메뉴 건너뛰기




Volumn 388, Issue 2, 2007, Pages 227-235

The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity

Author keywords

Cysteine protease inhibitors; Cysteine proteases; Regulation of proteolysis; Staphostatins; Staphylococci

Indexed keywords

CYSTEINE PROTEINASE INHIBITOR; LIPOCALIN; STAPHOSTATIN A; STAPHOSTATIN B; UNCLASSIFIED DRUG;

EID: 33846567123     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2007.025     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0015924438 scopus 로고
    • Studies on extracellular proteolytic enzymes from Staphylococcus aureus. I. Purification and characterization of one neutral and one alkaline protease
    • Arvidson, S., Holme, T., and Lindholm, B. (1973). Studies on extracellular proteolytic enzymes from Staphylococcus aureus. I. Purification and characterization of one neutral and one alkaline protease. Biochim. Biophys. Acta 302, 135-148.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 135-148
    • Arvidson, S.1    Holme, T.2    Lindholm, B.3
  • 2
    • 0001169698 scopus 로고
    • Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants
    • H. Fritz, H. Tschesche, L.J. Greene and E. Truscheit, eds, Berlin, Germany: Springer-Verlag, pp
    • Bieth, J. (1974). Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. In: Bayer-Symposium V: Proteinase Inhibitors, H. Fritz, H. Tschesche, L.J. Greene and E. Truscheit, eds. (Berlin, Germany: Springer-Verlag), pp. 463-469.
    • (1974) Bayer-Symposium V: Proteinase Inhibitors , pp. 463-469
    • Bieth, J.1
  • 3
    • 0019282838 scopus 로고
    • Pathophysiological interpretation of kinetic constants of protease inhibitors
    • Bieth, J.G. (1980). Pathophysiological interpretation of kinetic constants of protease inhibitors. Bull. Eur. Physiopathol. Respir. 16 (Suppl.), 183-195.
    • (1980) Bull. Eur. Physiopathol. Respir , vol.16 , Issue.SUPPL. , pp. 183-195
    • Bieth, J.G.1
  • 6
    • 0035202193 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of proteases form Staphylococcus epidermidis
    • Dubin, G., Chmiel, D., Mak, P., Rakwalska, M., Rzychon, M., and Dubin, A. (2001). Molecular cloning and biochemical characterization of proteases form Staphylococcus epidermidis. Biol. Chem. 382, 1575-1582.
    • (2001) Biol. Chem , vol.382 , pp. 1575-1582
    • Dubin, G.1    Chmiel, D.2    Mak, P.3    Rakwalska, M.4    Rzychon, M.5    Dubin, A.6
  • 7
    • 0345254948 scopus 로고    scopus 로고
    • A novel class of cysteine protease inhibitors: Solution structure of staphostatin A from Staphylococcus aureus
    • Dubin, G., Krajewski, M., Popowicz, G., Stec-Niemczyk, J., Bochtler, M., Potempa, J., Dubin, A., and Holak, T.A. (2003). A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus. Biochemistry 42, 13449-13456.
    • (2003) Biochemistry , vol.42 , pp. 13449-13456
    • Dubin, G.1    Krajewski, M.2    Popowicz, G.3    Stec-Niemczyk, J.4    Bochtler, M.5    Potempa, J.6    Dubin, A.7    Holak, T.A.8
  • 8
    • 3242795993 scopus 로고    scopus 로고
    • Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family
    • Dubin, G., Stec-Niemczyk, J., Dylag, T., Silberring, J., Dubin, A., and Potempa, J. (2004). Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family. Biol. Chem. 385, 543-546.
    • (2004) Biol. Chem , vol.385 , pp. 543-546
    • Dubin, G.1    Stec-Niemczyk, J.2    Dylag, T.3    Silberring, J.4    Dubin, A.5    Potempa, J.6
  • 9
    • 0001223455 scopus 로고
    • The absolute activity of choline-esterase
    • Easson, L.H. and Stedman, E. (1936). The absolute activity of choline-esterase. Proc. R. Soc. B, 121, 141-164.
    • (1936) Proc. R. Soc. B , vol.121 , pp. 141-164
    • Easson, L.H.1    Stedman, E.2
  • 10
    • 0142039915 scopus 로고    scopus 로고
    • The staphostatin-staphopain complex: A forward binding inhibitor in complex with its target cysteine protease
    • Filipek, R., Rzychon, M., Oleksy, A., Gruca, M., Dubin, A., Potempa, J., and Bochtler, M. (2003). The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease. J. Biol. Chem. 278, 40959-40966.
    • (2003) J. Biol. Chem , vol.278 , pp. 40959-40966
    • Filipek, R.1    Rzychon, M.2    Oleksy, A.3    Gruca, M.4    Dubin, A.5    Potempa, J.6    Bochtler, M.7
  • 11
    • 17644400742 scopus 로고    scopus 로고
    • A comparison of staphostatin B with standard mechanism serine protease inhibitors
    • Filipek, R., Potempa, J., and Bochtler, M. (2005). A comparison of staphostatin B with standard mechanism serine protease inhibitors. J. Biol. Chem. 280, 14669-14674.
    • (2005) J. Biol. Chem , vol.280 , pp. 14669-14674
    • Filipek, R.1    Potempa, J.2    Bochtler, M.3
  • 12
    • 10044261761 scopus 로고    scopus 로고
    • Genetic characterization of staphopain genes in Staphylococcus aureus
    • Golonka, E., Filipek, R., Sabat, A., Sinczak, A., and Potempa, J. (2004). Genetic characterization of staphopain genes in Staphylococcus aureus. Biol. Chem. 385, 1059-1067.
    • (2004) Biol. Chem , vol.385 , pp. 1059-1067
    • Golonka, E.1    Filipek, R.2    Sabat, A.3    Sinczak, A.4    Potempa, J.5
  • 13
    • 0141707105 scopus 로고    scopus 로고
    • Toxins-antitoxins: Plasmid maintenance, programmed cell death, and cell cycle arrest
    • Hayes, F. (2003). Toxins-antitoxins: plasmid maintenance, programmed cell death, and cell cycle arrest. Science 301, 1496-1499.
    • (2003) Science , vol.301 , pp. 1496-1499
    • Hayes, F.1
  • 15
    • 0015327378 scopus 로고
    • A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors
    • Henderson, P.F. (1972). A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors. Biochem. J. 127, 321-333.
    • (1972) Biochem. J , vol.127 , pp. 321-333
    • Henderson, P.F.1
  • 16
    • 22644433729 scopus 로고    scopus 로고
    • SpeB-Spi: A novel protease-inhibitor pair from Streptococcus pyogenes
    • Kagawa, T.F., O'Toole, P.W., and Cooney, J.C. (2005). SpeB-Spi: a novel protease-inhibitor pair from Streptococcus pyogenes. Mol. Microbiol. 57, 650-666.
    • (2005) Mol. Microbiol , vol.57 , pp. 650-666
    • Kagawa, T.F.1    O'Toole, P.W.2    Cooney, J.C.3
  • 17
    • 0036830351 scopus 로고    scopus 로고
    • Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus
    • Massimi, I., Park, E., Rice, K., Muller-Esterl,W., Sauder, D.N, and McGavin, M.J. (2002). Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of Staphylococcus aureus. J. Biol. Chem. 277, 41770-41777.
    • (2002) J. Biol. Chem , vol.277 , pp. 41770-41777
    • Massimi, I.1    Park, E.2    Rice, K.3    Muller-Esterl, W.4    Sauder, D.N.5    McGavin, M.J.6
  • 18
    • 0023833788 scopus 로고
    • Degradation of elastin by a cysteine proteinase form Staphylococcus aureus
    • Potempa, J., Dubin, A., Korzus, G., and Travis, J. (1988). Degradation of elastin by a cysteine proteinase form Staphylococcus aureus. J. Biol. Chem. 263, 2664-2667.
    • (1988) J. Biol. Chem , vol.263 , pp. 2664-2667
    • Potempa, J.1    Dubin, A.2    Korzus, G.3    Travis, J.4
  • 19
    • 22644435471 scopus 로고    scopus 로고
    • Fighting an enemy within: Cytoplasmic inhibitors of bacterial cysteine proteases
    • Potempa, J., Golonka, E., Filipek, R., and Shaw, L.N. (2005). Fighting an enemy within: cytoplasmic inhibitors of bacterial cysteine proteases. Mol. Microbiol. 57, 605-610.
    • (2005) Mol. Microbiol , vol.57 , pp. 605-610
    • Potempa, J.1    Golonka, E.2    Filipek, R.3    Shaw, L.N.4
  • 20
    • 0035167096 scopus 로고    scopus 로고
    • Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease
    • Rice, K., Perlata, R., Bast, D., Azavedo, J., and McGavin, M.J. (2001). Description of staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease. Infect. Immun. 69, 159-169.
    • (2001) Infect. Immun , vol.69 , pp. 159-169
    • Rice, K.1    Perlata, R.2    Bast, D.3    Azavedo, J.4    McGavin, M.J.5
  • 22
    • 0042565975 scopus 로고    scopus 로고
    • Staphostatins: An expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases
    • Rzychon, M., Sabat, A., Kosowska, K., Potempa, J., and Dubin, A. (2003b). Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases. Mol. Microbiol. 49, 1051-1066.
    • (2003) Mol. Microbiol , vol.49 , pp. 1051-1066
    • Rzychon, M.1    Sabat, A.2    Kosowska, K.3    Potempa, J.4    Dubin, A.5
  • 24
    • 0014211618 scopus 로고    scopus 로고
    • Schechter, I. and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • Schechter, I. and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
  • 25
    • 0345268668 scopus 로고    scopus 로고
    • Caenorhabditis elegans as a model host for Staphylococcus aureus pathogenesis
    • Sifri, C.D., Begun, J., Ausubel, F.M., and Calderwood, S.B. (2003). Caenorhabditis elegans as a model host for Staphylococcus aureus pathogenesis. Infect. Immun. 71, 2208-2217.
    • (2003) Infect. Immun , vol.71 , pp. 2208-2217
    • Sifri, C.D.1    Begun, J.2    Ausubel, F.M.3    Calderwood, S.B.4
  • 26
    • 1642473893 scopus 로고    scopus 로고
    • The role and regulation of the extracellular proteases of Staphylococcus aureus
    • Shaw, L., Golonka, E., Potempa, J., and Foster, S.J. (2004). The role and regulation of the extracellular proteases of Staphylococcus aureus. Microbiology 150, 217-228.
    • (2004) Microbiology , vol.150 , pp. 217-228
    • Shaw, L.1    Golonka, E.2    Potempa, J.3    Foster, S.J.4
  • 27
    • 14244266586 scopus 로고    scopus 로고
    • Cytoplasmic control of premature activation of a secreted protease zymogen: Deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype
    • Shaw, L.N., Golonka, E., Szmyd, G., Foster, S.J., Travis, J., and Potempa, J. (2005). Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (SspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype. J. Bacteriol. 187, 1751-1762.
    • (2005) J. Bacteriol , vol.187 , pp. 1751-1762
    • Shaw, L.N.1    Golonka, E.2    Szmyd, G.3    Foster, S.J.4    Travis, J.5    Potempa, J.6
  • 28
    • 0033049451 scopus 로고    scopus 로고
    • Purification and characterization of protease produced by Staphylococcus aureus isolated from a diseased chicken
    • Takeuchi, S., Kinoshita, T., Kaidoh, T., and Hashizume, N. (1999). Purification and characterization of protease produced by Staphylococcus aureus isolated from a diseased chicken. Vet. Microbiol. 67, 195-202.
    • (1999) Vet. Microbiol , vol.67 , pp. 195-202
    • Takeuchi, S.1    Kinoshita, T.2    Kaidoh, T.3    Hashizume, N.4
  • 29
    • 0037159105 scopus 로고    scopus 로고
    • Structural gene and strain specificity of a novel cysteine protease produced by Staphylococcus aureus isolated from a diseased chicken
    • Takeuchi, S., Matsunaga, K., Inubushi, S., Higuchi, H., Imaizumi, K., and Kaidoh, T. (2002). Structural gene and strain specificity of a novel cysteine protease produced by Staphylococcus aureus isolated from a diseased chicken. Vet. Microbiol. 89, 201-210.
    • (2002) Vet. Microbiol , vol.89 , pp. 201-210
    • Takeuchi, S.1    Matsunaga, K.2    Inubushi, S.3    Higuchi, H.4    Imaizumi, K.5    Kaidoh, T.6
  • 30
    • 0031921754 scopus 로고    scopus 로고
    • Characterization of the starvation-survival response of Staphylococcus aureus
    • Watson, S.P., Clements, M.O., and Foster, S.J. (1998). Characterization of the starvation-survival response of Staphylococcus aureus. J. Bacteriol. 180, 1750-1758.
    • (1998) J. Bacteriol , vol.180 , pp. 1750-1758
    • Watson, S.P.1    Clements, M.O.2    Foster, S.J.3
  • 31
    • 12744279612 scopus 로고    scopus 로고
    • Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli
    • Wladyka, B., Puzia, K., and Dubin, A. (2005). Efficient co-expression of a recombinant staphopain A and its inhibitor staphostatin A in Escherichia coli. Biochem. J. 385, 181-187.
    • (2005) Biochem. J , vol.385 , pp. 181-187
    • Wladyka, B.1    Puzia, K.2    Dubin, A.3
  • 32
    • 0035960883 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M
    • Yokoi, K., Kakikawa, M., Kimoto, H., Watanabe, K., Yasukawa, H., Yamakawa, A., Taketo, A., and Kodaira, K.I. (2001). Genetic and biochemical characterization of glutamyl endopeptidase of Staphylococcus warneri M. Gene 281, 115-122.
    • (2001) Gene , vol.281 , pp. 115-122
    • Yokoi, K.1    Kakikawa, M.2    Kimoto, H.3    Watanabe, K.4    Yasukawa, H.5    Yamakawa, A.6    Taketo, A.7    Kodaira, K.I.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.