메뉴 건너뛰기




Volumn 47, Issue 5, 2009, Pages 549-556

Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor m145

Author keywords

2D PAGE; MALDI TOF; Protein ADP ribosylation; S. coelicolor

Indexed keywords

STREPTOMYCES; STREPTOMYCES COELICOLOR;

EID: 71049184750     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-009-0032-y     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0032520234 scopus 로고    scopus 로고
    • The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme 1.5 A resolution
    • Allaire, M., R.E. MacKenzie, and M. Cygler. 1998. The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme 1.5 A resolution. Structure 6, 173-182.
    • (1998) Structure , vol.6 , pp. 173-182
    • Allaire, M.1    MacKenzie, R.E.2    Cygler, M.3
  • 2
    • 0033895238 scopus 로고    scopus 로고
    • Phosphate starvation-inducible proteins of Bacillus subtilis: Proteomics and transcriptional analysis
    • Antelmann, H., C. Scharf, and M. Hecker. 2000. Phosphate starvation-inducible proteins of Bacillus subtilis: Proteomics and transcriptional analysis. J. Bacteriol. 182, 4478-4490.
    • (2000) J. Bacteriol. , vol.182 , pp. 4478-4490
    • Antelmann, H.1    Scharf, C.2    Hecker, M.3
  • 3
    • 0026605465 scopus 로고
    • Coupling of m-aminophenyboronic acid to S-triazine-activated Sephacryl: Use in the affinity chromatography of glycated hemoglobins
    • Bisse, E. and H. Wieland. 1992. Coupling of m-aminophenyboronic acid to S-triazine-activated Sephacryl: Use in the affinity chromatography of glycated hemoglobins. J. Chromatogr. 575, 223-228.
    • (1992) J. Chromatogr. , vol.575 , pp. 223-228
    • Bisse, E.1    Wieland, H.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0026495323 scopus 로고
    • Functional modifications of transducin induced by cholera or pertussis-toxin-catalyzed ADP-ribosylation
    • Bornancin, F., M. Franco, J. Bigay, and M. Chabre. 1992. Functional modifications of transducin induced by cholera or pertussis-toxin-catalyzed ADP-ribosylation. Eur. J. Biochem. 210, 33-44.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 33-44
    • Bornancin, F.1    Franco, M.2    Bigay, J.3    Chabre, M.4
  • 6
    • 0027384770 scopus 로고
    • Genetics of differentiation in Streptomyces
    • Chater, K.F. 1993. Genetics of differentiation in Streptomyces. Annu. Rev. Microbiol. 47, 685-713.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 685-713
    • Chater, K.F.1
  • 7
    • 33746865723 scopus 로고    scopus 로고
    • Streptomyces inside out: A new perspective on the bacteria that provide us with antibiotics
    • Chater, K.F. 2006. Streptomyces inside out: A new perspective on the bacteria that provide us with antibiotics. Philos. Trans R. Soc. Lond. B Biol. Sci. 361, 761-768.
    • (2006) Philos. Trans R. Soc. Lond. B Biol. Sci. , vol.361 , pp. 761-768
    • Chater, K.F.1
  • 8
    • 0002838747 scopus 로고    scopus 로고
    • Mycelial life style of Streptomyces coelicolor A3(2) and its relatives
    • J. A. Shapiro and M. Dworkin (Eds.), London, UK: Oxford University Press
    • Chater, K.F. and R. Losick. 1997. Mycelial life style of Streptomyces coelicolor A3(2) and its relatives, p. 149-182. In J.A. Shapiro and M. Dworkin (eds.), Bacteria as multicellular organisms. Oxford University Press, London, UK.
    • (1997) Bacteria as Multicellular Organisms , pp. 149-182
    • Chater, K.F.1    Losick, R.2
  • 9
    • 0025959819 scopus 로고
    • Computer modelling of the NAD binding site of ADP-ribosylating toxins: Active-site structure and mechanism of NAD binding
    • Domenghini, M., C. Montecucco, W.C. Ripke, and R. Rappuoli. 1991. Computer modelling of the NAD binding site of ADP-ribosylating toxins: Active-site structure and mechanism of NAD binding. Mol. Microbiol. 5, 23-31.
    • (1991) Mol. Microbiol. , vol.5 , pp. 23-31
    • Domenghini, M.1    Montecucco, C.2    Ripke, W.C.3    Rappuoli, R.4
  • 11
    • 0030894501 scopus 로고    scopus 로고
    • A novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase
    • Haar, v.d.B., S. Walter, S. Schwapenheer, and H. Schrempf. 1997. A novel fusidic acid resistance gene from Streptomyces lividans 66 encodes a highly specific esterase. Microbiology 143, 867-874.
    • (1997) Microbiology , vol.143 , pp. 867-874
    • Haar, V.D.B.1    Walter, S.2    Schwapenheer, S.3    Schrempf, H.4
  • 12
    • 0034108232 scopus 로고    scopus 로고
    • Regulation of biological nitrogen fixation
    • Halbleib, C.M. and P.W. Ludden. 2000. Regulation of biological nitrogen fixation. J. Nutrition 130, 1081-1084.
    • (2000) J. Nutrition , vol.130 , pp. 1081-1084
    • Halbleib, C.M.1    Ludden, P.W.2
  • 15
    • 0036430005 scopus 로고    scopus 로고
    • The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria
    • Hesketh, A.R., D. Fink, B. Gust, H.U. Rexer, B. Scheel, K.F. Chater, W. Wohlleben, and A. Engels. 2002. The GlnD and GlnK homologues of Streptomyces coelicolor A3(2) are functionally dissimilar to their nitrogen regulatory system counterparts from enteric bacteria. Mol. Microbiol. 46, 319-330.
    • (2002) Mol. Microbiol. , vol.46 , pp. 319-330
    • Hesketh, A.R.1    Fink, D.2    Gust, B.3    Rexer, H.U.4    Scheel, B.5    Chater, K.F.6    Wohlleben, W.7    Engels, A.8
  • 16
    • 0028030535 scopus 로고
    • Sensing starvation: A homoserine lactone-dependent signaling pathway in Escherichia coli
    • Huisman, G.W. and R. Kolter. 1994. Sensing starvation: A homoserine lactone-dependent signaling pathway in Escherichia coli. Science 265, 537-539.
    • (1994) Science , vol.265 , pp. 537-539
    • Huisman, G.W.1    Kolter, R.2
  • 17
    • 0036306304 scopus 로고    scopus 로고
    • RelA protein is involved in induction of genetic competence in certain Bacillus subtilis strains by moderating the level of intracellular GTP
    • Inaoka, T. and K. Ochi. 2002. RelA protein is involved in induction of genetic competence in certain Bacillus subtilis strains by moderating the level of intracellular GTP. J. Bacteriol. 184, 3923-3930.
    • (2002) J. Bacteriol. , vol.184 , pp. 3923-3930
    • Inaoka, T.1    Ochi, K.2
  • 18
    • 0026860357 scopus 로고
    • Identification of basic nuclear proteins by their boronate complex
    • Jobst, K., A. Lakatos, and A. Horváth. 1992. Identification of basic nuclear proteins by their boronate complex. Biotech. Histochem. 67, 158-160.
    • (1992) Biotech. Histochem. , vol.67 , pp. 158-160
    • Jobst, K.1    Lakatos, A.2    Horváth, A.3
  • 19
    • 0028925010 scopus 로고
    • ADP-ribosylation of Rhizobium meliloti glutamine synthetase III in vivo
    • Liu, Y. and M.L. Kahn. 1995. ADP-ribosylation of Rhizobium meliloti glutamine synthetase III in vivo. J. Biol. Chem. 270, 1624-1628.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1624-1628
    • Liu, Y.1    Kahn, M.L.2
  • 21
    • 0027986527 scopus 로고
    • Reversible ADP-ribosylation as a mechanism of enzyme regulation in prokaryotes
    • Ludden, P.W. 1994. Reversible ADP-ribosylation as a mechanism of enzyme regulation in prokaryotes. Mol. Cell. Biochem. 138, 123-129.
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 123-129
    • Ludden, P.W.1
  • 22
    • 0031047960 scopus 로고    scopus 로고
    • Bacterial glycoproteins
    • Messner, P. 1997. Bacterial glycoproteins. Glycoconjugate J. 14, 3-11.
    • (1997) Glycoconjugate J , vol.14 , pp. 3-11
    • Messner, P.1
  • 23
    • 0023626550 scopus 로고
    • Metabolic initiation of differentiation and secondary metabolism by Streptomyces griseus: Significance of the stringent response (ppGpp) and GTP content in relation to A-factor
    • Ochi, K. 1987. Metabolic initiation of differentiation and secondary metabolism by Streptomyces griseus: Significance of the stringent response (ppGpp) and GTP content in relation to A-factor. J. Bacteriol. 169, 3608-3616.
    • (1987) J. Bacteriol. , vol.169 , pp. 3608-3616
    • Ochi, K.1
  • 24
    • 77956924601 scopus 로고
    • Mechanism of NAD-dependent enzymes
    • D. S. Sigman (Ed.), San Diego, USA: Academic Press
    • Oppenheimer, N.J. and A.L. Handlon. 1992. Mechanism of NAD-dependent enzymes, p. 453-505. In D.S. Sigman (ed.) The enzymes. Vol. XX. Academic Press, San Diego, USA.
    • (1992) The Enzymes , vol.XX , pp. 453-505
    • Oppenheimer, N.J.1    Handlon, A.L.2
  • 25
    • 0025290963 scopus 로고
    • ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1
    • Penyige, A., G. Barabás, I. Szabó, and J.C. Ensign. 1990. ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1. FEMS Microbiol. Lett. 57, 293-297.
    • (1990) FEMS Microbiol. Lett. , vol.57 , pp. 293-297
    • Penyige, A.1    Barabás, G.2    Szabó, I.3    Ensign, J.C.4
  • 27
    • 0029820402 scopus 로고    scopus 로고
    • + -glycohydrolase and ADP-ribosyltransferase in growth and differentiation of Streptomyces griseus NRRL B-2682: Inhibition by m-aminophenylboronic acid
    • + -glycohydrolase and ADP-ribosyltransferase in growth and differentiation of Streptomyces griseus NRRL B-2682: Inhibition by m-aminophenylboronic acid. Microbiology 142, 1937-1944.
    • (1996) Microbiology , vol.142 , pp. 1937-1944
    • Penyige, A.1    Deák, E.2    Kálmánczhelyi, A.3    Barabás, G.4
  • 29
    • 0023642638 scopus 로고
    • Effect of bacteriophage M13 infection on phosphorylation of dnaK protein and other Escherichia coli proteins
    • Rieul, C., J.C. Corta, F. Bleicher, and A.J. Cozzone. 1987. Effect of bacteriophage M13 infection on phosphorylation of dnaK protein and other Escherichia coli proteins. Eur. J. Biochem. 168, 621-627.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 621-627
    • Rieul, C.1    Corta, J.C.2    Bleicher, F.3    Cozzone, A.J.4
  • 30
    • 0030600466 scopus 로고    scopus 로고
    • Characterization of spaA a Streptomyces coelicolor gene homologous to a gene involved in sensing starvation in Escherichia coli
    • Schneider, D. and K.F. Chater. 1996. Characterization of spaA a Streptomyces coelicolor gene homologous to a gene involved in sensing starvation in Escherichia coli. Gene 177, 243-251.
    • (1996) Gene , vol.177 , pp. 243-251
    • Schneider, D.1    Chater, K.F.2
  • 31
    • 0029884413 scopus 로고    scopus 로고
    • Changes in patterns of ADP-ribosylated proteins during differentiation of Streptomyces coelicolor A3(2) and its developmental mutants
    • Shima, J., A. Penyige, and K. Ochi. 1996. Changes in patterns of ADP-ribosylated proteins during differentiation of Streptomyces coelicolor A3(2) and its developmental mutants. J. Bacteriol. 178, 3785-3790.
    • (1996) J. Bacteriol. , vol.178 , pp. 3785-3790
    • Shima, J.1    Penyige, A.2    Ochi, K.3
  • 32
    • 0029008677 scopus 로고
    • ADP-ribosylation of glutamine synthetase in the cyanobacterium Synechocystis strain PCC6803
    • Silmann, N.J., N.G. Carr, and N.H. Mann. 1995. ADP-ribosylation of glutamine synthetase in the cyanobacterium Synechocystis strain PCC6803. J. Bacteriol. 177, 3527-3533.
    • (1995) J. Bacteriol. , vol.177 , pp. 3527-3533
    • Silmann, N.J.1    Carr, N.G.2    Mann, N.H.3
  • 35
    • 0033027546 scopus 로고    scopus 로고
    • ADP-ribosylation of oncogenic Ras proteins by Pseudomonas aeruginosa exoenzyme S in vivo
    • Vincent, T.J., J.E. Fraylick, E.M. McGuffie, and J.C. Olson. 1999. ADP-ribosylation of oncogenic Ras proteins by Pseudomonas aeruginosa exoenzyme S in vivo. Mol. Microbiol. 32, 1054-1064.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1054-1064
    • Vincent, T.J.1    Fraylick, J.E.2    McGuffie, E.M.3    Olson, J.C.4
  • 36
    • 0025045391 scopus 로고
    • ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro
    • Woehle, D.L., B.A. Lueddecke, and P.W. Ludden. 1990. ATP-dependent and NAD-dependent modification of glutamine synthetase from Rhodospirillum rubrum in vitro. J. Biol. Chem. 23, 13741-13749.
    • (1990) J. Biol. Chem. , vol.23 , pp. 13741-13749
    • Woehle, D.L.1    Lueddecke, B.A.2    Ludden, P.W.3
  • 37
    • 0036062314 scopus 로고    scopus 로고
    • + -induced nitrogenase switch-off and ADP-ribosylation in Rhodobacter capsulatus
    • + -induced nitrogenase switch-off and ADP-ribosylation in Rhodobacter capsulatus. J. Bacteriol. 184, 4081-4088.
    • (2002) J. Bacteriol. , vol.184 , pp. 4081-4088
    • Yakunin, A.F.1    Hallenbeck, P.C.2
  • 38
    • 28844507784 scopus 로고    scopus 로고
    • Effects of spontaneous deamidation on the cytotoxic activity of the Bacillus anthracis protective antigen
    • Zomber, G., S. Reuveny, N. Garti, A. Shafferman, and E. Elhanany. 2005. Effects of spontaneous deamidation on the cytotoxic activity of the Bacillus anthracis protective antigen. J. Biol. Chem. 280, 39897-39906.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39897-39906
    • Zomber, G.1    Reuveny, S.2    Garti, N.3    Shafferman, A.4    Elhanany, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.