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Volumn 290, Issue 1, 2015, Pages 658-670

Miropin, a novel bacterial serpin from the periodontopathogen Tannerella forsythia, inhibits a broad range of proteases by using different peptide bonds within the reactive center loop

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; STOICHIOMETRY;

EID: 84920520300     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.601716     Document Type: Article
Times cited : (47)

References (47)
  • 1
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 5
    • 4644325614 scopus 로고    scopus 로고
    • Serpins in unicellular Eukarya, Archaea, and Bacteria: Sequence analysis and evolution
    • Roberts, T. H., Hejgaard, J., Saunders, N. F., Cavicchioli, R., and Curmi, P. M. (2004) Serpins in unicellular Eukarya, Archaea, and Bacteria: sequence analysis and evolution. J. Mol. Evol. 59, 437-447
    • (2004) J. Mol. Evol. , vol.59 , pp. 437-447
    • Roberts, T.H.1    Hejgaard, J.2    Saunders, N.F.3    Cavicchioli, R.4    Curmi, P.M.5
  • 6
    • 1542496192 scopus 로고    scopus 로고
    • The 1.5 A˚ crystal structure of a prokaryote serpin: Controlling conformational change in a heated environment
    • Irving, J. A., Cabrita, L. D., Rossjohn, J., Pike, R. N., Bottomley, S. P., and Whisstock, J. C. (2003) The 1.5 A˚ crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. Structure 11, 387-397
    • (2003) Structure , vol.11 , pp. 387-397
    • Irving, J.A.1    Cabrita, L.D.2    Rossjohn, J.3    Pike, R.N.4    Bottomley, S.P.5    Whisstock, J.C.6
  • 7
    • 78149359090 scopus 로고    scopus 로고
    • Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function
    • Kantyka, T., Rawlings, N. D., and Potempa, J. (2010) Prokaryote-derived protein inhibitors of peptidases: A sketchy occurrence and mostly unknown function. Biochimie 92, 1644-1656
    • (2010) Biochimie , vol.92 , pp. 1644-1656
    • Kantyka, T.1    Rawlings, N.D.2    Potempa, J.3
  • 8
    • 33744476159 scopus 로고    scopus 로고
    • The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors
    • Kang, S., Barak, Y., Lamed, R., Bayer, E. A., and Morrison, M. (2006) The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors. Mol. Microbiol. 60, 1344-1354
    • (2006) Mol. Microbiol. , vol.60 , pp. 1344-1354
    • Kang, S.1    Barak, Y.2    Lamed, R.3    Bayer, E.A.4    Morrison, M.5
  • 11
    • 34848911346 scopus 로고    scopus 로고
    • Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap
    • Cabrita, L. D., Irving, J. A., Pearce, M. C., Whisstock, J. C., and Bottomley, S. P. (2007) Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap. J. Biol. Chem. 282, 26802-26809
    • (2007) J. Biol. Chem. , vol.282 , pp. 26802-26809
    • Cabrita, L.D.1    Irving, J.A.2    Pearce, M.C.3    Whisstock, J.C.4    Bottomley, S.P.5
  • 12
    • 78650097591 scopus 로고    scopus 로고
    • Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakaraensis
    • Tanaka, S., Koga, Y., Takano, K., and Kanaya, S. (2011) Inhibition of chymotrypsin- and subtilisin-like serine proteases with Tk-serpin from hyperthermophilic archaeon Thermococcus kodakaraensis. Biochim. Biophys. Acta 1814, 299-307
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 299-307
    • Tanaka, S.1    Koga, Y.2    Takano, K.3    Kanaya, S.4
  • 14
    • 77953616099 scopus 로고    scopus 로고
    • Periodontitis: A polymicrobial disruption of host homeostasis
    • Darveau, R. P. (2010) Periodontitis: a polymicrobial disruption of host homeostasis. Nat. Rev. Microbiol. 8, 481-490
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 481-490
    • Darveau, R.P.1
  • 15
    • 0026824717 scopus 로고
    • New considerations in the prevalence of periodontal disease
    • Fox, C. H. (1992) New considerations in the prevalence of periodontal disease. Curr. Opin. Dent. 2, 5-11
    • (1992) Curr. Opin. Dent. , vol.2 , pp. 5-11
    • Fox, C.H.1
  • 17
    • 0035750050 scopus 로고    scopus 로고
    • Epidemiologic associations between periodontal disease and chronic obstructive pulmonary disease
    • Garcia, R. I., Nunn, M. E., and Vokonas, P. S. (2001) Epidemiologic associations between periodontal disease and chronic obstructive pulmonary disease. Ann. Periodontol. 6, 71-77
    • (2001) Ann. Periodontol. , vol.6 , pp. 71-77
    • Garcia, R.I.1    Nunn, M.E.2    Vokonas, P.S.3
  • 20
    • 33748337086 scopus 로고    scopus 로고
    • Periodontal infections and atherosclerotic vascular disease: An update
    • Behle, J. H., and Papapanou, P. N. (2006) Periodontal infections and atherosclerotic vascular disease: an update. Int. Dent. J. 56, 256-262
    • (2006) Int. Dent. J. , vol.56 , pp. 256-262
    • Behle, J.H.1    Papapanou, P.N.2
  • 22
    • 77955733490 scopus 로고    scopus 로고
    • Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and a-enolase: Implications for autoimmunity in rheumatoid arthritis
    • Wegner, N., Wait, R., Sroka, A., Eick, S., Nguyen, K. A., Lundberg, K., Kinloch, A., Culshaw, S., Potempa, J., and Venables, P. J. (2010) Peptidylarginine deiminase from Porphyromonas gingivalis citrullinates human fibrinogen and a-enolase: implications for autoimmunity in rheumatoid arthritis. Arthritis Rheum. 62, 2662-2672
    • (2010) Arthritis Rheum. , vol.62 , pp. 2662-2672
    • Wegner, N.1    Wait, R.2    Sroka, A.3    Eick, S.4    Nguyen, K.A.5    Lundberg, K.6    Kinloch, A.7    Culshaw, S.8    Potempa, J.9    Venables, P.J.10
  • 24
    • 0036816820 scopus 로고    scopus 로고
    • Neutrophil elastase-mediated killing of bacteria: Lessons from targeted mutagenesis
    • Belaaouaj, A. (2002) Neutrophil elastase-mediated killing of bacteria: lessons from targeted mutagenesis. Microbes Infect. 4, 1259-1264
    • (2002) Microbes Infect. , vol.4 , pp. 1259-1264
    • Belaaouaj, A.1
  • 25
    • 33644864110 scopus 로고
    • p-Nitrophenyl-p′-guanidinobenzoate HCl: A new active site titrant for trypsin
    • Chase, T., Jr., and Shaw, E. (1967) p-Nitrophenyl-p′-guanidinobenzoate HCl: a new active site titrant for trypsin. Biochem. Biophys. Res. Commun. 29, 508-514
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 508-514
    • Chase, T.1    Shaw, E.2
  • 26
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 27
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F., and Walsh, C. T. (1988) The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61, 201-301
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 29
    • 0033485345 scopus 로고    scopus 로고
    • Solvent/ detergent-treated plasma has decreased antitrypsin activity and absent antiplasmin activity
    • Mast, A. E., Stadanlick, J. E., Lockett, J. M., and Dietzen, D. J. (1999) Solvent/ detergent-treated plasma has decreased antitrypsin activity and absent antiplasmin activity. Blood 94, 3922-3927
    • (1999) Blood , vol.94 , pp. 3922-3927
    • Mast, A.E.1    Stadanlick, J.E.2    Lockett, J.M.3    Dietzen, D.J.4
  • 30
    • 0020510606 scopus 로고
    • Mutation of antitrypsin to antithrombin. α1-Antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder
    • Owen, M. C., Brennan, S. O., Lewis, J. H., and Carrell, R. W. (1983) Mutation of antitrypsin to antithrombin. α1-Antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder. N. Engl. J. Med. 309, 694-698
    • (1983) N. Engl. J. Med. , vol.309 , pp. 694-698
    • Owen, M.C.1    Brennan, S.O.2    Lewis, J.H.3    Carrell, R.W.4
  • 31
    • 77949500554 scopus 로고    scopus 로고
    • Control of granzymes by serpins
    • Kaiserman, D., and Bird, P. I. (2010) Control of granzymes by serpins. Cell Death Differ. 17, 586-595
    • (2010) Cell Death Differ. , vol.17 , pp. 586-595
    • Kaiserman, D.1    Bird, P.I.2
  • 32
    • 0029665326 scopus 로고    scopus 로고
    • Role of the P2 residue in determining the specificity of serpins
    • Djie, M. Z., Le Bonniec, B. F., Hopkins, P. C., Hipler, K., and Stone, S. R. (1996) Role of the P2 residue in determining the specificity of serpins. Biochemistry 35, 11461-11469
    • (1996) Biochemistry , vol.35 , pp. 11461-11469
    • Djie, M.Z.1    Le Bonniec, B.F.2    Hopkins, P.C.3    Hipler, K.4    Stone, S.R.5
  • 33
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J., and Carrell, R. W. (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 34
    • 33751087751 scopus 로고    scopus 로고
    • Polymerization of human angiotensinogen: Insights into its structural mechanism and functional significance
    • Stanley, P., Serpell, L. C., and Stein, P. E. (2006) Polymerization of human angiotensinogen: insights into its structural mechanism and functional significance. Biochem. J. 400, 169-178
    • (2006) Biochem. J. , vol.400 , pp. 169-178
    • Stanley, P.1    Serpell, L.C.2    Stein, P.E.3
  • 35
    • 0034039248 scopus 로고    scopus 로고
    • Analysis of free prostate-specific antigen (PSA) after chemical release from the complex with α1- antichymotrypsin (PSA-ACT)
    • Peter, J., Unverzagt, C., and Hoesel, W. (2000) Analysis of free prostate-specific antigen (PSA) after chemical release from the complex with α1- antichymotrypsin (PSA-ACT). Clin. Chem. 46, 474-482
    • (2000) Clin. Chem. , vol.46 , pp. 474-482
    • Peter, J.1    Unverzagt, C.2    Hoesel, W.3
  • 36
    • 0035235490 scopus 로고    scopus 로고
    • The serpins: Nature's molecular mousetraps
    • Huntington, J. A., and Carrell, R. W. (2001) The serpins: nature's molecular mousetraps. Sci. Prog. 84, 125-136
    • (2001) Sci. Prog. , vol.84 , pp. 125-136
    • Huntington, J.A.1    Carrell, R.W.2
  • 37
    • 0022395406 scopus 로고
    • Plakalbumin, α1-antitrypsin, antithrombin, and the mechanism of inflammatory thrombosis
    • Carrell, R. W., and Owen, M. C. (1985) Plakalbumin, α1-antitrypsin, antithrombin, and the mechanism of inflammatory thrombosis. Nature 317, 730-732
    • (1985) Nature , vol.317 , pp. 730-732
    • Carrell, R.W.1    Owen, M.C.2
  • 38
    • 0025833842 scopus 로고
    • Proteolytic inactivation of α-1-anti-chymotrypsin. Sites of cleavage and generation of chemotactic activity
    • Potempa, J., Fedak, D., Dubin, A., Mast, A., and Travis, J. (1991) Proteolytic inactivation of α-1-anti-chymotrypsin. Sites of cleavage and generation of chemotactic activity. J. Biol. Chem. 266, 21482-21487
    • (1991) J. Biol. Chem. , vol.266 , pp. 21482-21487
    • Potempa, J.1    Fedak, D.2    Dubin, A.3    Mast, A.4    Travis, J.5
  • 40
    • 0031917385 scopus 로고    scopus 로고
    • Inhibition of soluble recombinant furin by human proteinase inhibitor 8
    • Dahlen, J. R., Jean, F., Thomas, G., Foster, D. C., and Kisiel, W. (1998) Inhibition of soluble recombinant furin by human proteinase inhibitor 8. J. Biol. Chem. 273, 1851-1854
    • (1998) J. Biol. Chem. , vol.273 , pp. 1851-1854
    • Dahlen, J.R.1    Jean, F.2    Thomas, G.3    Foster, D.C.4    Kisiel, W.5
  • 41
    • 0023815149 scopus 로고
    • α-2-antiplasmin: A serpin with two separate but overlapping reactive sites
    • Potempa, J., Shieh, B. H., and Travis, J. (1988) α-2-antiplasmin: a serpin with two separate but overlapping reactive sites. Science 241, 699-700
    • (1988) Science , vol.241 , pp. 699-700
    • Potempa, J.1    Shieh, B.H.2    Travis, J.3
  • 42
    • 0029815085 scopus 로고    scopus 로고
    • Heterologous expression of three plant serpins with distinct inhibitory specificities
    • Dahl, S. W., Rasmussen, S. K., and Hejgaard, J. (1996) Heterologous expression of three plant serpins with distinct inhibitory specificities. J. Biol. Chem. 271, 25083-25088
    • (1996) J. Biol. Chem. , vol.271 , pp. 25083-25088
    • Dahl, S.W.1    Rasmussen, S.K.2    Hejgaard, J.3
  • 43
    • 17544383818 scopus 로고    scopus 로고
    • Human cytoplasmic antiproteinase neutralizes rapidly and efficiently chymotrypsin and trypsin-like proteases utilizing distinct reactive site residues
    • Riewald, M., and Schleef, R. R. (1996) Human cytoplasmic antiproteinase neutralizes rapidly and efficiently chymotrypsin and trypsin-like proteases utilizing distinct reactive site residues. J. Biol. Chem. 271, 14526-14532
    • (1996) J. Biol. Chem. , vol.271 , pp. 14526-14532
    • Riewald, M.1    Schleef, R.R.2
  • 44
    • 0034721763 scopus 로고    scopus 로고
    • Inhibitory serpins from wheat grain with reactive centers resembling glutamine- rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms
    • Ostergaard, H., Rasmussen, S. K., Roberts, T. H., and Hejgaard, J. (2000) Inhibitory serpins from wheat grain with reactive centers resembling glutamine- rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms. J. Biol. Chem. 275, 33272-33279
    • (2000) J. Biol. Chem. , vol.275 , pp. 33272-33279
    • Ostergaard, H.1    Rasmussen, S.K.2    Roberts, T.H.3    Hejgaard, J.4
  • 45
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • Irving, J. A., Pike, R. N., Lesk, A. M., and Whisstock, J. C. (2000) Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res. 10, 1845-1864
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 46
    • 78650231500 scopus 로고    scopus 로고
    • The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases
    • Cerdà-Costa, N., Guevara, T., Karim, A. Y., Ksiazek, M., Nguyen, K. A., Arolas, J. L., Potempa, J., and Gomis-Rüth, F. X. (2011) The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases. Mol. Microbiol. 79, 119-132
    • (2011) Mol. Microbiol. , vol.79 , pp. 119-132
    • Cerdà-Costa, N.1    Guevara, T.2    Karim, A.Y.3    Ksiazek, M.4    Nguyen, K.A.5    Arolas, J.L.6    Potempa, J.7    Gomis-Rüth, F.X.8
  • 47
    • 1842866213 scopus 로고    scopus 로고
    • The periplasmic serine protease inhibitor ecotin protects bacteria against neutrophil elastase
    • Eggers, C. T., Murray, I. A., Delmar, V. A., Day, A. G., and Craik, C. S. (2004) The periplasmic serine protease inhibitor ecotin protects bacteria against neutrophil elastase. Biochem. J. 379, 107-118
    • (2004) Biochem. J. , vol.379 , pp. 107-118
    • Eggers, C.T.1    Murray, I.A.2    Delmar, V.A.3    Day, A.G.4    Craik, C.S.5


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