메뉴 건너뛰기




Volumn 50, Issue 3, 2012, Pages 409-418

Disruption of SCO5461 gene coding for a mono-ADP-ribosyltransferase enzyme produces a conditional pleiotropic phenotype affecting morphological differentiation and antibiotic production in Streptomyces coelicolor

Author keywords

actinorhodin production and secretion; mono ADP ribosyltransferase; morphological differentiation; protein ADP ribosylation; Streptomyces

Indexed keywords

STREPTOMYCES; STREPTOMYCES COELICOLOR;

EID: 84863300262     PISSN: 12258873     EISSN: 19763794     Source Type: Journal    
DOI: 10.1007/s12275-012-1440-y     Document Type: Article
Times cited : (9)

References (34)
  • 3
    • 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
  • 4
    • 0002838747 scopus 로고    scopus 로고
    • Mycelial life style of Streptomyces coelicolor A3(2) and its relatives
    • London, UK: Oxford University Press
    • Chater, K. F. and Losick, R. 1997. Mycelial life style of Streptomyces coelicolor A3(2) and its relatives, pp. 149-182. In Shapiro, J. A. and Dworkin, M. (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    Shapiro, J.A.3    Dworkin, M.4
  • 5
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating 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 ADP-ribosylating 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
  • 6
    • 0028116726 scopus 로고
    • Endogenous ADP-ribosylation during development of the prokaryote Myxococcus xanthus
    • Eastman, D. and Dworkin, M. 1994. Endogenous ADP-ribosylation during development of the prokaryote Myxococcus xanthus. Microbiology-UK140, 3167-3176.
    • (1994) Microbiology-UK , vol.140 , pp. 3167-3176
    • Eastman, D.1    Dworkin, M.2
  • 7
    • 0025899144 scopus 로고
    • The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of streptomyces
    • Fernández-Moreno, M. A., Caballero, J. L., Hopwood, D. A., and Malpartida, F. 1991. The act cluster contains regulatory and antibiotic export genes, direct targets for translational control by the bldA tRNA gene of streptomyces. Cell66, 769-780.
    • (1991) Cell , vol.66 , pp. 769-780
    • Fernández-Moreno, M.A.1    Caballero, J.L.2    Hopwood, D.A.3    Malpartida, F.4
  • 8
    • 55549086417 scopus 로고    scopus 로고
    • Streptomyces morphogenetics: Dissecting differentiation in a filamentous bacterium
    • Flärdh, K. and Buttner, M. J. 2009. Streptomyces morphogenetics: Dissecting differentiation in a filamentous bacterium. Nat. Rev. Microbiol. 7, 36-49.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 36-49
    • Flärdh, K.1    Buttner, M.J.2
  • 9
    • 0030137024 scopus 로고    scopus 로고
    • ADP-ribosylation of an approximately 70-kilodalton protein of Klebsiella pneumoniae
    • Geipel, U., Just, I., and Aktories, K. 1996. ADP-ribosylation of an approximately 70-kilodalton protein of Klebsiella pneumoniae. Infect. Immun. 64, 1720-1723.
    • (1996) Infect. Immun. , vol.64 , pp. 1720-1723
    • Geipel, U.1    Just, I.2    Aktories, K.3
  • 10
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • Gust, B., Challis, G. L., Fowler, K., Kieser, T., and Chater, K. F. 2003. PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin. Proc. Natl. Acad. Sci. USA100, 1541-1546.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 11
    • 0036196923 scopus 로고    scopus 로고
    • The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases
    • Han, S. and Tainer, J. A. 2002. The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases. Int. J. Med. Microbiol. 291, 523-529.
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 523-529
    • Han, S.1    Tainer, J.A.2
  • 12
    • 33749387471 scopus 로고    scopus 로고
    • A family of killer toxins - Exploring the mechanism of ADP-ribosylating toxins
    • Holbourn, K. P., Shone, C. C., and Acharya, K. R. 2006. A family of killer toxins - Exploring the mechanism of ADP-ribosylating toxins. FEBS J. 273, 4579-4593.
    • (2006) FEBS J. , vol.273 , pp. 4579-4593
    • Holbourn, K.P.1    Shone, C.C.2    Acharya, K.R.3
  • 13
    • 0029767410 scopus 로고    scopus 로고
    • ADP-ribosylation of proteins in Bacillus subtilis and its possible importance in sporulation
    • Huh, J. W., Shima, J., and Ochi, K. 1996. ADP-ribosylation of proteins in Bacillus subtilis and its possible importance in sporulation. J. Bacteriol. 178, 4935-4941.
    • (1996) J. Bacteriol. , vol.178 , pp. 4935-4941
    • Huh, J.W.1    Shima, J.2    Ochi, K.3
  • 14
    • 0001515028 scopus 로고
    • ADP-ribosylation of dinitrogenase reductase in Rhodobacter capsulatus
    • Jouanneau, Y., Roby, C., Meyer, C. M., and Vignais, P. M. 1989. ADP-ribosylation of dinitrogenase reductase in Rhodobacter capsulatus. Biochem. 28, 6524-6530.
    • (1989) Biochem. , vol.28 , pp. 6524-6530
    • Jouanneau, Y.1    Roby, C.2    Meyer, C.M.3    Vignais, P.M.4
  • 16
    • 22144492215 scopus 로고    scopus 로고
    • Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins
    • Li, H., Jacques, P. E., Ghinet, M. G., Brzezinski, R., and Morosoli, R. 2005. Determining the functionality of putative Tat-dependent signal peptides in Streptomyces coelicolor A3(2) by using two different reporter proteins. Microbiology-UK151, 2189-2198.
    • (2005) Microbiology-UK , vol.151 , pp. 2189-2198
    • Li, H.1    Jacques, P.E.2    Ghinet, M.G.3    Brzezinski, R.4    Morosoli, R.5
  • 17
    • 0001093249 scopus 로고
    • Endogenous ADP-ribosylation in prokaryotes
    • Washington, D.C., USA: American Society for Microbiology
    • Lowery, R. G. and Ludden, P. W. 1990. Endogenous ADP-ribosylation in prokaryotes, pp. 459-468. In Moss, J. and Vaughan, M. (eds.), ADP-ribosylating toxins and G-proteins. American Society for Microbiology, Washington, D. C., USA.
    • (1990) ADP-Ribosylating Toxins and G-Proteins , pp. 459-468
    • Lowery, R.G.1    Ludden, P.W.2    Moss, J.3    Vaughan, M.4
  • 18
    • 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
  • 19
    • 0034029903 scopus 로고    scopus 로고
    • Characterization of the enzymatic component of Clostridium perfringens iota-toxin
    • Nagahama, M., Sakaguchi, Y., Kobayashi, K., Ochi, S., and Sakurai, J. 2000. Characterization of the enzymatic component of Clostridium perfringens iota-toxin. J. Bacteriol. 182, 2096-2103.
    • (2000) J. Bacteriol. , vol.182 , pp. 2096-2103
    • Nagahama, M.1    Sakaguchi, Y.2    Kobayashi, K.3    Ochi, S.4    Sakurai, J.5
  • 20
    • 0026746388 scopus 로고
    • The possible role of ADP-ribosylation in sporulation and streptomycin production by Streptomyces griseus
    • Ochi, K., Penyige, A., and Barabás, G. 1992. The possible role of ADP-ribosylation in sporulation and streptomycin production by Streptomyces griseus. J. Gen. Microbiol. 138, 1745-1750.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1745-1750
    • Ochi, K.1    Penyige, A.2    Barabás, G.3
  • 21
    • 0029820402 scopus 로고    scopus 로고
    • Evidence of a role for NAD(+)-glycohydrolase and ADP-ribosyltransferase in growth and differentiation of Streptomyces griseus NRRL B-2682: Inhibition by m-aminophenylboronic acid
    • Penyige, A., Deák, E., Kálmánczhelyi, A., and Barabás, G. 1996. Evidence of a role for NAD(+)-glycohydrolase and ADP-ribosyltransferase in growth and differentiation of Streptomyces griseus NRRL B-2682: Inhibition by m-aminophenylboronic acid. Microbiology-UK142, 1937-1944.
    • (1996) Microbiology-UK , vol.142 , pp. 1937-1944
    • Penyige, A.1    Deák, E.2    Kálmánczhelyi, A.3    Barabás, G.4
  • 22
    • 71049184750 scopus 로고    scopus 로고
    • Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145
    • Penyige, A., Keseru{double acute}, J., Fazakas, F., Schmelczer, I., Szirák, K., Barabás, G., and Biró, S. 2009. Analysis and identification of ADP-ribosylated proteins of Streptomyces coelicolor M145. J. Microbiol. 47, 549-556.
    • (2009) J. Microbiol. , vol.47 , pp. 549-556
    • Penyige, A.1    Keseru, J.2    Fazakas, F.3    Schmelczer, I.4    Szirák, K.5    Barabás, G.6    Biró, S.7
  • 23
    • 33644825968 scopus 로고    scopus 로고
    • Structure of the mosquitocidal toxin from Bacillus sphaericus
    • Reinert, D. J., Carpusca, I., Aktories, K., and Schulz, G. E. 2006. Structure of the mosquitocidal toxin from Bacillus sphaericus. J. Mol. Biol. 357, 1226-1236.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1226-1236
    • Reinert, D.J.1    Carpusca, I.2    Aktories, K.3    Schulz, G.E.4
  • 24
    • 0042324506 scopus 로고    scopus 로고
    • Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2.2 from rat
    • Ritter, H., Koch-Nolte, F., Marquez, V. E., and Schulz, G. E. 2003. Substrate binding and catalysis of ecto-ADP-ribosyltransferase 2. 2 from rat. Biochemistry42, 10155-10162.
    • (2003) Biochemistry , vol.42 , pp. 10155-10162
    • Ritter, H.1    Koch-Nolte, F.2    Marquez, V.E.3    Schulz, G.E.4
  • 26
    • 0029846964 scopus 로고    scopus 로고
    • Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis
    • Serres, M. H. and Ensign, J. C. 1996. Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis. J. Bacteriol. 178, 6074-6077.
    • (1996) J. Bacteriol. , vol.178 , pp. 6074-6077
    • Serres, M.H.1    Ensign, J.C.2
  • 27
    • 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., Penyige, A., and Ochi, K. 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
  • 28
    • 18844427294 scopus 로고    scopus 로고
    • Sec-dependent protein translocation across biological membranes: Evolutionary conservation of an essential protein transport pathway
    • Stephenson, K. 2005. Sec-dependent protein translocation across biological membranes: Evolutionary conservation of an essential protein transport pathway. Mol. Membr. Biol. 22, 17-28.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 17-28
    • Stephenson, K.1
  • 31
    • 0024419124 scopus 로고
    • Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus)
    • Vara, J., Lewandowska-Skarbek, M., Wang, Y. G., Donadio, S., and Hutchinson, C. R. 1989. Cloning of genes governing the deoxysugar portion of the erythromycin biosynthesis pathway in Saccharopolyspora erythraea (Streptomyces erythreus). J. Bacteriol. 171, 5872-5881.
    • (1989) J. Bacteriol. , vol.171 , pp. 5872-5881
    • Vara, J.1    Lewandowska-Skarbek, M.2    Wang, Y.G.3    Donadio, S.4    Hutchinson, C.R.5
  • 32
    • 2442666308 scopus 로고    scopus 로고
    • Enzymatic properties of pierisin-1 and its N-terminal domain, a guanine-specific ADP-ribosyltransferase from the cabbage butterfly
    • Watanabe, M., Enomoto, S., Takamura-Enya, T., Nakano, T., Koyama, K., Sugimura, T., and Wakabayashi, K. 2004. Enzymatic properties of pierisin-1 and its N-terminal domain, a guanine-specific ADP-ribosyltransferase from the cabbage butterfly. J. Biochem. 135, 471-477.
    • (2004) J. Biochem. , vol.135 , pp. 471-477
    • Watanabe, M.1    Enomoto, S.2    Takamura-Enya, T.3    Nakano, T.4    Koyama, K.5    Sugimura, T.6    Wakabayashi, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.