메뉴 건너뛰기




Volumn 27, Issue 12, 2013, Pages 4723-4730

Auto ADP-ribosylation of NarE, a neisseria meningitidis ADP-ribosyltransferase, regulates its catalytic activities

Author keywords

NAD; NAD glycohydrolase; Pathogenesis

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE TRIPHOSPHATE; ARGININE; GUANOSINE TRIPHOSPHATE; HYDROXYLAMINE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE NARE; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; NOVOBIOCIN; UNCLASSIFIED DRUG;

EID: 84890506649     PISSN: None     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.13-229955     Document Type: Article
Times cited : (9)

References (38)
  • 1
    • 0020673403 scopus 로고
    • The pathogenic potential of commensal species of neisseria
    • Johnson, A. P. (1983) The pathogenic potential of commensal species of Neisseria. J. Clin. Pathol. 36, 213-223
    • (1983) J. Clin. Pathol. , vol.36 , pp. 213-223
    • Johnson, A.P.1
  • 4
    • 0023742061 scopus 로고
    • Adp-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins
    • Moss, J., and Vaughan, M. (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
  • 5
    • 0034629478 scopus 로고    scopus 로고
    • Complete genome sequence of neisseria meningitidis serogroup b strain mc58
    • Tettelin, H., Saunders, N. J., Heidelberg, J., Jeffries, A. C., Nelson, K. E., Eisen, J. A., Ketchum, K. A., Hood, D. W., Peden, J. F., Dodson, R. J., Nelson, W. C., Gwinn, M. L., DeBoy, R., Peterson, J. D., Hickey, E. K., Haft, D. H., Salzberg, S. L., White, O., Fleischmann, R. D., Dougherty, B. A., Mason, T., Ciecko, A., Parksey, D. S., Blair, E., Cittone, H., Clark, E. B., Cotton, M. D., Utterback, T. R., Khouri, H., Qin, H., Vamathevan, J., Gill, J., Scarlato, V., Masignani, V., Pizza, M., Grandi, G., Sun, L., Smith, H. O., Fraser, C. M., Moxon, E. R., Rappuoli, R., and Venter, J. C. (2000) Complete genome sequence of Neisseria meningitidis serogroup B strain MC58. Science 287, 1809-1815
    • (2000) Science , vol.287 , pp. 1809-1815
    • Tettelin, H.1    Saunders, N.J.2    Heidelberg, J.3    Jeffries, A.C.4    Nelson, K.E.5    Eisen, J.A.6    Ketchum, K.A.7
  • 7
    • 70450270635 scopus 로고    scopus 로고
    • Identification of an iron-sulfur cluster that modulates the enzymatic activity in nare, a neisseria meningitidis adp-ribosyltransferase
    • Del Vecchio, M., Pogni, R., Baratto, M. C., Nobbs, A., Rappuoli, R., Pizza, M., and Balducci, E. (2009) Identification of an iron-sulfur cluster that modulates the enzymatic activity in NarE, a Neisseria meningitidis ADP-ribosyltransferase. J. Biol. Chem. 284, 33040-33047
    • (2009) J. Biol. Chem. , vol.284 , pp. 33040-33047
    • Del Vecchio, M.1    Pogni, R.2    Baratto, M.C.3    Nobbs, A.4    Rappuoli, R.5    Pizza, M.6    Balducci, E.7
  • 9
    • 23944509984 scopus 로고    scopus 로고
    • A filter plate-based assay for mono adenosine 5=-diphosphate- ribosyltransferases
    • Balducci, E. (2005) A filter plate-based assay for mono adenosine 5=-diphosphate-ribosyltransferases. Anal. Biochem. 344, 278-280
    • (2005) Anal. Biochem. , vol.344 , pp. 278-280
    • Balducci, E.1
  • 10
    • 0017042555 scopus 로고
    • Hydrolysis of nicotinamide adenine dinucleotide by choleragen and its a protomer: Possible role in the activation of adenylate cyclase
    • Moss, J., Manganiello, V. C., and Vaughan, M. (1976) Hydrolysis of nicotinamide adenine dinucleotide by choleragen and its A protomer: possible role in the activation of adenylate cyclase. Proc. Natl. Acad. Sci. U. S. A. 73, 4424-4427
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 4424-4427
    • Moss, J.1    Manganiello, V.C.2    Vaughan, M.3
  • 11
    • 0026601666 scopus 로고
    • Specific inhibitors of poly(adp-ribose) synthetase and mono-(adp-ribosyl)transferase
    • Banasik, M., Komura, H., Shimoyama, M., and Ueda, K. (1992) Specific inhibitors of poly(ADP-ribose) synthetase and mono-(ADP-ribosyl)transferase. J. Biol. Chem. 267, 1569-1575
    • (1992) J. Biol. Chem. , vol.267 , pp. 1569-1575
    • Banasik, M.1    Komura, H.2    Shimoyama, M.3    Ueda, K.4
  • 13
    • 0000512471 scopus 로고
    • The isolation and properties of the isonicotinic acid hydrazide analogue of diphosphopyridine nucleotide
    • Zatman, L. J., Kaplan, N. O., Colowick, S. P., and Ciotti, M. M. (1954) The isolation and properties of the isonicotinic acid hydrazide analogue of diphosphopyridine nucleotide. J. Biol. Chem. 209, 467-484
    • (1954) J. Biol. Chem. , vol.209 , pp. 467-484
    • Zatman, L.J.1    Kaplan, N.O.2    Colowick, S.P.3    Ciotti, M.M.4
  • 14
    • 31044438096 scopus 로고    scopus 로고
    • Exchange of glutamine-217 to glutamate of clostridium limosum exoenzyme c3 turns the asparagine-specific adp-ribosyltransferase into an arginine-modifying enzyme
    • Vogelsgesang, M., and Aktories, K. (2006) Exchange of glutamine-217 to glutamate of Clostridium limosum exoenzyme C3 turns the asparagine-specific ADP-ribosyltransferase into an arginine-modifying enzyme. Biochemistry 45, 1017-1025
    • (2006) Biochemistry , vol.45 , pp. 1017-1025
    • Vogelsgesang, M.1    Aktories, K.2
  • 15
    • 0021813348 scopus 로고
    • Alkylationinduced mono(adp-ribosyl)-histones h1 and h2b. Hydroxylamine-resistant linkage in hepatoma cells
    • Kreimeyer, A., Adamietz, P., and Hilz, H. (1985) Alkylationinduced mono(ADP-ribosyl)-histones H1 and H2B. Hydroxylamine-resistant linkage in hepatoma cells. Biol. Chem. Hoppe Seyler 366, 537-544
    • (1985) Biol. Chem. Hoppe Seyler , vol.366 , pp. 537-544
    • Kreimeyer, A.1    Adamietz, P.2    Hilz, H.3
  • 16
    • 0022355594 scopus 로고
    • Amino acid-specific adp-ribosylation. Sensitivity to hydroxylamine of [cysteine(adp-ribose)]protein and [arginine (adp-ribose)]protein linkages
    • Hsia, J. A., Tsai, S. C., Adamik, R., Yost, D. A., Hewlett, E. L., and Moss, J. (1985) Amino acid-specific ADP-ribosylation. Sensitivity to hydroxylamine of [cysteine(ADP-ribose)]protein and [arginine (ADP-ribose)]protein linkages. J. Biol. Chem. 260, 16187-16191
    • (1985) J. Biol. Chem. , vol.260 , pp. 16187-16191
    • Hsia, J.A.1    Tsai, S.C.2    Adamik, R.3    Yost, D.A.4    Hewlett, E.L.5    Moss, J.6
  • 17
    • 0021111995 scopus 로고
    • Amino acid-specific adp-ribosylation
    • Moss, J., Yost, D. A., and Stanley, S. J. (1983) Amino acid-specific ADP-ribosylation. J. Biol. Chem. 258, 6466-6470
    • (1983) J. Biol. Chem. , vol.258 , pp. 6466-6470
    • Moss, J.1    Yost, D.A.2    Stanley, S.J.3
  • 18
    • 0025752819 scopus 로고
    • Cholera toxin-catalyzed [32p]adp-ribosylation of proteins
    • Gill, D. M., and Woolkalis, M. J. (1991) Cholera toxin-catalyzed [32P]ADP-ribosylation of proteins. Methods Enzymol. 195, 267-280
    • (1991) Methods Enzymol , vol.195 , pp. 267-280
    • Gill, D.M.1    Woolkalis, M.J.2
  • 19
    • 0023773267 scopus 로고
    • Adp-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions
    • Meyer, T., Koch, R., Fanick, W., and Hilz, H. (1988) ADP-ribosyl proteins formed by pertussis toxin are specifically cleaved by mercury ions. Biol. Chem. Hoppe Seyler 369, 579-583
    • (1988) Biol. Chem. Hoppe Seyler , vol.369 , pp. 579-583
    • Meyer, T.1    Koch, R.2    Fanick, W.3    Hilz, H.4
  • 23
    • 0028238028 scopus 로고
    • Automodification of arginine-specific adp-ribosyltransferase purified from chicken peripheral heterophils and alteration of the transferase activity
    • Yamada, K., Tsuchiya, M., Nishikori, Y., and Shimoyama, M. (1994) Automodification of arginine-specific ADP-ribosyltransferase purified from chicken peripheral heterophils and alteration of the transferase activity. Arch. Biochem. Biophys. 308, 31-36
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 31-36
    • Yamada, K.1    Tsuchiya, M.2    Nishikori, Y.3    Shimoyama, M.4
  • 24
    • 0033527561 scopus 로고    scopus 로고
    • Modification of the adp-ribosyltransferase and nad glycohydrolase activities of a mammalian transferase (adpribosyltransferase 5) by auto-Adp-ribosylation
    • Weng, B., Thompson, W. C., Kim, H. J., Levine, R. L., and Moss, J. (1999) Modification of the ADP-ribosyltransferase and NAD glycohydrolase activities of a mammalian transferase (ADPribosyltransferase 5) by auto-ADP-ribosylation. J. Biol. Chem. 274, 31797-31803
    • (1999) J. Biol. Chem. , vol.274 , pp. 31797-31803
    • Weng, B.1    Thompson, W.C.2    Kim, H.J.3    Levine, R.L.4    Moss, J.5
  • 25
    • 0028138580 scopus 로고
    • Common features of the nad-binding and catalytic site of adp-ribosylating toxins
    • Domenighini, M., Magagnoli, C., Pizza, M., and Rappuoli, R. (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
  • 26
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the nad-binding site of adpribosylating enzymes, expressed by eukaryotes, bacteria and t-even bacteriophages
    • Domenighini, M., and Rappuoli, R. (1996) Three conserved consensus sequences identify the NAD-binding site of ADPribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Mol. Microbiol. 21, 667-674
    • (1996) Mol. Microbiol. , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 27
    • 54249118102 scopus 로고    scopus 로고
    • Needle in the haystack: Structure-based toxin discovery
    • Fieldhouse, R. J., and Merrill, A. R. (2008) Needle in the haystack: structure-based toxin discovery. Trends. Biochem. Sci. 33, 546-556
    • (2008) Trends. Biochem. Sci. , vol.33 , pp. 546-556
    • Fieldhouse, R.J.1    Merrill, A.R.2
  • 28
    • 0029130505 scopus 로고
    • The arg7lys mutant of heat-labile enterotoxin exhibits great flexibility of active site loop 47-56 of the a subunit
    • Van, D. A. F., Merritt, E. A., Pizza, M., Domenighini, M., Rappuoli, R., and Hol, W. G. (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, D.A.F.1    Merritt, E.A.2    Pizza, M.3    Domenighini, M.4    Rappuoli, R.5    Hol, W.G.6
  • 29
    • 0029980483 scopus 로고    scopus 로고
    • Mouse t cell membrane proteins rt6-1 and rt6-2 are arginine/protein mono(adpribosyl)transferases and share secondary structure motifs with adp-ribosylating bacterial toxins
    • Koch-Nolte, F., Petersen, D., Balasubramanian, S., Haag, F., Kahlke, D., Willer, T., Kastelein, R., Bazan, F., and Thiele, H. G. (1996) Mouse T cell membrane proteins Rt6-1 and Rt6-2 are arginine/protein mono(ADPribosyl) transferases and share secondary structure motifs with ADP-ribosylating bacterial toxins. J. Biol. Chem. 271, 7686-7693
    • (1996) J. Biol. Chem. , vol.271 , pp. 7686-7693
    • Koch-Nolte, F.1    Petersen, D.2    Balasubramanian, S.3    Haag, F.4    Kahlke, D.5    Willer, T.6    Kastelein, R.7    Bazan, F.8    Thiele, H.G.9
  • 31
    • 0029910348 scopus 로고    scopus 로고
    • Glutamic acid 207 in rodent t-cell rt6 antigens is essential for argininespecific adp-ribosylation
    • Hara, N., Tsuchiya, M., and Shimoyama, M. (1996) Glutamic acid 207 in rodent T-cell RT6 antigens is essential for argininespecific ADP-ribosylation. J. Biol. Chem. 271, 29552-29555
    • (1996) J. Biol. Chem. , vol.271 , pp. 29552-29555
    • Hara, N.1    Tsuchiya, M.2    Shimoyama, M.3
  • 33
    • 0001461935 scopus 로고
    • The mechanism of the specific depression of an enzyme activity in cells in tissue culture
    • Lieberman, I. (1957) The mechanism of the specific depression of an enzyme activity in cells in tissue culture. J. Biol. Chem. 225, 883-898
    • (1957) J. Biol. Chem. , vol.225 , pp. 883-898
    • Lieberman, I.1
  • 34
    • 0019334486 scopus 로고
    • Selfinactivation of an erythrocyte nad glycohydrolase
    • Pekala, P. H., Yost, D. A., and Anderson, B. M. (1980) Selfinactivation of an erythrocyte NAD glycohydrolase. Mol. Cell. Biochem. 31, 49-56
    • (1980) Mol. Cell. Biochem. , vol.31 , pp. 49-56
    • Pekala, P.H.1    Yost, D.A.2    Anderson, B.M.3
  • 35
    • 0029760867 scopus 로고    scopus 로고
    • Regulation of nad-glycohydrolase activity by nad(-)-dependent auto-Adp-ribosylation
    • Han, M. K., Lee, J. Y., Cho, Y. S., Song, Y. M., An, N. H., Kim, H. R., and Kim, U. H. (1996) Regulation of NAD-glycohydrolase activity by NAD(-)-dependent auto-ADP-ribosylation. Biochem. J. 318, 903-908
    • (1996) Biochem. J. , vol.318 , pp. 903-908
    • Han, M.K.1    Lee, J.Y.2    Cho, Y.S.3    Song, Y.M.4    An, N.H.5    Kim, H.R.6    Kim, U.H.7
  • 36
    • 0036307241 scopus 로고    scopus 로고
    • Nad-dependent inhibition of the nad-glycohydrolase activity in a549 cells
    • Balducci, E., and Micossi, L. G. (2002) NAD-dependent inhibition of the NAD-glycohydrolase activity in A549 cells. Mol. Cell. Biochem. 233, 127-132
    • (2002) Mol. Cell. Biochem. , vol.233 , pp. 127-132
    • Balducci, E.1    Micossi, L.G.2
  • 38
    • 25444459642 scopus 로고    scopus 로고
    • Role of nadase in virulence in experimental invasive group a streptococcal infection
    • Bricker, A. L., Carey, V. J., and Wessels, M. R. (2005) Role of NADase in virulence in experimental invasive group A streptococcal infection. Infect. Immun. 73, 6562-6566
    • (2005) Infect. Immun. , vol.73 , pp. 6562-6566
    • Bricker A, L.1    Carey V, J.2    Wessels M, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.