.A. Baker, N.A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 32 : W665 W667.
    • (2004) Nucleic Acids Res , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 12
    • 14644394260 scopus 로고    scopus 로고
    • Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii
    • Durá, M.A., Receveur-Brechot, V., Andrieu, J.-P., Ebel, C., Schoehn, G., Roussel, A. Franzetti, B. (2005) Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemistry 44 : 3477 3486.
    • (2005) Biochemistry , vol.44 , pp. 3477-3486
    • Durá, M.A.1    Receveur-Brechot, V.2    Andrieu, J.-P.3    Ebel, C.4    Schoehn, G.5    Roussel, A.6    Franzetti, B.7
  • 13
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 : 2126 2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 16
    • 0031705698 scopus 로고    scopus 로고
    • Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus
    • Ghosh, M., Grunden, A.M., Dunn, D.M., Weiss, R. Adams, M.W. (1998) Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol 180 : 4781 4789.
    • (1998) J Bacteriol , vol.180 , pp. 4781-4789
    • Ghosh, M.1    Grunden, A.M.2    Dunn, D.M.3    Weiss, R.4    Adams, M.W.5
  • 17
    • 0034194703 scopus 로고    scopus 로고
    • Physiology and continuous culture of the hyperthermophilic deep-sea vent archaeon Pyrococcus abyssi ST549
    • Godfroy, A., Raven, N.D. Sharp, R.J. (2000) Physiology and continuous culture of the hyperthermophilic deep-sea vent archaeon Pyrococcus abyssi ST549. FEMS Microbiol Lett 186 : 127 132.
    • (2000) FEMS Microbiol Lett , vol.186 , pp. 127-132
    • Godfroy, A.1    Raven, N.D.2    Sharp, R.J.3
  • 18
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: Properties and functions
    • Gonzales, T. Robert-Baudouy, J. (1996) Bacterial aminopeptidases: properties and functions. FEMS Microbiol Rev 18 : 319 344.
    • (1996) FEMS Microbiol Rev , vol.18 , pp. 319-344
    • Gonzales, T.1    Robert-Baudouy, J.2
  • 19
    • 2642641281 scopus 로고    scopus 로고
    • Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough
    • González, J.M., Masuchi, Y., Robb, F.T., Ammerman, J.W., Maeder, D.L., Yanagibayashi, M., et al. (1998) Pyrococcus horikoshii sp. nov., a hyperthermophilic archaeon isolated from a hydrothermal vent at the Okinawa Trough. Extremophiles 2 : 123 130.
    • (1998) Extremophiles , vol.2 , pp. 123-130
    • González, J.M.1    Masuchi, Y.2    Robb, F.T.3    Ammerman, J.W.4    Maeder, D.L.5    Yanagibayashi, M.6
  • 21
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S. (2003) Proteolysis in bacterial regulatory circuits. Annu Rev Cell Dev Biol 19 : 565 587.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 22
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux très faibles angles: Applications à l'étude des phénomènes ultra-microscopiques
    • Guinier, A. (1939) La diffraction des rayons X aux très faibles angles: applications à l'étude des phénomènes ultra-microscopiques. Ann Phys (Paris) 12 : 161 236.
    • (1939) Ann Phys (Paris) , vol.12 , pp. 161-236
    • Guinier, A.1
  • 23
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988) Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J Appl Crystallogr 21 : 916 924.
    • (1988) J Appl Crystallogr , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 : 2577 2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0036710534 scopus 로고    scopus 로고
    • Nutrient dynamics in the deep blue sea
    • Karl, D.M. (2002) Nutrient dynamics in the deep blue sea. Trends Microbiol 10 : 410 418.
    • (2002) Trends Microbiol , vol.10 , pp. 410-418
    • Karl, D.M.1
  • 26
    • 0033408348 scopus 로고    scopus 로고
    • Intracellular proteolysis
    • Kirschner, M. (1999) Intracellular proteolysis. Trends Cell Biol 9 : M42 M45.
    • (1999) Trends Cell Biol , vol.9
    • Kirschner, M.1
  • 27
    • 0031892541 scopus 로고    scopus 로고
    • Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes
    • Kisselev, A.F., Akopian, T.N. Goldberg, A.L. (1998) Range of sizes of peptide products generated during degradation of different proteins by archaeal proteasomes. J Biol Chem 273 : 1982 1989.
    • (1998) J Biol Chem , vol.273 , pp. 1982-1989
    • Kisselev, A.F.1    Akopian, T.N.2    Goldberg, A.L.3
  • 28
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev, A.F., Akopian, T.N., Woo, K.M. Goldberg, A.L. (1999) The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes. Implications for understanding the degradative mechanism and antigen presentation. J Biol Chem 274 : 3363 3371.
    • (1999) J Biol Chem , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 29
    • 0032562136 scopus 로고    scopus 로고
    • Essential binding and functional domains of human bleomycin hydrolase
    • Koldamova, R.P., Lefterov, I.M., Gadjeva, V.G. Lazo, J.S. (1998) Essential binding and functional domains of human bleomycin hydrolase. Biochemistry 37 : 2282 2290.
    • (1998) Biochemistry , vol.37 , pp. 2282-2290
    • Koldamova, R.P.1    Lefterov, I.M.2    Gadjeva, V.G.3    Lazo, J.S.4
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26 : 283 291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 32
    • 0033857926 scopus 로고    scopus 로고
    • Susceptibility to heavy metals and cadmium accumulation in aerobic and anaerobic thermophilic microorganisms isolated from deep-sea hydrothermal vents
    • Llanos, J., Capasso, C., Parisi, E., Prieur, D. Jeanthon, C. (2000) Susceptibility to heavy metals and cadmium accumulation in aerobic and anaerobic thermophilic microorganisms isolated from deep-sea hydrothermal vents. Curr Microbiol 41 : 201 205.
    • (2000) Curr Microbiol , vol.41 , pp. 201-205
    • Llanos, J.1    Capasso, C.2    Parisi, E.3    Prieur, D.4    Jeanthon, C.5
  • 35
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R.J. (2001) Pushing the boundaries of molecular replacement with maximum likelihood. Acta Crystallogr D Biol Crystallogr 57 : 1373 1382.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1373-1382
    • Read, R.J.1
  • 37
    • 10944251348 scopus 로고    scopus 로고
    • Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase
    • Russo, S. Baumann, U. (2004) Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase. J Biol Chem 279 : 51275 51281.
    • (2004) J Biol Chem , vol.279 , pp. 51275-51281
    • Russo, S.1    Baumann, U.2
  • 38
    • 8744237281 scopus 로고    scopus 로고
    • Pathway for degradation of peptides generated by proteasomes: A key role for thimet oligopeptidase and other metallopeptidases
    • Saric, T., Graef, C.I. Goldberg, A.L. (2004) Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases. J Biol Chem 279 : 46723 46732.
    • (2004) J Biol Chem , vol.279 , pp. 46723-46732
    • Saric, T.1    Graef, C.I.2    Goldberg, A.L.3
  • 39
    • 5344269437 scopus 로고    scopus 로고
    • Sculpting the proteome with AAA (+) proteases and disassembly machines
    • Sauer, R.T., Bolon, D.N., Burton, B.M., Burton, R.E., Flynn, J.M., Grant, R.A., et al. (2004) Sculpting the proteome with AAA (+) proteases and disassembly machines. Cell 119 : 9 18.
    • (2004) Cell , vol.119 , pp. 9-18
    • Sauer, R.T.1    Bolon, D.N.2    Burton, B.M.3    Burton, R.E.4    Flynn, J.M.5    Grant, R.A.6
  • 40
    • 33846021304 scopus 로고    scopus 로고
    • An archaeal peptidase assembles into two different quaternary structures: A tetrahedron and a giant octahedron
    • Schoehn, G., Vellieux, F.M.D., Durá, M.A., Receveur- Bréchot, V., Fabry, C.M.S., Ruigrok, R.W.H., et al. (2006) An archaeal peptidase assembles into two different quaternary structures: a tetrahedron and a giant octahedron. J Biol Chem 281 : 36327 36337.
    • (2006) J Biol Chem , vol.281 , pp. 36327-36337
    • Schoehn, G.1    Vellieux, F.M.D.2    Durá, M.A.3    Receveur-Bréchot, V.4    Fabry, C.M.S.5    Ruigrok, R.W.H.6
  • 41
    • 0019332136 scopus 로고
    • α-N-Benzoylarginine-β-naphthylamide hydrolase, an aminoendopeptidase from rabbit lung
    • Singh, H. Kalnitsky, G. (1980) α-N-Benzoylarginine-β- naphthylamide hydrolase, an aminoendopeptidase from rabbit lung. J Biol Chem 255 : 369 374.
    • (1980) J Biol Chem , vol.255 , pp. 369-374
    • Singh, H.1    Kalnitsky, G.2
  • 42
    • 0026553652 scopus 로고
    • Regulation of proteolytic activity in the hyperthermophile Pyrococcus furiosus
    • Snowden, L.J., Blumentals, I.I. Kelly, R.M. (1992) Regulation of proteolytic activity in the hyperthermophile Pyrococcus furiosus. Appl Environ Microbiol 58 : 1134 1141.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 1134-1141
    • Snowden, L.J.1    Blumentals, I.I.2    Kelly, R.M.3
  • 43
    • 0035912827 scopus 로고    scopus 로고
    • Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis
    • Stamper, C., Bennett, B., Edwards, T., Holz, R.C., Ringe, D. Petsko, G. (2001) Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis. Biochemistry 40 : 7035 7046.
    • (2001) Biochemistry , vol.40 , pp. 7035-7046
    • Stamper, C.1    Bennett, B.2    Edwards, T.3    Holz, R.C.4    Ringe, D.5    Petsko, G.6
  • 44
    • 14644414793 scopus 로고    scopus 로고
    • Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Story, S.V., Shah, C., Jenney, F.E. Adams, M.W.W. (2005) Characterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bact 187 : 2077 2083.
    • (2005) J Bact , vol.187 , pp. 2077-2083
    • Story, S.V.1    Shah, C.2    Jenney, F.E.3    Adams, M.W.W.4
  • 45
    • 0032478214 scopus 로고    scopus 로고
    • Protein hydration in solution: Experimental observation by X-ray and neutron scattering
    • Svergun, D., Richard, S., Koch, M.H.J., Sayers, Z., Kuprin, S. Zaccai, G. (1998) Protein hydration in solution: experimental observation by X-ray and neutron scattering. Proc Natl Acad Sci USA 95 : 2267 2272.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2267-2272
    • Svergun, D.1    Richard, S.2    Koch, M.H.J.3    Sayers, Z.4    Kuprin, S.5    Zaccai, G.6
  • 46
    • 0032567040 scopus 로고    scopus 로고
    • The role of Tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation
    • Tamura, N., Lottspeich, F., Baumeister, W. Tamura, T. (1998) The role of Tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation. Cell 95 : 637 648.
    • (1998) Cell , vol.95 , pp. 637-648
    • Tamura, N.1    Lottspeich, F.2    Baumeister, W.3    Tamura, T.4
  • 48
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • Taylor, A. (1993) Aminopeptidases: structure and function. FASEB J 7 : 290 298.
    • (1993) FASEB J , vol.7 , pp. 290-298
    • Taylor, A.1
  • 49
    • 0033198680 scopus 로고    scopus 로고
    • Tripeptidyl peptidases: Enzymes that count
    • Tomkinson, B. (1999) Tripeptidyl peptidases: enzymes that count. Trends Biochem Sci 24 : 355 359.
    • (1999) Trends Biochem Sci , vol.24 , pp. 355-359
    • Tomkinson, B.1
  • 50
    • 0030699086 scopus 로고    scopus 로고
    • Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: Molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme
    • Tsunasawa, S., Izu, Y., Miyagi, M. Kato, I. (1997) Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme. J Biochem 122 : 843 850.
    • (1997) J Biochem , vol.122 , pp. 843-850
    • Tsunasawa, S.1    Izu, Y.2    Miyagi, M.3    Kato, I.4
  • 51
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., Turk, B. Turk, D. (2001) Lysosomal cysteine proteases: facts and opportunities. EMBO J 20 : 4629 4633.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3


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