메뉴 건너뛰기




Volumn 21, Issue 6, 2011, Pages 617-626

A novel transglutaminase substrate from Streptomyces mobaraensis inhibiting papain-like cysteine proteases

Author keywords

Cysteine protease inhibitor; Oligoglutamate; Papain inhibitor; Streptomyces; Transglutaminase; Transglutaminase substrate

Indexed keywords

PAPAIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 79959996681     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1012.12004     Document Type: Article
Times cited : (18)

References (41)
  • 2
    • 33747335690 scopus 로고    scopus 로고
    • Characterization of cysteine proteases in Malian medicinal plants
    • Bah, S., B. S. Paulsen, D. Diallo, and H. T. Johansen. 2006. Characterization of cysteine proteases in Malian medicinal plants. J. Ethnopharmacol. 107: 189-198.
    • (2006) J. Ethnopharmacol. , vol.107 , pp. 189-198
    • Bah, S.1    Paulsen, B.S.2    Diallo, D.3    Johansen, H.T.4
  • 4
    • 51449114441 scopus 로고    scopus 로고
    • Malarial proteases and host cell egress: An 'emerging' cascade
    • Blackman, M. J. 2008. Malarial proteases and host cell egress: An 'emerging' cascade. Cell. Microbiol. 10: 1925-1934.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1925-1934
    • Blackman, M.J.1
  • 5
    • 0345862190 scopus 로고    scopus 로고
    • Production and activation of recombinant papain-like cysteine proteases
    • Brömme, D., F. S. Nallaseth, and B. Turk. 2004. Production and activation of recombinant papain-like cysteine proteases. Methods 32: 199-206.
    • (2004) Methods , vol.32 , pp. 199-206
    • Brömme, D.1    Nallaseth, F.S.2    Turk, B.3
  • 6
    • 33745289074 scopus 로고    scopus 로고
    • Poly-gamma-glutamate in bacteria
    • Candela, T. and A. Fouet. 2006. Poly-gamma-glutamate in bacteria. Mol. Microbiol. 60: 1091-1098.
    • (2006) Mol. Microbiol. , vol.60 , pp. 1091-1098
    • Candela, T.1    Fouet, A.2
  • 9
    • 70350167108 scopus 로고    scopus 로고
    • Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose
    • De Jong, W., H. A. B. Wösten, L. Dijkhuizen, and D. Claessen. 2009. Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose. Mol. Microbiol. 73: 1128-1140.
    • (2009) Mol. Microbiol. , vol.73 , pp. 1128-1140
    • de Jong, W.1    Wösten, H.A.B.2    Dijkhuizen, L.3    Claessen, D.4
  • 10
    • 36148979683 scopus 로고    scopus 로고
    • Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus
    • Devaraj, S. G., N. Wang, Z. Chen, Z. Chen, M. Tseng, N. Barretto, et al. 2007. Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus. J. Biol. Chem. 282: 32208-32221.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32208-32221
    • Devaraj, S.G.1    Wang, N.2    Chen, Z.3    Chen, Z.4    Tseng, M.5    Barretto, N.6
  • 11
    • 50249136588 scopus 로고    scopus 로고
    • Function and redundancy of the chaplin cell surface proteins in aerial hypha formation, rodlet assembly, and viability in Streptomyces coelicolor
    • Di Berardo, C., D. S. Capstick, M. J. Bibb, K. C. Findlay, M. J. Buttner, and M. A. Elliot. 2008. Function and redundancy of the chaplin cell surface proteins in aerial hypha formation, rodlet assembly, and viability in Streptomyces coelicolor. J. Bacteriol. 190: 5879-5889.
    • (2008) J. Bacteriol. , vol.190 , pp. 5879-5889
    • di Berardo, C.1    Capstick, D.S.2    Bibb, M.J.3    Findlay, K.C.4    Buttner, M.J.5    Elliot, M.A.6
  • 12
    • 0038681008 scopus 로고    scopus 로고
    • The chaplins: A family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor
    • Elliot, M. A., N. Karoonuthaisiri, J. Huang, M. J. Bibb, S. N. Cohen, C. M. Cao, and M. J. Buttner. 2003. The chaplins: A family of hydrophobic cell-surface proteins involved in aerial mycelium formation in Streptomyces coelicolor. Genes Dev. 17: 1727-1740.
    • (2003) Genes Dev. , vol.17 , pp. 1727-1740
    • Elliot, M.A.1    Karoonuthaisiri, N.2    Huang, J.3    Bibb, M.J.4    Cohen, S.N.5    Cao, C.M.6    Buttner, M.J.7
  • 13
    • 0016837688 scopus 로고
    • Inhibition of thymidylate synthetase and dihydrofolate reductase by naturally occurring oligoglutamate derivatives of folic acid
    • Friedkin, M., L. T. Plante, E. J. Crawford, and M. Crumm. 1975. Inhibition of thymidylate synthetase and dihydrofolate reductase by naturally occurring oligoglutamate derivatives of folic acid. J. Biol. Chem. 250: 5614-5621.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5614-5621
    • Friedkin, M.1    Plante, L.T.2    Crawford, E.J.3    Crumm, M.4
  • 14
    • 0028300118 scopus 로고
    • A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense
    • Gerber, U., U. Jucknischke, S. Putzien, and H.-L. Fuchsbauer. 1994. A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense. Biochem. J. 299: 825-829.
    • (1994) Biochem. J. , vol.299 , pp. 825-829
    • Gerber, U.1    Jucknischke, U.2    Putzien, S.3    Fuchsbauer, H.-L.4
  • 15
    • 0034682835 scopus 로고    scopus 로고
    • A novel doubleheaded proteinaceous inhibitor for metalloproteinase and serine proteinase
    • Hiraga, K., T. Suzuki, and K. Oda. 2000. A novel doubleheaded proteinaceous inhibitor for metalloproteinase and serine proteinase. J. Biol. Chem. 275: 25173-25179.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25173-25179
    • Hiraga, K.1    Suzuki, T.2    Oda, K.3
  • 17
    • 0027223075 scopus 로고
    • Primary structure of microbial transglutaminase from Streptoverticillium sp. strain S-8112
    • Kanaji, T., H. Ozaki, T. Takao, H. Kawajiri, H. Ide, M. Motoki, and Y. Shimonishi. 1993. Primary structure of microbial transglutaminase from Streptoverticillium sp. strain S-8112. J. Biol. Chem. 268: 11565-11572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11565-11572
    • Kanaji, T.1    Ozaki, H.2    Takao, T.3    Kawajiri, H.4    Ide, H.5    Motoki, M.6    Shimonishi, Y.7
  • 18
  • 19
    • 0028016089 scopus 로고
    • Primary structure and inhibitory properties of a proteinase inhibitor produced by Streptomyces cacaoi
    • Koshima, S., M. Terabe, S. Taguchi, H. Momose, and K. Miura. 1994. Primary structure and inhibitory properties of a proteinase inhibitor produced by Streptomyces cacaoi. Biochim. Biophys. Acta 1207: 120-125.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 120-125
    • Koshima, S.1    Terabe, M.2    Taguchi, S.3    Momose, H.4    Miura, K.5
  • 21
    • 0033117369 scopus 로고    scopus 로고
    • Molecular characterization and analysis of the biosynthetic gene cluster for the antitumor antibiotic mitomycin C from Streptomyces lavendulae NRRL 2564
    • Mao, Y. Q., M. Varoglu, and D. H. Sherman. 1999. Molecular characterization and analysis of the biosynthetic gene cluster for the antitumor antibiotic mitomycin C from Streptomyces lavendulae NRRL 2564. Chem. Biol. 6: 251-263.
    • (1999) Chem. Biol. , vol.6 , pp. 251-263
    • Mao, Y.Q.1    Varoglu, M.2    Sherman, D.H.3
  • 22
    • 71549166319 scopus 로고    scopus 로고
    • Cell division is dispensable but not irrelevant in Streptomyces
    • McCormick, J. R. 2009. Cell division is dispensable but not irrelevant in Streptomyces. Curr. Opin. Microbiol. 12: 689-698.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 689-698
    • McCormick, J.R.1
  • 23
    • 56349085281 scopus 로고    scopus 로고
    • Transglutaminases. Family of enzymes with diverse functions
    • (eds.), In J. R. Bertino (ed.)., Karger, Basel, Switzerland
    • Mehta, K. and R. Eckert (eds.). 2005. Transglutaminases. Family of enzymes with diverse functions. In J. R. Bertino (ed.). Progress in Experimental Tumor Research. Karger, Basel, Switzerland.
    • (2005) Progress in Experimental Tumor Research
    • Mehta, K.1    Eckert, R.2
  • 24
    • 69949130234 scopus 로고    scopus 로고
    • Streptomyces roseoverticillatus produces two different poly(amino acid)s: Lariatshaped γ-poly(L-glutamic acid) and ε-poly(L-lysine)
    • Nishikawa, M. and K. Kobayashi. 2009. Streptomyces roseoverticillatus produces two different poly(amino acid)s: Lariatshaped γ-poly(L-glutamic acid) and ε-poly(L-lysine). Microbiology 155: 2988-2993.
    • (2009) Microbiology , vol.155 , pp. 2988-2993
    • Nishikawa, M.1    Kobayashi, K.2
  • 26
    • 69949122122 scopus 로고    scopus 로고
    • SwrAA activates poly-γ-glutamate synthesis in addition to swarming in Bacillus subtilis
    • Osera, C., G. Amati, C. Calvio, and A. Galizzi. 2009. SwrAA activates poly-γ-glutamate synthesis in addition to swarming in Bacillus subtilis. Microbiology 155: 2282-2287.
    • (2009) Microbiology , vol.155 , pp. 2282-2287
    • Osera, C.1    Amati, G.2    Calvio, C.3    Galizzi, A.4
  • 27
    • 0032212390 scopus 로고    scopus 로고
    • Bacterial pro-transglutaminase from Streptoverticillium mobaraense. Purification, characterisation and sequence of the zymogen
    • Pasternack, R., S. Dorsch, J. T. Otterbach, I. R. Robenek, S. Wolf, and H.-L. Fuchsbauer. 1998. Bacterial pro-transglutaminase from Streptoverticillium mobaraense. Purification, characterisation and sequence of the zymogen. Eur. J. Biochem. 257: 570-576.
    • (1998) Eur. J. Biochem. , vol.257 , pp. 570-576
    • Pasternack, R.1    Dorsch, S.2    Otterbach, J.T.3    Robenek, I.R.4    Wolf, S.5    Fuchsbauer, H.-L.6
  • 28
  • 29
    • 16844365217 scopus 로고    scopus 로고
    • Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells
    • Santos, C. C., C. Sant'anna, A. Terres, N. L. Chuna-e-Silva, J. Scharfstein, and A. P. de A. Lima. 2005. Chagasin, the endogenous cysteine-protease inhibitor of Trypanosoma cruzi, modulates parasite differentiation and invasion of mammalian cells. J. Cell Sci. 118: 901-915.
    • (2005) J. Cell Sci. , vol.118 , pp. 901-915
    • Santos, C.C.1    Sant'Anna, C.2    Terres, A.3    Chuna-E-Silva, N.L.4    Scharfstein, J.5    de Lima, A.P.A.6
  • 31
    • 49649129361 scopus 로고    scopus 로고
    • The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine substrate of the intrinsic transglutaminase
    • Schmidt, S., F. Adolf, and H.-L. Fuchsbauer. 2008. The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine substrate of the intrinsic transglutaminase. FEBS Lett. 582: 3132-3138.
    • (2008) FEBS Lett. , vol.582 , pp. 3132-3138
    • Schmidt, S.1    Adolf, F.2    Fuchsbauer, H.-L.3
  • 32
    • 0001916980 scopus 로고
    • Biosynthesis of glutamine and glutamate and the assimilation of ammonia
    • In A. L. Sonenshein, J. A. Hoch, and R. Losick (eds.), American Society of Microbiology, Washington, DC
    • Schreier, H. J. 1993. Biosynthesis of glutamine and glutamate and the assimilation of ammonia, pp. 281-298. In A. L. Sonenshein, J. A. Hoch, and R. Losick (eds.). Bacillus subtilis and Other Gram-Positive Bacteria. American Society of Microbiology, Washington, DC.
    • (1993) Bacillus subtilis and Other Gram-Positive Bacteria. , pp. 281-298
    • Schreier, H.J.1
  • 34
    • 23744435412 scopus 로고    scopus 로고
    • Defining the genetic differences between wild and domestic strains of Bacillus subtilis that affect poly-γ-DL-glutamic acid production and biofilm formation
    • Stanley, N. R. and B. A. Lazazzera. 2005. Defining the genetic differences between wild and domestic strains of Bacillus subtilis that affect poly-γ-DL-glutamic acid production and biofilm formation. Mol. Microbiol. 57: 1143-1158.
    • (2005) Mol. Microbiol. , vol.57 , pp. 1143-1158
    • Stanley, N.R.1    Lazazzera, B.A.2
  • 35
    • 37349092681 scopus 로고    scopus 로고
    • Papain-like cysteine proteases: Key players at molecular battlefields employed by both plants and their invaders
    • Takayuki, S. and R. A. L. van der Hoorn. 2008. Papain-like cysteine proteases: Key players at molecular battlefields employed by both plants and their invaders. Mol. Plant Pathol. 9: 119-125.
    • (2008) Mol. Plant Pathol. , vol.9 , pp. 119-125
    • Takayuki, S.1    van der Hoorn, R.A.L.2
  • 36
    • 0027250038 scopus 로고
    • Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis
    • Uchida, I., S. Makino, C. Sasakawa, M. Yoshikawa, C. Sugimoto, and N. Terakado. 1993. Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis. Mol. Microbiol. 9: 487-496.
    • (1993) Mol. Microbiol. , vol.9 , pp. 487-496
    • Uchida, I.1    Makino, S.2    Sasakawa, C.3    Yoshikawa, M.4    Sugimoto, C.5    Terakado, N.6
  • 37
    • 33646056411 scopus 로고    scopus 로고
    • A quenched fluorescent dipeptide for assaying dispase-and thermolysin-like proteases
    • Weimer, S., K. Oertel, and H.-L. Fuchsbauer. 2006. A quenched fluorescent dipeptide for assaying dispase-and thermolysin-like proteases. Anal. Biochem. 352: 110-119.
    • (2006) Anal. Biochem. , vol.352 , pp. 110-119
    • Weimer, S.1    Oertel, K.2    Fuchsbauer, H.-L.3
  • 38
    • 33645064834 scopus 로고    scopus 로고
    • Morphogenetic surfactants and their role in the formation of aerial hyphae in Streptomyces coelicolor
    • Willey, J. M., A. Willems, S. Kodani, and J. R. Nodwell. 2006. Morphogenetic surfactants and their role in the formation of aerial hyphae in Streptomyces coelicolor. Mol. Microbiol. 59: 731-742.
    • (2006) Mol. Microbiol. , vol.59 , pp. 731-742
    • Willey, J.M.1    Willems, A.2    Kodani, S.3    Nodwell, J.R.4
  • 39
    • 44349088345 scopus 로고    scopus 로고
    • Surfactant protein of the Streptomyces subtilisin inhibitor family inhibits transglutaminase activation in Streptomyces hygroscopicus
    • Zhang, D., M. Wang, G. Du, Q. Zhao, J. Wu, and J. Chen. 2008. Surfactant protein of the Streptomyces subtilisin inhibitor family inhibits transglutaminase activation in Streptomyces hygroscopicus. J. Agric. Food Chem. 56: 3403-3408.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 3403-3408
    • Zhang, D.1    Wang, M.2    Du, G.3    Zhao, Q.4    Wu, J.5    Chen, J.6
  • 40
    • 0041767546 scopus 로고    scopus 로고
    • Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease
    • Zotzel, J., P. Keller, and H.-L. Fuchsbauer. 2003. Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease. Eur. J. Biochem. 270: 3214-3222.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3214-3222
    • Zotzel, J.1    Keller, P.2    Fuchsbauer, H.-L.3
  • 41
    • 0142120480 scopus 로고    scopus 로고
    • Activated transglutaminase from Streptomyces mobaraensis is processed by a tripeptidyl aminopeptidase in the final step
    • Zotzel, J., R. Pasternack, C. Pelzer, M. Mainusch, and H.-L. Fuchsbauer. 2003. Activated transglutaminase from Streptomyces mobaraensis is processed by a tripeptidyl aminopeptidase in the final step. Eur. J. Biochem. 270: 4149-4155.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4149-4155
    • Zotzel, J.1    Pasternack, R.2    Pelzer, C.3    Mainusch, M.4    Fuchsbauer, H.-L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.