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Volumn 67, Issue 1, 1999, Pages 259-265

Effects of site-directed mutagenesis of Escherichia coli heat-labile enterotoxin on ADP-ribosyltransferase activity and interaction with ADP- ribosylation factors

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DERIVATIVE; ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE DIPHOSPHATE RIBOSYLAGMATINE; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; AMINO ACID; ARGININE; CHOLERA TOXIN; DITHIOTHREITOL; ESCHERICHIA COLI ENTEROTOXIN; GUANINE NUCLEOTIDE BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEIN SUBUNIT; SERINE; TRYPSIN; TYROSINE; UNCLASSIFIED DRUG; VALINE;

EID: 0032945714     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.67.1.259-265.1999     Document Type: Article
Times cited : (20)

References (36)
  • 1
    • 0024418570 scopus 로고
    • Photolabeling of Glu-129 of the S-1 subunit of pertussis toxin with NAD
    • Barbieri, J. T., L. M. Mende-Mueller, R. Rappuoli, and R. J. Collier. 1989. Photolabeling of Glu-129 of the S-1 subunit of pertussis toxin with NAD. Infect. Immun. 57:3549-3554.
    • (1989) Infect. Immun. , vol.57 , pp. 3549-3554
    • Barbieri, J.T.1    Mende-Mueller, L.M.2    Rappuoli, R.3    Collier, R.J.4
  • 2
    • 0009777440 scopus 로고
    • Recent advances in the understanding of multiple roles of G proteins in coupling of receptors to ionic channels and other effectors
    • J. Moss and M. Vaughan (ed.). American Society for Microbiology, Washington, D.C.
    • Birnbaumer, L., R. Mattera, A. Yatani, J. Codina, A. M. J. VanDongen, and A. M. Brown. 1990. Recent advances in the understanding of multiple roles of G proteins in coupling of receptors to ionic channels and other effectors, p. 225-266. In J. Moss and M. Vaughan (ed.), ADP-ribosylating toxins and G proteins: insights into signal transduction. American Society for Microbiology, Washington, D.C.
    • (1990) ADP-Ribosylating Toxins and G Proteins: Insights into Signal Transduction , pp. 225-266
    • Birnbaumer, L.1    Mattera, R.2    Yatani, A.3    Codina, J.4    VanDongen, A.M.J.5    Brown, A.M.6
  • 3
    • 0021280847 scopus 로고
    • NAD binding site of diphtheria toxin: Identification of a residue within the nicotinamide subsite by photochemical modification with NAD
    • Carroll, S. F., and R. J. Collier. 1984. NAD binding site of diphtheria toxin: identification of a residue within the nicotinamide subsite by photochemical modification with NAD. Proc. Natl. Acad. Sci. USA 81:3307-3311.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3307-3311
    • Carroll, S.F.1    Collier, R.J.2
  • 4
    • 0023664604 scopus 로고
    • Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin
    • Carroll, S. F., and R. J. Collier. 1987. Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin. J. Biol. Chem. 262: 8707-8711.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8707-8711
    • Carroll, S.F.1    Collier, R.J.2
  • 5
    • 0030760897 scopus 로고    scopus 로고
    • Coatomer (COPI)-coated vesicles: Role in intracellular transport and protein sorting
    • Cosson, P., and F. Letourneur. 1997. Coatomer (COPI)-coated vesicles: role in intracellular transport and protein sorting. Curr. Opin. Cell Biol. 9:484-487.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 484-487
    • Cosson, P.1    Letourneur, F.2
  • 6
    • 0028138580 scopus 로고
    • Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins
    • Domenighini, M., C. Magagnoli, M. Pizza, and R. Rappuoli. 1994. Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins. Mol. Microbiol. 14:41-50.
    • (1994) Mol. Microbiol. , vol.14 , pp. 41-50
    • Domenighini, M.1    Magagnoli, C.2    Pizza, M.3    Rappuoli, R.4
  • 9
    • 0031027336 scopus 로고    scopus 로고
    • Protease susceptibility and toxicity of heat-labile enterotoxins with a mutation in the active site or in the protease-sensitive loop
    • Giannelli, V., M. R. Fontana, M. M. Giuliani, D. Guangcai, R. Rappuoli, and M. Pizza. 1997. Protease susceptibility and toxicity of heat-labile enterotoxins with a mutation in the active site or in the protease-sensitive loop. Infect. Immun. 63:331-334.
    • (1997) Infect. Immun. , vol.63 , pp. 331-334
    • Giannelli, V.1    Fontana, M.R.2    Giuliani, M.M.3    Guangcai, D.4    Rappuoli, R.5    Pizza, M.6
  • 11
    • 0027519408 scopus 로고
    • NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum
    • Jung, M., I. Just, J. Damme, J. Vandekerckhove, and K. Aktories. 1993. NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum. J. Biol. Chem. 268:23215-23218.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23215-23218
    • Jung, M.1    Just, I.2    Damme, J.3    Vandekerckhove, J.4    Aktories, K.5
  • 12
    • 0021250807 scopus 로고
    • Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin
    • Kahn, R. A., and A. G. Gilman. 1984 Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin. J. Biol. Chem. 259:6228-6234.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6228-6234
    • Kahn, R.A.1    Gilman, A.G.2
  • 13
    • 0025909488 scopus 로고
    • Activation of Escherichia coli heat-labile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins
    • Lee, C.-M., P. P. Chang, S.-C. Tsai, S.-C. R. Adamik, S. R. Price, B. C. Kunz, J. Moss, E. M. Twiddy, and R. K. Holmes. 1991. Activation of Escherichia coli heat-labile enterotoxins by native and recombinant adenosine diphosphate-ribosylation factors, 20-kD guanine nucleotide-binding proteins. J. Clin. Invest. 87:1780-1786.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1780-1786
    • Lee, C.-M.1    Chang, P.P.2    Tsai, S.-C.3    Adamik, S.-C.R.4    Price, S.R.5    Kunz, B.C.6    Moss, J.7    Twiddy, E.M.8    Holmes, R.K.9
  • 14
    • 0025900567 scopus 로고
    • Effect of site-directed mutagenic alterations on ADP-ribosyltransferase activity of the A subunit of Escherichia coli heat-labile enterotoxin
    • Lobet, Y., C. W. Cluff, and W. Cieplak, Jr. 1991. Effect of site-directed mutagenic alterations on ADP-ribosyltransferase activity of the A subunit of Escherichia coli heat-labile enterotoxin. Infect. Immun. 59:2870-2879.
    • (1991) Infect. Immun. , vol.59 , pp. 2870-2879
    • Lobet, Y.1    Cluff, C.W.2    Cieplak W., Jr.3
  • 15
    • 0029852233 scopus 로고    scopus 로고
    • Mutations in the A subunit affect yield, stability, and protease sensitivity of nontoxic derivatives of heat-labile enterotoxin
    • Magagnoli, C., R. Manetti, M. R. Fontana, V. Giannelli, M. M. Giuliani, R. Rappuoli, and M. Pizza. 1996. Mutations in the A subunit affect yield, stability, and protease sensitivity of nontoxic derivatives of heat-labile enterotoxin. Infect. Immun. 64:5434-5438.
    • (1996) Infect. Immun. , vol.64 , pp. 5434-5438
    • Magagnoli, C.1    Manetti, R.2    Fontana, M.R.3    Giannelli, V.4    Giuliani, M.M.5    Rappuoli, R.6    Pizza, M.7
  • 16
    • 0027264855 scopus 로고
    • Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase
    • McDonald, L. J., and J. Moss. 1993. Stimulation by nitric oxide of an NAD linkage to glyceraldehyde-3-phosphate dehydrogenase. Proc. Natl. Acad. Sci. USA 90:6238-6241.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6238-6241
    • McDonald, L.J.1    Moss, J.2
  • 17
    • 0027250465 scopus 로고
    • Nitric oxide-independent, thiol-associated ADP-ribosylation inactivates aldehyde dehydrogenase
    • McDonald, L. J., and J. Moss. 1993. Nitric oxide-independent, thiol-associated ADP-ribosylation inactivates aldehyde dehydrogenase. J. Biol. Chem. 268:17878-17882.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17878-17882
    • McDonald, L.J.1    Moss, J.2
  • 18
    • 0018308483 scopus 로고
    • Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulfide bond reduction, and subunit composition
    • Mekalanos, J. J., R. J. Collier, and W. R. Romig. 1979. Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulfide bond reduction, and subunit composition. J. Biol. Chem. 254:5855-5861.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5855-5861
    • Mekalanos, J.J.1    Collier, R.J.2    Romig, W.R.3
  • 19
    • 0027955887 scopus 로고
    • Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 Å resolution
    • Merritt, E. A., S. E. Pronk, T. K. Sixma, K. H. Kalk, B. A. M. Van Zanten, and W. G. J. Hol. 1994. Structure of partially-activated E. coli heat-labile enterotoxin (LT) at 2.6 Å resolution. FEBS Lett. 337:88-92.
    • (1994) FEBS Lett. , vol.337 , pp. 88-92
    • Merritt, E.A.1    Pronk, S.E.2    Sixma, T.K.3    Kalk, K.H.4    Van Zanten, B.A.M.5    Hol, W.G.J.6
  • 20
    • 0028970215 scopus 로고
    • Mutation of a buried residue causes loss of activity hut no conformational change in the heat-labile enterotoxin of Escherichia coli
    • Merrit, E. A., S. Sarfaty, M. Pizza, M. Domenighini, R. Rappuoli, and W. G. J. Hol. 1995. Mutation of a buried residue causes loss of activity hut no conformational change in the heat-labile enterotoxin of Escherichia coli. Nat. Struct. Biol. 2:269-272.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 269-272
    • Merrit, E.A.1    Sarfaty, S.2    Pizza, M.3    Domenighini, M.4    Rappuoli, R.5    Hol, W.G.J.6
  • 21
    • 0019839033 scopus 로고
    • Escherichia coli heat-labile enterotoxin: Ganglioside specificity and ADP-ribosyltransferase activity
    • Moss, J., J. C. Osborne Jr., P. H. Fishman, S. Nakaya, and D. C. Robertson. 1981. Escherichia coli heat-labile enterotoxin: ganglioside specificity and ADP-ribosyltransferase activity. J. Biol. Chem. 256:12861-12865.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12861-12865
    • Moss, J.1    Osborne J.C., Jr.2    Fishman, P.H.3    Nakaya, S.4    Robertson, D.C.5
  • 22
    • 0027466663 scopus 로고
    • Interaction of ADP-ribosylation factor with Eschenchia coli enterotoxin that contains an inactivating lysine 112 substitution
    • Moss, J., S. J. Stanley, M. Vaughan, and T. Tsuji. 1993. Interaction of ADP-ribosylation factor with Eschenchia coli enterotoxin that contains an inactivating lysine 112 substitution. J. Biol. Chem. 268:6383-6387.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6383-6387
    • Moss, J.1    Stanley, S.J.2    Vaughan, M.3    Tsuji, T.4
  • 23
    • 0023742061 scopus 로고
    • ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins
    • Moss, J., and M. Vaughan. 1988. ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins. Adv. Enzymol. Relat. Areas Mol. Biol. 61:303-379.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 303-379
    • Moss, J.1    Vaughan, M.2
  • 24
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: Activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss, J., and M. Vaughan. 1995. Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270:12327-12330.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 25
    • 0025215485 scopus 로고
    • Mechanism of cholera toxin activation by a guanine nucleotide-dependent 19 kDa protein
    • Noda, M., S.-C. Tsai, R. Adamik, J. Moss, and M. Vaughan. 1990. Mechanism of cholera toxin activation by a guanine nucleotide-dependent 19 kDa protein. Biochim. Biophys. Acta 1034:195-199.
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 195-199
    • Noda, M.1    Tsai, S.-C.2    Adamik, R.3    Moss, J.4    Vaughan, M.5
  • 28
    • 0026666365 scopus 로고
    • Effects of phospholipid and GTP on recombinant ADP-ribosylation factors (ARFs). Molecular basis for differences in requirements for activity of mammalian ARFs
    • Price, S. R., C. F. Welsh, R. S. Haun, S. J. Stanley, J. Moss, and M. Vaughan. 1992. Effects of phospholipid and GTP on recombinant ADP-ribosylation factors (ARFs). Molecular basis for differences in requirements for activity of mammalian ARFs. J. Biol. Chem. 267:17766-17772.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17766-17772
    • Price, S.R.1    Welsh, C.F.2    Haun, R.S.3    Stanley, S.J.4    Moss, J.5    Vaughan, M.6
  • 29
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. 1994. Mechanisms of intracellular protein transport. Nature 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 31
    • 0023887976 scopus 로고
    • Separation of the 24 kDa substrate for Botulinum C3 ADP-ribosyltransferase and the cholera toxin ADP-ribosylation factor
    • Tsai, S.-C., R. Adamik, J. Moss, and K. Aktories. 1988. Separation of the 24 kDa substrate for Botulinum C3 ADP-ribosyltransferase and the cholera toxin ADP-ribosylation factor. Biochem. Biophys. Res. Commun. 152:957-961.
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 957-961
    • Tsai, S.-C.1    Adamik, R.2    Moss, J.3    Aktories, K.4
  • 32
    • 0023930341 scopus 로고
    • Stimulation of choleragen enzymatic activities by GTP and two soluble proteins purified from bovine brain
    • Tsai, S.-C., M. Noda, R. Adamik, P. P. Chang, H.-C. Chen, J. Moss, and M. Vaughan. 1988. Stimulation of choleragen enzymatic activities by GTP and two soluble proteins purified from bovine brain. J. Biol. Chem. 263:1768-1772.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1768-1772
    • Tsai, S.-C.1    Noda, M.2    Adamik, R.3    Chang, P.P.4    Chen, H.-C.5    Moss, J.6    Vaughan, M.7
  • 33
    • 0025731953 scopus 로고
    • Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells
    • Tsuchiya, M., S. R. Price, S.-C. Tsai, J. Moss, and M. Vaughan. 1991. Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. J. Biol. Chem. 266:2772-2777.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2772-2777
    • Tsuchiya, M.1    Price, S.R.2    Tsai, S.-C.3    Moss, J.4    Vaughan, M.5
  • 34
    • 0025641214 scopus 로고
    • A single amino acid substitution in the A subunit of Escherichia coli enterotoxin results in a loss of its toxic activity
    • Tsuji, T., T. Inoue, A. Miyama, K. Okamoto, T. Honda, and T. Miwatani. 1990. A single amino acid substitution in the A subunit of Escherichia coli enterotoxin results in a loss of its toxic activity. J. Biol. Chem. 265:22520-22525.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22520-22525
    • Tsuji, T.1    Inoue, T.2    Miyama, A.3    Okamoto, K.4    Honda, T.5    Miwatani, T.6
  • 35
    • 0029130505 scopus 로고
    • The Arg7Lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the A subunit
    • Van den Akker, F., E. A. Merritt, M. G. Pizza, M. Domenighini, R. Rappuoli, and W. G. J. Hol. 1995. The Arg7Lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the A subunit. Biochemistry 34:10996-11004.
    • (1995) Biochemistry , vol.34 , pp. 10996-11004
    • Van Den Akker, F.1    Merritt, E.A.2    Pizza, M.G.3    Domenighini, M.4    Rappuoli, R.5    Hol, W.G.J.6
  • 36
    • 0031441034 scopus 로고    scopus 로고
    • Crystal structure of a non-toxic mutant of heat-labile enterotoxin, which is a potent mucosal adjuvant
    • Van den Akker, F., M. Pizza, R. Rappuoli, and W. G. Hol. 1997. Crystal structure of a non-toxic mutant of heat-labile enterotoxin, which is a potent mucosal adjuvant. Protein Sci. 6:2650-2654.
    • (1997) Protein Sci. , vol.6 , pp. 2650-2654
    • Van Den Akker, F.1    Pizza, M.2    Rappuoli, R.3    Hol, W.G.4


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