메뉴 건너뛰기




Volumn 77, Issue 3, 2010, Pages 716-729

Guanosine 5′-diphosphate 3′-diphosphate (ppGpp) as a negative modulator of polynucleotide phosphorylase activity in a 'rare' actinomycete

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; MESSENGER RNA; NUCLEOSIDE DIPHOSPHATASE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; BACTERIAL PROTEIN;

EID: 77954837414     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2010.07240.x     Document Type: Article
Times cited : (23)

References (55)
  • 1
    • 27644460268 scopus 로고    scopus 로고
    • Expression in Streptomyces lividans of Nonomuraea genes cloned in an artificial chromosome
    • Alduina, R., Giardina, A., Gallo, G., Tenzone, G., Ferraro, C., Contino, A., et al. (2005) Expression in Streptomyces lividans of Nonomuraea genes cloned in an artificial chromosome. Appl Microbiol Biotechnol 68 : 656 662.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 656-662
    • Alduina, R.1    Giardina, A.2    Gallo, G.3    Tenzone, G.4    Ferraro, C.5    Contino, A.6
  • 2
    • 0028711703 scopus 로고
    • Control of mRNA processing and decay in prokaryotes
    • Alifano, P., Bruni, C.B. Carlomagno, M.S. (1994) Control of mRNA processing and decay in prokaryotes. Genetica 94 : 157 172.
    • (1994) Genetica , vol.94 , pp. 157-172
    • Alifano, P.1    Bruni, C.B.2    Carlomagno, M.S.3
  • 3
    • 40449098228 scopus 로고    scopus 로고
    • PNPase is a key player in the regulation of small RNAs that control the expression of outer membrane proteins
    • Andrade, J.M. Arraiano, C.M. (2008) PNPase is a key player in the regulation of small RNAs that control the expression of outer membrane proteins. RNA 14 : 543 551.
    • (2008) RNA , vol.14 , pp. 543-551
    • Andrade, J.M.1    Arraiano, C.M.2
  • 5
    • 33947377937 scopus 로고    scopus 로고
    • Role of mRNA stability in growth phase regulation of gene expression in the group A streptococcus
    • Barnett, T.C., Bugrysheva, J.V. Scott, J.R. (2007) Role of mRNA stability in growth phase regulation of gene expression in the group A streptococcus. J Bacteriol 189 : 1866 1873.
    • (2007) J Bacteriol , vol.189 , pp. 1866-1873
    • Barnett, T.C.1    Bugrysheva, J.V.2    Scott, J.R.3
  • 6
    • 0029945534 scopus 로고    scopus 로고
    • The regulation of antibiotic production in Streptomyces coelicolor A3(2)
    • Bibb, M. (1996) The regulation of antibiotic production in Streptomyces coelicolor A3(2). Microbiology 142 : 1335 1344.
    • (1996) Microbiology , vol.142 , pp. 1335-1344
    • Bibb, M.1
  • 7
    • 0036267108 scopus 로고    scopus 로고
    • CDNA cloning confirms the polyadenylation of RNA decay intermediates in Streptomyces coelicolor
    • Bralley, P. Jones, G.H. (2002) cDNA cloning confirms the polyadenylation of RNA decay intermediates in Streptomyces coelicolor. Microbiology 148 : 1421 1425.
    • (2002) Microbiology , vol.148 , pp. 1421-1425
    • Bralley, P.1    Jones, G.H.2
  • 8
    • 0041923884 scopus 로고    scopus 로고
    • Overexpression of the polynucleotide phosphorylase gene (pnp) of Streptomyces antibioticus affects mRNA stability and poly(A) tail length but not ppGpp levels
    • Bralley, P. Jones, G.H. (2003) Overexpression of the polynucleotide phosphorylase gene (pnp) of Streptomyces antibioticus affects mRNA stability and poly(A) tail length but not ppGpp levels. Microbiology 149 : 2173 2182.
    • (2003) Microbiology , vol.149 , pp. 2173-2182
    • Bralley, P.1    Jones, G.H.2
  • 9
    • 2342547758 scopus 로고    scopus 로고
    • Organization and expression of the polynucleotide phosphorylase gene (pnp) of Streptomyces: Processing of pnp transcripts in Streptomyces antibioticus
    • Bralley, P. Jones, G.H. (2004) Organization and expression of the polynucleotide phosphorylase gene (pnp) of Streptomyces: processing of pnp transcripts in Streptomyces antibioticus. J Bacteriol 186 : 3160 3172.
    • (2004) J Bacteriol , vol.186 , pp. 3160-3172
    • Bralley, P.1    Jones, G.H.2
  • 10
    • 0021128938 scopus 로고
    • Bacterial dry matter content and biomass estimations
    • Bratbak, G. Dundas, I. (1984) Bacterial dry matter content and biomass estimations. Appl Environ Microbiol 48 : 755 757.
    • (1984) Appl Environ Microbiol , vol.48 , pp. 755-757
    • Bratbak, G.1    Dundas, I.2
  • 12
    • 0026475908 scopus 로고
    • Identification of the gene for an Escherichia coli poly(A) polymerase
    • Cao, G.J. Sarkar, N. (1992) Identification of the gene for an Escherichia coli poly(A) polymerase. Proc Natl Acad Sci USA 89 : 10380 10384.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10380-10384
    • Cao, G.J.1    Sarkar, N.2
  • 13
    • 64949203863 scopus 로고    scopus 로고
    • Phenotypes and gene expression profiles of Saccharopolyspora erythraea rifampicin-resistant (rif) mutants affected in erythromycin production
    • Carata, E., Peano, C., Tredici, S.M., Ferrari, F., Talà, A., Corti, G., et al. (2009) Phenotypes and gene expression profiles of Saccharopolyspora erythraea rifampicin-resistant (rif) mutants affected in erythromycin production. Microb Cell Fact 8 : 18.
    • (2009) Microb Cell Fact , vol.8 , pp. 18
    • Carata, E.1    Peano, C.2    Tredici, S.M.3    Ferrari, F.4    Talà, A.5    Corti, G.6
  • 14
    • 0036549769 scopus 로고    scopus 로고
    • The Escherichia coli RNA degradosome: Structure, function, and relationship in other ribonucleolytic multienzyme complexes
    • Carpousis, A.J. (2002) The Escherichia coli RNA degradosome: structure, function, and relationship in other ribonucleolytic multienzyme complexes. Biochem Soc Trans 30 : 150 155.
    • (2002) Biochem Soc Trans , vol.30 , pp. 150-155
    • Carpousis, A.J.1
  • 15
    • 63049138147 scopus 로고    scopus 로고
    • Autogenous regulation of Escherichia coli polynucleotide phosphorylase revisited
    • Carzaniga, T., Briani, F., Zangrossi, S., Merlino, G., Marchi, P. Dehò, G. (2009) Autogenous regulation of Escherichia coli polynucleotide phosphorylase revisited. J Bacteriol 191 : 1738 1748.
    • (2009) J Bacteriol , vol.191 , pp. 1738-1748
    • Carzaniga, T.1    Briani, F.2    Zangrossi, S.3    Merlino, G.4    Marchi, P.5    Dehò, G.6
  • 17
    • 0030922782 scopus 로고    scopus 로고
    • The ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation
    • Chakraburtty, R. Bibb, M. (1997) The ppGpp synthetase gene (relA) of Streptomyces coelicolor A3(2) plays a conditional role in antibiotic production and morphological differentiation. J Bacteriol 179 : 5854 5861.
    • (1997) J Bacteriol , vol.179 , pp. 5854-5861
    • Chakraburtty, R.1    Bibb, M.2
  • 18
    • 0002099010 scopus 로고    scopus 로고
    • Actinomycete development, antibiotic production, and phylogeny: Questions and challenges
    • Brun, Y.V. Shimkets, L.J. (eds)
    • Champness, W. (2000) Actinomycete development, antibiotic production, and phylogeny: questions and challenges. In Prokaryotic Development. Brun, Y.V. Shimkets, L.J. (eds).
    • (2000) Prokaryotic Development.
    • Champness, W.1
  • 19
    • 25844517141 scopus 로고    scopus 로고
    • The absB gene encodes a double strand-specific endoribonuclease that cleaves the read-through transcript of the rpsO-pnp operon in Streptomyces coelicolor
    • Chang, S.A., Bralley, P. Jones, G.H. (2005) The absB gene encodes a double strand-specific endoribonuclease that cleaves the read-through transcript of the rpsO-pnp operon in Streptomyces coelicolor. J Biol Chem 280 : 33213 33219.
    • (2005) J Biol Chem , vol.280 , pp. 33213-33219
    • Chang, S.A.1    Bralley, P.2    Jones, G.H.3
  • 20
    • 37549012162 scopus 로고    scopus 로고
    • Kinetics of polynucleotide phosphorylase: Comparison of enzymes from Streptomyces and Escherichia coli and effects of nucleoside diphosphates
    • Chang, S.A., Cozad, M., Mackie, G.A. Jones, G.H. (2008) Kinetics of polynucleotide phosphorylase: comparison of enzymes from Streptomyces and Escherichia coli and effects of nucleoside diphosphates. J Bacteriol 190 : 98 106.
    • (2008) J Bacteriol , vol.190 , pp. 98-106
    • Chang, S.A.1    Cozad, M.2    MacKie, G.A.3    Jones, G.H.4
  • 21
    • 0037383031 scopus 로고    scopus 로고
    • Signalling early developmental events in two highly diverged Streptomyces species
    • Chater, K.F. Horinouchi, S. (2003) Signalling early developmental events in two highly diverged Streptomyces species. Mol Microbiol 48 : 9 15.
    • (2003) Mol Microbiol , vol.48 , pp. 9-15
    • Chater, K.F.1    Horinouchi, S.2
  • 22
    • 0028286232 scopus 로고
    • The gene coding for polynucleotide phosphorylase in Photorhabdus sp. strain K122 is induced at low temperatures
    • Clarke, D.J. Dowds, B.C. (1994) The gene coding for polynucleotide phosphorylase in Photorhabdus sp. strain K122 is induced at low temperatures. J Bacteriol 176 : 3775 3784.
    • (1994) J Bacteriol , vol.176 , pp. 3775-3784
    • Clarke, D.J.1    Dowds, B.C.2
  • 24
    • 33747179857 scopus 로고    scopus 로고
    • Structure and expression of the atp operon coding for F1F0-ATP synthase from the antibiotic-producing actinomycete Nonomuraea sp. ATCC
    • 39727
    • Gaballo, A., Abbrescia, A., Palese, L.L., Micelli, L., Summa, R., Alifano, P. Papa, S. (2006) Structure and expression of the atp operon coding for F1F0-ATP synthase from the antibiotic-producing actinomycete Nonomuraea sp. ATCC 39727. Res Microbiol 157 : 675 683.
    • (2006) Res Microbiol , vol.157 , pp. 675-683
    • Gaballo, A.1    Abbrescia, A.2    Palese, L.L.3    Micelli, L.4    Summa, R.5    Alifano, P.6    Papa, S.7
  • 26
    • 0030924592 scopus 로고    scopus 로고
    • A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease e of Escherichia coli
    • Hagège, J.M. Cohen, S.N. (1997) A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease E of Escherichia coli. Mol Microbiol 25 : 1077 1090.
    • (1997) Mol Microbiol , vol.25 , pp. 1077-1090
    • Hagège, J.M.1    Cohen, S.N.2
  • 27
    • 0028235826 scopus 로고
    • Roles of RNase E, RNase II and PNPase in the degradation of the rpsO transcripts of Escherichia coli: Stabilizing function of RNase II and evidence for efficient degradation in an ams pnp rnb mutant
    • Hajnsdorf, E., Steier, O., Coscoy, L., Teysset, L. Regnier, P. (1994) Roles of RNase E, RNase II and PNPase in the degradation of the rpsO transcripts of Escherichia coli: stabilizing function of RNase II and evidence for efficient degradation in an ams pnp rnb mutant. EMBO J 13 : 3368 3377.
    • (1994) EMBO J , vol.13 , pp. 3368-3377
    • Hajnsdorf, E.1    Steier, O.2    Coscoy, L.3    Teysset, L.4    Regnier, P.5
  • 28
    • 2442555334 scopus 로고    scopus 로고
    • RNase ES of Streptomyces coelicolor A3(2) can complement the rne and rng mutations in Escherichia coli
    • Inagawa, T., Okamoto, S., Wachi, M. Ochi, K. (2003) RNase ES of Streptomyces coelicolor A3(2) can complement the rne and rng mutations in Escherichia coli. Biosci Biotechnol Biochem 67 : 1767 1771.
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1767-1771
    • Inagawa, T.1    Okamoto, S.2    Wachi, M.3    Ochi, K.4
  • 29
    • 0035803559 scopus 로고    scopus 로고
    • PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader
    • Jarrige, A.C., Mathy, N. Portier, C. (2001) PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader. EMBO J 20 : 6845 6855.
    • (2001) EMBO J , vol.20 , pp. 6845-6855
    • Jarrige, A.C.1    Mathy, N.2    Portier, C.3
  • 30
    • 0029974966 scopus 로고    scopus 로고
    • Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase
    • Jones, G.H. Bibb, M.J. (1996) Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase. J Bacteriol 178 : 4281 4288.
    • (1996) J Bacteriol , vol.178 , pp. 4281-4288
    • Jones, G.H.1    Bibb, M.J.2
  • 31
    • 0346305936 scopus 로고    scopus 로고
    • Overexpression and purification of untagged polynucleotide phosphorylases
    • Jones, G.H., Symmons, M.F., Hankins, J.S. Mackie, G.A. (2003) Overexpression and purification of untagged polynucleotide phosphorylases. Protein Expr Purif 32 : 202 209.
    • (2003) Protein Expr Purif , vol.32 , pp. 202-209
    • Jones, G.H.1    Symmons, M.F.2    Hankins, J.S.3    MacKie, G.A.4
  • 32
    • 0030775035 scopus 로고    scopus 로고
    • Molecular analysis of the ribosomal L11 protein gene (rplK = relC) of Streptomyces griseus and identification of a deletion allele
    • Kawamoto, S., Zhang, D. Ochi, K. (1997) Molecular analysis of the ribosomal L11 protein gene (rplK = relC) of Streptomyces griseus and identification of a deletion allele. Mol Gen Genet 255 : 549 560.
    • (1997) Mol Gen Genet , vol.255 , pp. 549-560
    • Kawamoto, S.1    Zhang, D.2    Ochi, K.3
  • 33
    • 0038687705 scopus 로고    scopus 로고
    • A Streptomyces coelicolor functional orthologue of Escherichia coli RNase e shows shuffling of catalytic and PNPase-binding domains
    • Lee, K. Cohen, S.N. (2003) A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows shuffling of catalytic and PNPase-binding domains. Mol Microbiol 48 : 349 360.
    • (2003) Mol Microbiol , vol.48 , pp. 349-360
    • Lee, K.1    Cohen, S.N.2
  • 34
    • 17544367082 scopus 로고    scopus 로고
    • A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls antibiotic biosynthetic genes
    • Martínez-Costa, O.H., Arias, P., Romero, N.M., Parro, V., Mellado, R.P. Malpartida, F. (1996) A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls antibiotic biosynthetic genes. J Biol Chem 271 : 10627 10634.
    • (1996) J Biol Chem , vol.271 , pp. 10627-10634
    • Martínez-Costa, O.H.1    Arias, P.2    Romero, N.M.3    Parro, V.4    Mellado, R.P.5    Malpartida, F.6
  • 35
    • 0031829736 scopus 로고    scopus 로고
    • The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp-synthesizing and -degrading activities
    • Martínez-Costa, O.H., Fernández-Moreno, M.A. Malpartida, F. (1998) The relA/spoT-homologous gene in Streptomyces coelicolor encodes both ribosome-dependent (p)ppGpp-synthesizing and -degrading activities. J Bacteriol 180 : 4123 4132.
    • (1998) J Bacteriol , vol.180 , pp. 4123-4132
    • Martínez-Costa, O.H.1    Fernández-Moreno, M.A.2    Malpartida, F.3
  • 36
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Masse′, E., Escorcia, F.E. Gottesman, S. (2003) Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev 17 : 2374 2383.
    • (2003) Genes Dev , vol.17 , pp. 2374-2383
    • Masse, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 37
    • 33947614717 scopus 로고    scopus 로고
    • The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature
    • Matus-Ortega, M.E., Regonesi, M.E., Pina-Escobedo, A., Tortora, P., Dehò, G. García-Mena, J. (2007) The KH and S1 domains of Escherichia coli polynucleotide phosphorylase are necessary for autoregulation and growth at low temperature. Biochim Biophys Acta 1769 : 194 203.
    • (2007) Biochim Biophys Acta , vol.1769 , pp. 194-203
    • Matus-Ortega, M.E.1    Regonesi, M.E.2    Pina-Escobedo, A.3    Tortora, P.4    Dehò, G.5    García-Mena, J.6
  • 38
    • 33749021074 scopus 로고    scopus 로고
    • The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor
    • Milon, P., Tischenko, E., Tomsic, J., Caserta, E., Folkers, G., La Teana, A., et al. (2006) The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor. Proc Natl Acad Sci USA 103 : 13962 13967.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13962-13967
    • Milon, P.1    Tischenko, E.2    Tomsic, J.3    Caserta, E.4    Folkers, G.5    La Teana, A.6
  • 39
    • 24944507588 scopus 로고    scopus 로고
    • RNase E-based ribonucleoprotein complexes: Mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs
    • Morita, T., Maki, K. Aiba, H. (2005) RNase E-based ribonucleoprotein complexes: mechanical basis of mRNA destabilization mediated by bacterial noncoding RNAs. Genes Dev 19 : 2176 2186.
    • (2005) Genes Dev , vol.19 , pp. 2176-2186
    • Morita, T.1    Maki, K.2    Aiba, H.3
  • 40
    • 67349257830 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: Implications for catalytic mechanism and RNA degradosome assembly
    • Nurmohamed, S., Vaidialingam, B., Callaghan, A.J. Luisi, B.F. (2009) Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly. J Mol Biol 389 : 17 33.
    • (2009) J Mol Biol , vol.389 , pp. 17-33
    • Nurmohamed, S.1    Vaidialingam, B.2    Callaghan, A.J.3    Luisi, B.F.4
  • 41
    • 0030784850 scopus 로고    scopus 로고
    • Molecular and functional analysis of the ribosomal L11 and S12 protein genes (rplK and rpsL) of Streptomyces coelicolor A3(2)
    • Ochi, K., Zhang, D., Kawamoto, S. Hesketh, A. (1997) Molecular and functional analysis of the ribosomal L11 and S12 protein genes (rplK and rpsL) of Streptomyces coelicolor A3(2). Mol Gen Genet 256 : 488 498.
    • (1997) Mol Gen Genet , vol.256 , pp. 488-498
    • Ochi, K.1    Zhang, D.2    Kawamoto, S.3    Hesketh, A.4
  • 42
    • 0021112086 scopus 로고
    • Organization of the Escherichia coli chromosome around the genes for translation initiation factor IF2 (infB) and a transcription termination factor (nusA)
    • Plumbridge, J.A. Springer, M. (1983) Organization of the Escherichia coli chromosome around the genes for translation initiation factor IF2 (infB) and a transcription termination factor (nusA). J Mol Biol 167 : 227 243.
    • (1983) J Mol Biol , vol.167 , pp. 227-243
    • Plumbridge, J.A.1    Springer, M.2
  • 43
    • 0021759579 scopus 로고
    • Expression of the rpsO and pnp genes: Structural analysis of a DNA fragment carrying their control regions
    • Portier, C. Regnier, P. (1984) Expression of the rpsO and pnp genes: structural analysis of a DNA fragment carrying their control regions. Nucleic Acids Res 12 : 6091 6102.
    • (1984) Nucleic Acids Res , vol.12 , pp. 6091-6102
    • Portier, C.1    Regnier, P.2
  • 44
    • 9644284618 scopus 로고    scopus 로고
    • Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: Evidence for a 'cold shock degradosome'
    • Prud'homme-Genereux, A., Beran, R.K., Iost, I., Ramey, C.S., Mackie, G.A. Simons, R.W. (2004) Physical and functional interactions among RNase E, polynucleotide phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock degradosome'. Mol Microbiol 54 : 1409 1421.
    • (2004) Mol Microbiol , vol.54 , pp. 1409-1421
    • Prud'Homme-Genereux, A.1    Beran, R.K.2    Iost, I.3    Ramey, C.S.4    MacKie, G.A.5    Simons, R.W.6
  • 45
    • 0025649204 scopus 로고
    • RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression
    • Regnier, P. Grunberg-Manago, M. (1990) RNase III cleavages in non-coding leaders of Escherichia coli transcripts control mRNA stability and genetic expression. Biochimie 72 : 825 834.
    • (1990) Biochimie , vol.72 , pp. 825-834
    • Regnier, P.1    Grunberg-Manago, M.2
  • 46
    • 0025973574 scopus 로고
    • Decay of mRNA encoding ribosomal protein S15 of Escherichia coli is initiated by an RNase E-dependent endonucleolytic cleavage that removes the 3′ stabilizing stem and loop structure
    • Regnier, P. Hajnsdorf, E. (1991) Decay of mRNA encoding ribosomal protein S15 of Escherichia coli is initiated by an RNase E-dependent endonucleolytic cleavage that removes the 3′ stabilizing stem and loop structure. J Mol Biol 217 : 283 292.
    • (1991) J Mol Biol , vol.217 , pp. 283-292
    • Regnier, P.1    Hajnsdorf, E.2
  • 47
    • 0023041808 scopus 로고
    • Initiation, attenuation and RNase III processing of transcripts from the Escherichia coli operon encoding ribosomal protein S15 and polynucleotide phosphorylase
    • Regnier, P. Portier, C. (1986) Initiation, attenuation and RNase III processing of transcripts from the Escherichia coli operon encoding ribosomal protein S15 and polynucleotide phosphorylase. J Mol Biol 187 : 23 32.
    • (1986) J Mol Biol , vol.187 , pp. 23-32
    • Regnier, P.1    Portier, C.2
  • 48
    • 0028358101 scopus 로고
    • Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation
    • Robert-Le Meur, M. Portier, C. (1994) Polynucleotide phosphorylase of Escherichia coli induces the degradation of its RNase III processed messenger by preventing its translation. Nucleic Acids Res 22 : 397 403.
    • (1994) Nucleic Acids Res , vol.22 , pp. 397-403
    • Robert-Le Meur, M.1    Portier, C.2
  • 50
    • 0038167479 scopus 로고    scopus 로고
    • The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species
    • Sosio, M., Stinchi, S., Beltrametti, F., Lazzarini, A. Donadio, S. (2003) The gene cluster for the biosynthesis of the glycopeptide antibiotic A40926 by Nonomuraea species. Chem Biol 10 : 541 549.
    • (2003) Chem Biol , vol.10 , pp. 541-549
    • Sosio, M.1    Stinchi, S.2    Beltrametti, F.3    Lazzarini, A.4    Donadio, S.5
  • 51
    • 0001978432 scopus 로고
    • The stringent response, ppGpp and antibiotic production in Streptomyces coelicolor A3(2)
    • Takano, E. Bibb, M.J. (1994) The stringent response, ppGpp and antibiotic production in Streptomyces coelicolor A3(2). Actinomycetology 8 : 1 10.
    • (1994) Actinomycetology , vol.8 , pp. 1-10
    • Takano, E.1    Bibb, M.J.2
  • 52
    • 0022432451 scopus 로고
    • Attenuation and processing of RNA from the rpsO-pnp transcription unit of Escherichia coli
    • Takata, R., Mukai, T. Hori, K. (1985) Attenuation and processing of RNA from the rpsO-pnp transcription unit of Escherichia coli. Nucleic Acids Res 13 : 7289 7297.
    • (1985) Nucleic Acids Res , vol.13 , pp. 7289-7297
    • Takata, R.1    Mukai, T.2    Hori, K.3
  • 53
    • 63449126395 scopus 로고    scopus 로고
    • Activation of dormant bacterial genes by Nonomuraea sp. strain ATCC
    • 39727 mutant-type RNA polymerase
    • Talà, A., Wang, G., Zemanova, M., Okamoto, S., Ochi, K. Alifano, P. (2009) Activation of dormant bacterial genes by Nonomuraea sp. strain ATCC 39727 mutant-type RNA polymerase. J Bacteriol 191 : 805 814.
    • (2009) J Bacteriol , vol.191 , pp. 805-814
    • Talà, A.1    Wang, G.2    Zemanova, M.3    Okamoto, S.4    Ochi, K.5    Alifano, P.6
  • 54
    • 8644221215 scopus 로고    scopus 로고
    • Design of mineral medium for growth of Actinomadura sp. ATCC
    • 39727, producer of the glycopeptide A40926: effects of calcium ions and nitrogen sources
    • Technikova-Dobrova, Z., Damiano, F., Tredici, S.M., Vigliotta, G., di Summa, R., Palese, L., et al. (2004) Design of mineral medium for growth of Actinomadura sp. ATCC 39727, producer of the glycopeptide A40926: effects of calcium ions and nitrogen sources. Appl Microbiol Biotechnol 65 : 671 677.
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 671-677
    • Technikova-Dobrova, Z.1    Damiano, F.2    Tredici, S.M.3    Vigliotta, G.4    Di Summa, R.5    Palese, L.6
  • 55
    • 13144260672 scopus 로고    scopus 로고
    • Natural merodiploidy involving duplicated rpoB alleles affects secondary metabolism in a producer actinomycete
    • Vigliotta, G., Tredici, S.M., Damiano, F., Montinaro, M.R., Pulimeno, R., Summa, R., et al. (2005) Natural merodiploidy involving duplicated rpoB alleles affects secondary metabolism in a producer actinomycete. Mol Microbiol 55 : 396 412.
    • (2005) Mol Microbiol , vol.55 , pp. 396-412
    • Vigliotta, G.1    Tredici, S.M.2    Damiano, F.3    Montinaro, M.R.4    Pulimeno, R.5    Summa, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.