메뉴 건너뛰기




Volumn 13, Issue 5, 2014, Pages 1219-1230

Temporal dynamics of the saccharopolyspora erythraea phosphoproteome

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; ISOCITRATE LYASE; OXOGLUTARATE DEHYDROGENASE; PHOSPHOPEPTIDE; RIBONUCLEASE; RIBOSOME PROTEIN; SERINE PROTEINASE; TITANIUM DIOXIDE; TRYPSIN LIKE SERINE PROTEASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; PROTEOME;

EID: 84899742652     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.033951     Document Type: Article
Times cited : (23)

References (65)
  • 1
    • 77953292595 scopus 로고    scopus 로고
    • Post-translational modifications in signal integration
    • Deribe, Y. L., Pawson, T., and Dikic, I. (2010) Post-translational modifications in signal integration. Nat. Struct. Mol. Biol. 17, 666-672
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 666-672
    • Deribe, Y.L.1    Pawson, T.2    Dikic, I.3
  • 2
    • 74349091207 scopus 로고    scopus 로고
    • Protein phosphorylation in bacteria
    • Mijakovic, I. (2010) Protein phosphorylation in bacteria. Microbe 5, 21-25
    • (2010) Microbe , vol.5 , pp. 21-25
    • Mijakovic, I.1
  • 4
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E. Coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • Macek, B., Gnad, F., Soufi, B., Kumar, C., Olsen, J. V., Mijakovic, I., and Mann, M. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell. Proteomics 7, 299-307
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5    Mijakovic, I.6    Mann, M.7
  • 6
    • 37049007689 scopus 로고    scopus 로고
    • The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: Evidence for modification by unidentified protein kinases
    • Voisin, S., Watson, D. C., Tessier, L., Ding, W., Foote, S., Bhatia, S., Kelly, J. F., and Young, N. M. (2007) The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: Evidence for modification by unidentified protein kinases. Proteomics 7, 4338-4348
    • (2007) Proteomics , vol.7 , pp. 4338-4348
    • Voisin, S.1    Watson, D.C.2    Tessier, L.3    Ding, W.4    Foote, S.5    Bhatia, S.6    Kelly, J.F.7    Young, N.M.8
  • 8
    • 77953160473 scopus 로고    scopus 로고
    • The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: Analysis of the complete known ser/thr kinome suggests the existence of novel kinases
    • Schmidl, S. R., Gronau, K., Pietack, N., Hecker, M., Becher, D., and Stu?lke, J. (2010) The phosphoproteome of the minimal bacterium Mycoplasma pneumoniae: Analysis of the complete known ser/thr kinome suggests the existence of novel kinases. Mol. Cell. Proteomics 9, 1228-1242
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1228-1242
    • Schmidl, S.R.1    Gronau, K.2    Pietack, N.3    Hecker, M.4    Becher, D.5    Stulke, J.6
  • 9
    • 73649133664 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae
    • Sun, X., Ge, F., Xiao, C.-L., Yin, X.-F., Ge, R., Zhang, L.-H., and He, Q.-Y. (2009) Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. J. Proteome Res. 9, 275-282
    • (2009) J. Proteome Res. , vol.9 , pp. 275-282
    • Sun, X.1    Ge, F.2    Xiao, C.-L.3    Yin, X.-F.4    Ge, R.5    Zhang, L.-H.6    He, Q.-Y.7
  • 10
    • 75149190104 scopus 로고    scopus 로고
    • Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulence
    • Lin, M.-H., Hsu, T.-L., Lin, S.-Y., Pan, Y.-J., Jan, J.-T., Wang, J.-T., Khoo, K.-H., and Wu, S.-H. (2009) Phosphoproteomics of Klebsiella pneumoniae NTUH-K2044 reveals a tight link between tyrosine phosphorylation and virulence. Mol. Cell. Proteomics 8, 2613-2623
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2613-2623
    • Lin, M.-H.1    Hsu, T.-L.2    Lin, S.-Y.3    Pan, Y.-J.4    Jan, J.-T.5    Wang, J.-T.6    Khoo, K.-H.7    Wu, S.-H.8
  • 11
    • 66449094321 scopus 로고    scopus 로고
    • Ser/Thr/Tyr phosphoproteome analysis of pathogenic and nonpathogenic Pseudomonas species
    • Ravichandran, A., Sugiyama, N., Tomita, M., Swarup, S., and Ishihama, Y. (2009) Ser/Thr/Tyr phosphoproteome analysis of pathogenic and nonpathogenic Pseudomonas species. Proteomics 9, 2764-2775
    • (2009) Proteomics , vol.9 , pp. 2764-2775
    • Ravichandran, A.1    Sugiyama, N.2    Tomita, M.3    Swarup, S.4    Ishihama, Y.5
  • 12
    • 52649125713 scopus 로고    scopus 로고
    • The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
    • Soufi, B., Gnad, F., Jensen, P. R., Petranovic, D., Mann, M., Mijakovic, I., and Macek, B. (2008) The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins. Proteomics 8, 3486-3493
    • (2008) Proteomics , vol.8 , pp. 3486-3493
    • Soufi, B.1    Gnad, F.2    Jensen, P.R.3    Petranovic, D.4    Mann, M.5    Mijakovic, I.6    Macek, B.7
  • 14
    • 77954696406 scopus 로고    scopus 로고
    • Analysis of the phosphoproteome of the multicellular bacterium Streptomyces coelicolor A3(2) by protein/peptide fractionation, phosphopeptide enrichment and high-accuracy mass spectrometry
    • Parker, J. L., Jones, A. M. E., Serazetdinova, L., Saalbach, G., Bibb, M. J., and Naldrett, M. J. (2010) Analysis of the phosphoproteome of the multicellular bacterium Streptomyces coelicolor A3(2) by protein/peptide fractionation, phosphopeptide enrichment and high-accuracy mass spectrometry. Proteomics 10, 2486-2497
    • (2010) Proteomics , vol.10 , pp. 2486-2497
    • Parker, J.L.1    Jones, A.M.E.2    Serazetdinova, L.3    Saalbach, G.4    Bibb, M.J.5    Naldrett, M.J.6
  • 15
    • 77954371891 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis
    • Soufi, B., Kumar, C., Gnad, F., Mann, M., Mijakovic, I., and Macek, B. (2010) Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis. J. Proteome Res. 9, 3638-3646
    • (2010) J. Proteome Res. , vol.9 , pp. 3638-3646
    • Soufi, B.1    Kumar, C.2    Gnad, F.3    Mann, M.4    Mijakovic, I.5    Macek, B.6
  • 16
    • 82755198873 scopus 로고    scopus 로고
    • Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation
    • Manteca, A., Ye, J., Sanchez, J., and Jensen, O. N. (2011) Phosphoproteome analysis of Streptomyces development reveals extensive protein phosphorylation accompanying bacterial differentiation. J. Proteome Res. 10, 5481-5492
    • (2011) J. Proteome Res. , vol.10 , pp. 5481-5492
    • Manteca, A.1    Ye, J.2    Sanchez, J.3    Jensen, O.N.4
  • 17
    • 84879401680 scopus 로고    scopus 로고
    • Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium
    • Soares, N. C., Spa?t, P., Krug, K., and Macek, B. (2013) Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. J. Proteome Res. 12, 2611-2621
    • (2013) J. Proteome Res. , vol.12 , pp. 2611-2621
    • Soares, N.C.1    Spat, P.2    Krug, K.3    Macek, B.4
  • 18
    • 14544294545 scopus 로고    scopus 로고
    • Bioactive microbial metabolites
    • Berdy, J. (2005) Bioactive microbial metabolites. J. Antibiotics 58, 1-26
    • (2005) J. Antibiotics , vol.58 , pp. 1-26
    • Berdy, J.1
  • 20
    • 84872175708 scopus 로고    scopus 로고
    • Saccharopolyspora erythraea?s genome is organised in high-order transcriptional regions mediated by targeted degradation at the metabolic switch
    • Marcellin, E., Mercer, T., Licona-Cassani, C., Palfreyman, R., Dinger, M., Steen, J., Mattick, J., and Nielsen, L. (2013) Saccharopolyspora erythraea?s genome is organised in high-order transcriptional regions mediated by targeted degradation at the metabolic switch. BMC Genomics 14, 15
    • (2013) BMC Genomics , vol.14 , pp. 15
    • Marcellin, E.1    Mercer, T.2    Licona-Cassani, C.3    Palfreyman, R.4    Dinger, M.5    Steen, J.6    Mattick, J.7    Nielsen, L.8
  • 22
    • 70350722394 scopus 로고    scopus 로고
    • Genomic basis for natural product biosynthetic diversity in the actinomycetes
    • Nett, M., Ikeda, H., and Moore, B. S. (2009) Genomic basis for natural product biosynthetic diversity in the actinomycetes. Nat. Prod. Rep. 26, 1362-1384
    • (2009) Nat. Prod. Rep. , vol.26 , pp. 1362-1384
    • Nett, M.1    Ikeda, H.2    Moore, B.S.3
  • 23
    • 40849142590 scopus 로고    scopus 로고
    • Improvement of erythromycin production by Saccharopolyspora erythraea in molasses based medium through cultivation medium optimization
    • El-Enshasy, H. A., Mohamed, N. A., Farid, M. A., and El-Diwany, A. I. (2008) Improvement of erythromycin production by Saccharopolyspora erythraea in molasses based medium through cultivation medium optimization. Bioresour. Technol. 99, 4263-4268
    • (2008) Bioresour. Technol. , vol.99 , pp. 4263-4268
    • El-Enshasy, H.A.1    Mohamed, N.A.2    Farid, M.A.3    El-Diwany, A.I.4
  • 24
    • 84880864034 scopus 로고    scopus 로고
    • Systems perspectives on erythromycin biosynthesis by comparative genomic and transcriptomic analyses of S. Erythraea E3 and NRRL23338 strains
    • Li, Y.-Y., Chang, X., Yu, W.-B., Li, H., Ye, Z.-Q., Yu, H., Liu, B.-H., Zhang, Y., Zhang, S.-L., Ye, B.-C., and Li, Y.-X. (2013) Systems perspectives on erythromycin biosynthesis by comparative genomic and transcriptomic analyses of S. erythraea E3 and NRRL23338 strains. BMC Genomics 14, 523
    • (2013) BMC Genomics , vol.14 , pp. 523
    • Li, Y.-Y.1    Chang, X.2    Yu, W.-B.3    Li, H.4    Ye, Z.-Q.5    Yu, H.6    Liu, B.-H.7    Zhang, Y.8    Zhang, S.-L.9    Ye, B.-C.10    Li, Y.-X.11
  • 25
    • 84998829073 scopus 로고    scopus 로고
    • Genome sequence of Saccharopolyspora erythraea D, a hyperproducer of erythromycin
    • Liu, W.-B., Yu, W.-B., Gao, S.-H., and Ye, B.-C. (2013) Genome sequence of Saccharopolyspora erythraea D, a hyperproducer of erythromycin. Genome Announc. 1, e00718-13
    • (2013) Genome Announc. , vol.1 , pp. 00718-00813
    • Liu, W.-B.1    Yu, W.-B.2    Gao, S.-H.3    Ye, B.-C.4
  • 26
    • 84857950749 scopus 로고    scopus 로고
    • Comparative genomics and transcriptional profiles of Saccharopolyspora erythraea NRRL 2338 and a classically improved erythromycin over-producing strain
    • Peano, C., Tala, A., Corti, G., Pasanisi, D., Durante, M., Mita, G., Bicciato, S., De Bellis, G., and Alifano, P. (2012) Comparative genomics and transcriptional profiles of Saccharopolyspora erythraea NRRL 2338 and a classically improved erythromycin over-producing strain. Microb. Cell Fact. 11, 32
    • (2012) Microb. Cell Fact. , vol.11 , pp. 32
    • Peano, C.1    Tala, A.2    Corti, G.3    Pasanisi, D.4    Durante, M.5    Mita, G.6    Bicciato, S.7    De Bellis, G.8    Alifano, P.9
  • 27
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A., Tang, W. H., Keating, S. P., Hunter, C. L., Nuwaysir, L. M., and Schaeffer, D. A. (2007) The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 6, 1638-1655
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 29
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structurebased prediction of eukaryotic protein phosphorylation sites
    • Blom, N., Gammeltoft, S., and Brunak, S. (1999) Sequence and structurebased prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294, 1351-1362
    • (1999) J. Mol. Biol. , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 30
    • 59449102308 scopus 로고    scopus 로고
    • Netphosbac-A predictor for ser/thr phosphorylation sites in bacterial proteins
    • Miller, M. L., Soufi, B., Jers, C., Blom, N., Macek, B., and Mijakovic, I. (2009) NetPhosBac-a predictor for Ser/Thr phosphorylation sites in bacterial proteins. Proteomics 9, 116-125
    • (2009) Proteomics , vol.9 , pp. 116-125
    • Miller, M.L.1    Soufi, B.2    Jers, C.3    Blom, N.4    Macek, B.5    Mijakovic, I.6
  • 31
    • 63349105962 scopus 로고    scopus 로고
    • Phoscalc: A tool for evaluating the sites of peptide phosphorylation from mass spectrometer data
    • MacLean, D., Burrell, M., Studholme, D., and Jones, A. (2008) PhosCalc: A tool for evaluating the sites of peptide phosphorylation from mass spectrometer data. BMC Res. Notes 1, 30
    • (2008) BMC Res. Notes , vol.1 , pp. 30
    • Maclean, D.1    Burrell, M.2    Studholme, D.3    Jones, A.4
  • 32
    • 61449172037 scopus 로고    scopus 로고
    • Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
    • Huang, D. W., Sherman, B. T., and Lempicki, R. A. (2008) Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44-57
    • (2008) Nat. Protoc. , vol.4 , pp. 44-57
    • Huang, D.W.1    Sherman, B.T.2    Lempicki, R.A.3
  • 33
    • 9444225935 scopus 로고    scopus 로고
    • Java Treeview-extensible visualization of microarray data
    • Saldanha, A. J. (2004) Java Treeview-extensible visualization of microarray data. Bioinformatics 20, 3246-3248
    • (2004) Bioinformatics , vol.20 , pp. 3246-3248
    • Saldanha, A.J.1
  • 34
    • 67650566399 scopus 로고    scopus 로고
    • Hyaluronan molecular weight is controlled by UDP-N-acetylglucosamine concentration in Streptococcus zooepidemicus
    • Chen, W. Y., Marcellin, E., Hung, J., and Nielsen, L. K. (2009) Hyaluronan molecular weight is controlled by UDP-N-acetylglucosamine concentration in Streptococcus zooepidemicus. J. Biol. Chem. 284, 18007-18014
    • (2009) J. Biol. Chem. , vol.284 , pp. 18007-18014
    • Chen, W.Y.1    Marcellin, E.2    Hung, J.3    Nielsen, L.K.4
  • 35
    • 84867574100 scopus 로고    scopus 로고
    • Reconstruction of the Saccharopolyspora erythraea genomescale model and its use for enhancing erythromycin production
    • Licona-Cassani, C., Marcellin, E., Quek, L.-E., Jacob, S., and Nielsen, L. (2012) Reconstruction of the Saccharopolyspora erythraea genomescale model and its use for enhancing erythromycin production. Antonie Van Leeuwenhoek 102, 493-502
    • (2012) Antonie Van Leeuwenhoek , vol.102 , pp. 493-502
    • Licona-Cassani, C.1    Marcellin, E.2    Quek, L.-E.3    Jacob, S.4    Nielsen, L.5
  • 37
    • 0038460070 scopus 로고    scopus 로고
    • Proteomic studies of diauxic lag in the differentiating prokaryote Streptomyces coelicolor reveal a regulatory network of stress-induced proteins and central metabolic enzymes
    • Novotna, J., Vohradsky, J., Berndt, P., Gramajo, H., Langen, H., Li, X.-M., Minas, W., Orsaria, L., Roeder, D., and Thompson, C. J. (2003) Proteomic studies of diauxic lag in the differentiating prokaryote Streptomyces coelicolor reveal a regulatory network of stress-induced proteins and central metabolic enzymes. Mol. Microbiol. 48, 1289-1303
    • (2003) Mol. Microbiol. , vol.48 , pp. 1289-1303
    • Novotna, J.1    Vohradsky, J.2    Berndt, P.3    Gramajo, H.4    Langen, H.5    Li, X.-M.6    Minas, W.7    Orsaria, L.8    Roeder, D.9    Thompson, C.J.10
  • 38
    • 33845228342 scopus 로고    scopus 로고
    • A proteomic analysis of Streptomyces coelicolor programmed cell death
    • Manteca, A., Ma?der, U., Connolly, B. A., and Sanchez, J. (2006) A proteomic analysis of Streptomyces coelicolor programmed cell death. Proteomics 6, 6008-6022
    • (2006) Proteomics , vol.6 , pp. 6008-6022
    • Manteca, A.1    Mader, U.2    Connolly, B.A.3    Sanchez, J.4
  • 40
    • 77956329728 scopus 로고    scopus 로고
    • Quantitative proteome analysis of Streptomyces coelicolor nonsporulating liquid cultures demonstrates a complex differentiation process comparable to that occurring in sporulating solid cultures
    • Manteca, A., Jung, H. R., Schwa?mmle, V., Jensen, O. N., and Sanchez, J. (2010) Quantitative proteome analysis of Streptomyces coelicolor nonsporulating liquid cultures demonstrates a complex differentiation process comparable to that occurring in sporulating solid cultures. J. Proteome Res. 9, 4801-4811
    • (2010) J. Proteome Res. , vol.9 , pp. 4801-4811
    • Manteca, A.1    Jung, H.R.2    Schwammle, V.3    Jensen, O.N.4    Sanchez, J.5
  • 41
    • 84862596522 scopus 로고    scopus 로고
    • Impact of phosphoproteomics on studies of bacterial physiology
    • Mijakovic, I., and Macek, B. (2012) Impact of phosphoproteomics on studies of bacterial physiology. FEMS Microbiol. Rev. 36, 877-892
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 877-892
    • Mijakovic, I.1    Macek, B.2
  • 42
    • 0035231423 scopus 로고    scopus 로고
    • The esat-6 gene cluster of mycobacterium tuberculosis and other high g-c gram-positive bacteria
    • research0044.1-0044.18
    • Gey Van Pittius, N., Gamieldien, J., Hide, W., Brown, G., Siezen, R., and Beyers, A. (2001) The ESAT-6 gene cluster of Mycobacterium tuberculosis and other high G-C Gram-positive bacteria. Genome Biol. 2, research0044.1-0044.18
    • (2001) Genome Biol. , vol.2
    • Gey Van Pittius, N.1    Gamieldien, J.2    Hide, W.3    Brown, G.4    Siezen, R.5    Beyers, A.6
  • 43
    • 77953181571 scopus 로고    scopus 로고
    • A heterodimer of esxa and esxb is involved in sporulation and is secreted by a type vii secretion system in streptomyces coelicolor
    • Akpe San Roman, S., Facey, P. D., Fernandez-Martinez, L., Rodriguez, C., Vallin, C., Del Sol, R., and Dyson, P. (2010) A heterodimer of EsxA and EsxB is involved in sporulation and is secreted by a type VII secretion system in Streptomyces coelicolor. Microbiology 156, 1719-1729
    • (2010) Microbiology , vol.156 , pp. 1719-1729
    • Akpe San Roman, S.1    Facey, P.D.2    Fernandez-Martinez, L.3    Rodriguez, C.4    Vallin, C.5    Del Sol, R.6    Dyson, P.7
  • 44
    • 33748776564 scopus 로고    scopus 로고
    • C-terminal signal sequence promotes virulence factor secretion in mycobacterium tuberculosis
    • Champion, P. A. D., Stanley, S. A., Champion, M. M., Brown, E. J., and Cox, J. S. (2006) C-terminal signal sequence promotes virulence factor secretion in Mycobacterium tuberculosis. Science 313, 1632-1636
    • (2006) Science , vol.313 , pp. 1632-1636
    • Champion, P.A.D.1    Stanley, S.A.2    Champion, M.M.3    Brown, E.J.4    Cox, J.S.5
  • 46
    • 0024289985 scopus 로고
    • In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7
    • Hoyt, J. C., and Reeves, H. C. (1988) In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7. Biochem. Biophys. Res. Commun. 153, 875-880
    • (1988) Biochem. Biophys. Res. Commun. , vol.153 , pp. 875-880
    • Hoyt, J.C.1    Reeves, H.C.2
  • 48
    • 34249301015 scopus 로고    scopus 로고
    • Engineering of the methylmalonyl-CoA metabolite node of Saccharopolyspora erythraea for increased erythromycin production
    • Reeves, A. R., Brikun, I. A., Cernota, W. H., Leach, B. I., Gonzalez, M. C., and Mark Weber, J. (2007) Engineering of the methylmalonyl-CoA metabolite node of Saccharopolyspora erythraea for increased erythromycin production. Metab. Eng. 9, 293-303
    • (2007) Metab. Eng. , vol.9 , pp. 293-303
    • Reeves, A.R.1    Brikun, I.A.2    Cernota, W.H.3    Leach, B.I.4    Gonzalez, M.C.5    Mark Weber, J.6
  • 49
    • 33645057433 scopus 로고    scopus 로고
    • Metabolic pathway engineering for complex polyketide biosynthesis in saccharomyces cerevisiae
    • Mutka, S. C., Bondi, S. M., Carney, J. R., Da Silva, N. A., and Kealey, J. T. (2006) Metabolic pathway engineering for complex polyketide biosynthesis in Saccharomyces cerevisiae. FEMS Yeast Res. 6, 40-47
    • (2006) FEMS Yeast Res. , vol.6 , pp. 40-47
    • Mutka, S.C.1    Bondi, S.M.2    Carney, J.R.3    Da Silva, N.A.4    Kealey, J.T.5
  • 50
    • 0036015638 scopus 로고    scopus 로고
    • Identification and cloning of a type III polyketide synthase required for diffusible pigment biosynthesis in Saccharopolyspora erythraea
    • Corte?s, J., Velasco, J., Foster, G., Blackaby, A. P., Rudd, B. A. M., and Wilkinson, B. (2002) Identification and cloning of a type III polyketide synthase required for diffusible pigment biosynthesis in Saccharopolyspora erythraea. Mol. Microbiol. 44, 1213-1224
    • (2002) Mol. Microbiol. , vol.44 , pp. 1213-1224
    • Cortes, J.1    Velasco, J.2    Foster, G.3    Blackaby, A.P.4    Rudd, B.A.M.5    Wilkinson, B.6
  • 51
    • 34748822934 scopus 로고    scopus 로고
    • Role of adenosine kinase in the control of Streptomyces differentiations: Loss of adenosine kinase suppresses sporulation and actinorhodin biosynthesis while inducing hyperproduction of undecylprodigiosin in Streptomyces lividans
    • Rajkarnikar, A., Kwon, H.-J., and Suh, J.-W. (2007) Role of adenosine kinase in the control of Streptomyces differentiations: Loss of adenosine kinase suppresses sporulation and actinorhodin biosynthesis while inducing hyperproduction of undecylprodigiosin in Streptomyces lividans. Biochem. Biophys. Res. Commun. 363, 322-328
    • (2007) Biochem. Biophys. Res. Commun. , vol.363 , pp. 322-328
    • Rajkarnikar, A.1    Kwon, H.-J.2    Suh, J.-W.3
  • 52
    • 80051570211 scopus 로고    scopus 로고
    • An ArsR-like transcriptional factor recognizes a conserved sequence motif and positively regulates the expression of phoP in mycobacteria
    • Gao, C.-H., Yang, M., and He, Z.-G. (2011) An ArsR-like transcriptional factor recognizes a conserved sequence motif and positively regulates the expression of phoP in mycobacteria. Biochem. Biophys. Res. Commun. 411, 726-731
    • (2011) Biochem. Biophys. Res. Commun. , vol.411 , pp. 726-731
    • Gao, C.-H.1    Yang, M.2    He, Z.-G.3
  • 53
    • 84860467728 scopus 로고    scopus 로고
    • Characterization of a novel arsr-like regulator encoded by rv2034 in mycobacterium tuberculosis
    • Gao, C.-h., Yang, M., and He, Z.-G. (2012) Characterization of a novel ArsR-like regulator encoded by Rv2034 in Mycobacterium tuberculosis. PLoS One 7, e36255
    • (2012) PLoS One , vol.7
    • Gao, C.-H.1    Yang, M.2    He, Z.-G.3
  • 54
    • 58249087037 scopus 로고    scopus 로고
    • Identifying and characterizing substrates of the rnase e/g family of enzymes
    • Kime, L., Jourdan, S. S., and McDowall, K. J. (2008) Identifying and characterizing substrates of the RNase E/G family of enzymes. Methods in Enzymology 447, 215-241
    • (2008) Methods in Enzymology , vol.447 , pp. 215-241
    • Kime, L.1    Jourdan, S.S.2    McDowall, K.J.3
  • 55
    • 84861205241 scopus 로고    scopus 로고
    • RNA-Seq and RNA immunoprecipitation analyses of the transcriptome of Streptomyces coelicolor identify substrates for RNase III
    • Gatewood, M. L., Bralley, P., Weil, M. R., and Jones, G. H. (2012) RNA-Seq and RNA immunoprecipitation analyses of the transcriptome of Streptomyces coelicolor identify substrates for RNase III. J. Bacteriol. 194, 2228-2237
    • (2012) J. Bacteriol. , vol.194 , pp. 2228-2237
    • Gatewood, M.L.1    Bralley, P.2    Weil, M.R.3    Jones, G.H.4
  • 56
    • 10344258624 scopus 로고    scopus 로고
    • Endonuclease-mediated mRNA decay requires tyrosine phosphorylation of polysomal ribonuclease 1 (PMR1) for the targeting and degradation of polyribosome-bound substrate mRNA
    • Yang, F., Peng, Y., and Schoenberg, D. R. (2004) Endonuclease-mediated mRNA decay requires tyrosine phosphorylation of polysomal ribonuclease 1 (PMR1) for the targeting and degradation of polyribosome-bound substrate mRNA. J. Biol. Chem. 279, 48993-49002
    • (2004) J. Biol. Chem. , vol.279 , pp. 48993-49002
    • Yang, F.1    Peng, Y.2    Schoenberg, D.R.3
  • 57
    • 0028945837 scopus 로고
    • RNA degradation in Escherichia coli regulated by 3 adenylation and 5 phosphorylation
    • Xu, F., and Cohen, S. N. (1995) RNA degradation in Escherichia coli regulated by 3 adenylation and 5 horylation. Nature 374, 180-183
    • (1995) Nature , vol.374 , pp. 180-183
    • Xu, F.1    Cohen, S.N.2
  • 58
    • 79951967246 scopus 로고    scopus 로고
    • HTRA proteases: Regulated proteolysis in protein quality control
    • Clausen, T., Kaiser, M., Huber, R., and Ehrmann, M. (2011) HTRA proteases: Regulated proteolysis in protein quality control. Nat. Rev. Mol. Cell Biol. 12, 152-162
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 152-162
    • Clausen, T.1    Kaiser, M.2    Huber, R.3    Ehrmann, M.4
  • 63
    • 79951598380 scopus 로고    scopus 로고
    • Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor
    • Mikulik, K., Bobek, J., Zikova, A., Smetakova, M., and Bezouskova, S. (2011) Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor. Mol. Biosyst. 7, 817-823
    • (2011) Mol. Biosyst. , vol.7 , pp. 817-823
    • Mikulik, K.1    Bobek, J.2    Zikova, A.3    Smetakova, M.4    Bezouskova, S.5
  • 64
    • 56949100388 scopus 로고    scopus 로고
    • Characterization of heterogeneous LSU rRNA profiles in Streptomyces coelicolor under different growth stages and conditions
    • Kim, H. L., Song, W. S., Kim, K., and Lee, K. (2008) Characterization of heterogeneous LSU rRNA profiles in Streptomyces coelicolor under different growth stages and conditions. Curr. Microbiol. 57, 537-541
    • (2008) Curr. Microbiol. , vol.57 , pp. 537-541
    • Kim, H.L.1    Song, W.S.2    Kim, K.3    Lee, K.4
  • 65
    • 34548588389 scopus 로고    scopus 로고
    • Heterogeneous rRNAs are differentially expressed during the morphological development of Streptomyces coelicolor
    • Kim, H. L., Shin, E. K., Kim, H. M., Ryou, S. M., Kim, S., Cha, C. J., Bae, J., and Lee, K. (2007) Heterogeneous rRNAs are differentially expressed during the morphological development of Streptomyces coelicolor. FEMS Microbiol. Lett. 275, 146-152
    • (2007) FEMS Microbiol. Lett. , vol.275 , pp. 146-152
    • Kim, H.L.1    Shin, E.K.2    Kim, H.M.3    Ryou, S.M.4    Kim, S.5    Cha, C.J.6    Bae, J.7    Lee, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.