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Volumn 192, Issue 21, 2010, Pages 5799-5805

Residue histidine 669 is essential for the catalytic activity of Bacillus anthracis lethal factor

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; HISTIDINE; ANTHRAX TOXIN; BACTERIAL ANTIGEN; BACTERIAL TOXIN; PROTEIN BINDING;

EID: 78049384875     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00485-10     Document Type: Article
Times cited : (3)

References (38)
  • 1
    • 12944322216 scopus 로고    scopus 로고
    • Anthrax toxin: The long and winding road that leads to the kill
    • Abrami, L., N. Reig, and F. G. Goot. 2005. Anthrax toxin: the long and winding road that leads to the kill. Trends Microbiol. 13:72-78.
    • (2005) Trends Microbiol. , vol.13 , pp. 72-78
    • Abrami, L.1    Reig, N.2    Goot, F.G.3
  • 2
    • 0030859761 scopus 로고    scopus 로고
    • Site directed mutagenesis of histidine residues in anthrax toxin lethal factor binding domain reduces toxicity
    • Arora, N. 1997. Site directed mutagenesis of histidine residues in anthrax toxin lethal factor binding domain reduces toxicity. Mol. Cell. Biochem. 177:7-14.
    • (1997) Mol. Cell. Biochem. , vol.177 , pp. 7-14
    • Arora, N.1
  • 3
    • 0027403919 scopus 로고
    • Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides
    • Arora, N., and S. H. Leppla. 1993. Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides. J. Biol. Chem. 268:3334-3341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3334-3341
    • Arora, N.1    Leppla, S.H.2
  • 4
    • 40849102523 scopus 로고    scopus 로고
    • Efficient production and characterization of Bacillus anthracis lethal factor and a novel inactive mutant rLFm-Y236F
    • Cao, S., Z. Liu, A. Guo, Y. Li, C. Zhang, G. Wu, C. Feng, Y. Tan, and H. Chen. 2008. Efficient production and characterization of Bacillus anthracis lethal factor and a novel inactive mutant rLFm-Y236F. Protein Expr. Purif. 59:25-30.
    • (2008) Protein Expr. Purif. , vol.59 , pp. 25-30
    • Cao, S.1    Liu, Z.2    Guo, A.3    Li, Y.4    Zhang, C.5    Wu, G.6    Feng, C.7    Tan, Y.8    Chen, H.9
  • 5
    • 70349413068 scopus 로고    scopus 로고
    • Investigation of new dominant-negative inhibitors of anthrax protective antigen mutants for use in therapy and vaccination
    • Cao, S., A. Guo, Z. Liu, Y. Tan, G. Wu, C. Zhang, Y. Zhao, and H. Chen. 2009. Investigation of new dominant-negative inhibitors of anthrax protective antigen mutants for use in therapy and vaccination. Infect. Immun. 77:4679-4687.
    • (2009) Infect. Immun. , vol.77 , pp. 4679-4687
    • Cao, S.1    Guo, A.2    Liu, Z.3    Tan, Y.4    Wu, G.5    Zhang, C.6    Zhao, Y.7    Chen, H.8
  • 6
    • 0036468526 scopus 로고    scopus 로고
    • Quickening the pace of anthrax research: Three advances point towards possible therapies
    • Chaudry, G., J. Moayeri, M. Liu, and S. H. Leppla. 2002. Quickening the pace of anthrax research: three advances point towards possible therapies. Trends Microbiol. 10:58-62.
    • (2002) Trends Microbiol. , vol.10 , pp. 58-62
    • Chaudry, G.1    Moayeri, J.2    Liu, M.3    Leppla, S.H.4
  • 7
    • 33748350938 scopus 로고    scopus 로고
    • Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II
    • Cheng, Y., C. Hsueh, S. Lu, and T. Liao. 2006. Identification of three crucial histidine residues (His115, His132 and His297) in porcine deoxyribonuclease II. Biochem. J. 398:177-185.
    • (2006) Biochem. J. , vol.398 , pp. 177-185
    • Cheng, Y.1    Hsueh, C.2    Lu, S.3    Liao, T.4
  • 8
    • 0038322024 scopus 로고    scopus 로고
    • Anthrax lethal factor proteolysis and inactivation of MAPK kinase
    • Chopra, A. P., S. A. Boone, X. Liang, and N. S. Duesbery. 2003. Anthrax lethal factor proteolysis and inactivation of MAPK kinase. J. Biol. Chem. 278:9402-9406.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9402-9406
    • Chopra, A.P.1    Boone, S.A.2    Liang, X.3    Duesbery, N.S.4
  • 9
    • 7944233858 scopus 로고    scopus 로고
    • His-404 and His-405 are essential for enzyme catalytic activities of a bacterial indole-3-acetyl-L-aspartic acid hydrolase
    • Chou, J. C., W. H. Welch, and J. D. Cohen. 2004. His-404 and His-405 are essential for enzyme catalytic activities of a bacterial indole-3-acetyl-L- aspartic acid hydrolase. Plant Cell Physiol. 45:1335-1341.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1335-1341
    • Chou, J.C.1    Welch, W.H.2    Cohen, J.D.3
  • 12
    • 11844262754 scopus 로고    scopus 로고
    • Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1
    • DOI 10.1128/JB.187.2.480-487.2005
    • Fujiwara, T., S. Aoki, H. Komatsuzawa, T. Nishida, M. Ohara, H. Suginaka, and M. Sugai. 2005. Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1. J. Bacteriol. 187:480-487. (Pubitemid 40096236)
    • (2005) Journal of Bacteriology , vol.187 , Issue.2 , pp. 480-487
    • Fujiwara, T.1    Aoki, S.2    Komatsuzawa, H.3    Nishida, T.4    Ohara, M.5    Suginaka, H.6    Sugai, M.7
  • 13
    • 0031946979 scopus 로고    scopus 로고
    • Lethal factor active-site mutations affect catalytic activity in vitro
    • Hammond, S. E., and P. C. Hanna. 1998. Lethal factor active-site mutations affect catalytic activity in vitro. Infect. Immun. 66:2374-2378.
    • (1998) Infect. Immun. , vol.66 , pp. 2374-2378
    • Hammond, S.E.1    Hanna, P.C.2
  • 14
    • 0035098034 scopus 로고    scopus 로고
    • Effect of His1992 mutation on the activity of alginate lyase A1-III from sphingomonas species A1
    • Hye-jin, Y., Y. J. Choi, O. Miyake, W. Hashimoto, K. Mutata, and B. Mikami. 2001. Effect of His1992 mutation on the activity of alginate lyase A1-III from sphingomonas species A1. J. Microbiol. Biotechnol. 11:118-123.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 118-123
    • Hye-jin, Y.1    Choi, Y.J.2    Miyake, O.3    Hashimoto, W.4    Mutata, K.5    Mikami, B.6
  • 15
    • 0348111399 scopus 로고    scopus 로고
    • Implication of pH in the catalytic properties of anthrax lethal factor
    • Kim, J., Y. G. Chai, and M. Y. Yoon. 2004. Implication of pH in the catalytic properties of anthrax lethal factor. Biochem. Biophys. Res. Commun. 313:217-222.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 217-222
    • Kim, J.1    Chai, Y.G.2    Yoon, M.Y.3
  • 18
    • 0028088404 scopus 로고
    • Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity
    • Klimpel, K. R., N. Arora, and S. H. Leppla. 1994. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol. Microbiol. 13:1093-1100.
    • (1994) Mol. Microbiol. , vol.13 , pp. 1093-1100
    • Klimpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 20
    • 0034833135 scopus 로고    scopus 로고
    • Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen
    • Kumar, P., N. Ahuja, and R. Bhatnagar. 2001. Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen. Infect. Immun. 69:6532-6536.
    • (2001) Infect. Immun. , vol.69 , pp. 6532-6536
    • Kumar, P.1    Ahuja, N.2    Bhatnagar, R.3
  • 21
    • 4444267311 scopus 로고    scopus 로고
    • Structure of heptameric protective antigen bound to an anthrax toxin receptor: A role for receptor in pH-dependent pore formation
    • Lacy, D. B., D. J. Wigelsworth, R. A. Melnyk, S. C. Harrison, and R. J. Collier. 2004. Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Proc. Natl. Acad. Sci. U. S. A. 101:13147-13151.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13147-13151
    • Lacy, D.B.1    Wigelsworth, D.J.2    Melnyk, R.A.3    Harrison, S.C.4    Collier, R.J.5
  • 22
    • 0037169549 scopus 로고    scopus 로고
    • Mapping the anthrax protective antigen binding site on the lethal and edema factors
    • Lacy, D. B., M. Mourez, A. Fouassier, and R. J. Collier. 2002. Mapping the anthrax protective antigen binding site on the lethal and edema factors. J. Biol. Chem. 277:3006-3010.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3006-3010
    • Lacy, D.B.1    Mourez, M.2    Fouassier, A.3    Collier, R.J.4
  • 23
    • 0001616921 scopus 로고    scopus 로고
    • Anthrax toxin fusion proteins for intracellular delivery of macromolecules
    • Leppla, S. H., N. Arora, and M. Varughese. 1999. Anthrax toxin fusion proteins for intracellular delivery of macromolecules. J. Appl. Microbiol. 87:284.
    • (1999) J. Appl. Microbiol. , vol.87 , pp. 284
    • Leppla, S.H.1    Arora, N.2    Varughese, M.3
  • 25
    • 0035097284 scopus 로고    scopus 로고
    • Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin
    • Mogridge, J., M. Mourez, and R. J. Collier. 2001. Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin. J. Bacteriol. 183:2111-2116.
    • (2001) J. Bacteriol. , vol.183 , pp. 2111-2116
    • Mogridge, J.1    Mourez, M.2    Collier, R.J.3
  • 26
    • 3242804491 scopus 로고    scopus 로고
    • Stop the killer: How to inhibit the anthrax lethal factor metalloprotease
    • Montecucco, C., F. Tonello, and G. Zanotti. 2004. Stop the killer: how to inhibit the anthrax lethal factor metalloprotease. Trends Biochem. Sci. 29:282-285.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 282-285
    • Montecucco, C.1    Tonello, F.2    Zanotti, G.3
  • 29
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • Park, J. M., F. R. Greten, Z. W. Li, and M. Karin. 2002. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 297:2048-2051.
    • (2002) Science , vol.297 , pp. 2048-2051
    • Park, J.M.1    Greten, F.R.2    Li, Z.W.3    Karin, M.4
  • 31
    • 1642385648 scopus 로고    scopus 로고
    • Anthrax toxin: Can a little be a good thing?
    • Sanchez, A. M., and K. A. Bradley. 2004. Anthrax toxin: can a little be a good thing? Trends Microbiol. 12:143-145.
    • (2004) Trends Microbiol. , vol.12 , pp. 143-145
    • Sanchez, A.M.1    Bradley, K.A.2
  • 32
    • 0346433832 scopus 로고    scopus 로고
    • Tyrosine-728 and glutamic acid-735 are essential for the metalloproteolytic activity of the lethal factor of Bacillus anthracis
    • Tonello, F., L. Naletto, V. Romanello, F. D. Molin, and C. Montecucco. 2004. Tyrosine-728 and glutamic acid-735 are essential for the metalloproteolytic activity of the lethal factor of Bacillus anthracis. Biochem. Biophys. Res. Commun. 313:496-502.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 496-502
    • Tonello, F.1    Naletto, L.2    Romanello, V.3    Molin, F.D.4    Montecucco, C.5
  • 33
    • 0037173617 scopus 로고    scopus 로고
    • Screening inhibitors of anthrax lethal factor
    • DOI 10.1038/418386a
    • Tonello, F., M. Seveso, O. Marin, M. Mock, and C. Montecucco. 2002. Screening inhibitors of anthrax lethal factor. Nature 418:386. (Pubitemid 34826833)
    • (2002) Nature , vol.418 , Issue.6896 , pp. 386
    • Tonello, F.1    Seveso, M.2    Marin, O.3    Mock, M.4    Montecucco, C.5
  • 34
    • 0141994729 scopus 로고    scopus 로고
    • The metalloproteolytic activity of the anthrax lethal factor is substrate-inhibited
    • Tonello, F., P. Ascenzi, and C. Montecucco. 2003. The metalloproteolytic activity of the anthrax lethal factor is substrate-inhibited. J. Biol. Chem. 278:40075-40078.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40075-40078
    • Tonello, F.1    Ascenzi, P.2    Montecucco, C.3
  • 35
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • DOI 10.1042/0264-6021:3520739
    • Vitale, G., L. Bernardi, G. Napolitani, M. Mock, and C. Montecucco. 2000. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 3:739-745. (Pubitemid 32015030)
    • (2000) Biochemical Journal , vol.352 , Issue.3 , pp. 739-745
    • Vitale, G.1    Bernardi, L.2    Napolitani, G.3    Mock, M.4    Montecucco, C.5
  • 36
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale, G., R. Pellizzari, C. Recchi, G. Napolitani, M. Mock, and C. Montecucco. 1998. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248:706-711.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 37
    • 0037868151 scopus 로고    scopus 로고
    • Characterization of dominant-negative forms of anthrax protective antigen
    • Yan, M., and R. J. Collier. 2003. Characterization of dominant-negative forms of anthrax protective antigen. Mol. Med. 9:46-51.
    • (2003) Mol. Med. , vol.9 , pp. 46-51
    • Yan, M.1    Collier, R.J.2
  • 38
    • 38649141825 scopus 로고    scopus 로고
    • Selection and evaluation of the immunogenicity of protective antigen mutants as anthrax vaccine candidates
    • Yan, M., M. H. Roehrl, E. Basar, and J. Y. Wang. 2008. Selection and evaluation of the immunogenicity of protective antigen mutants as anthrax vaccine candidates. Vaccine 26:947-955.
    • (2008) Vaccine , vol.26 , pp. 947-955
    • Yan, M.1    Roehrl, M.H.2    Basar, E.3    Wang, J.Y.4


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