메뉴 건너뛰기




Volumn 75, Issue 2, 2010, Pages 349-364

PolY, a transcriptional regulator with ATPase activity, directly activates transcription of polR in polyoxin biosynthesis in Streptomyces cacaoi

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; DEOXYRIBONUCLEASE I; OUTER MEMBRANE PROTEIN REGULATOR; POLYOXIN B; PROTEIN POLY; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 74349130880     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06968.x     Document Type: Article
Times cited : (44)

References (45)
  • 1
    • 0028213705 scopus 로고
    • An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B. subtilis
    • Alper, S., Duncan, L. Losick, R. (1994) An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B. subtilis. Cell 77 : 195 205.
    • (1994) Cell , vol.77 , pp. 195-205
    • Alper, S.1    Duncan, L.2    Losick, R.3
  • 2
    • 1942539982 scopus 로고    scopus 로고
    • Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis
    • Anton, N., Mendes, M.V., Martin, J.F. Aparicio, J.F. (2004) Identification of PimR as a positive regulator of pimaricin biosynthesis in Streptomyces natalensis. J Bacteriol 186 : 2567 2575.
    • (2004) J Bacteriol , vol.186 , pp. 2567-2575
    • Anton, N.1    Mendes, M.V.2    Martin, J.F.3    Aparicio, J.F.4
  • 3
    • 0344146592 scopus 로고    scopus 로고
    • Characterization of the pathway-specific positive transcriptional regulator for actinorhodin biosynthesis in Streptomyces coelicolor A3(2) as a DNA-binding protein
    • Arias, P., Fernandez-Moreno, M.A. Malpartida, F. (1999) Characterization of the pathway-specific positive transcriptional regulator for actinorhodin biosynthesis in Streptomyces coelicolor A3(2) as a DNA-binding protein. J Bacteriol 181 : 6958 6968.
    • (1999) J Bacteriol , vol.181 , pp. 6958-6968
    • Arias, P.1    Fernandez-Moreno, M.A.2    Malpartida, F.3
  • 4
    • 15744383448 scopus 로고    scopus 로고
    • Regulation of secondary metabolism in streptomycetes
    • Bibb, M.J. (2005) Regulation of secondary metabolism in streptomycetes. Curr Opin Microbiol 8 : 208 215.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 208-215
    • Bibb, M.J.1
  • 5
    • 0026645203 scopus 로고
    • Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp
    • Bierman, M., Logan, R., O'Brien, K., Seno, E.T., Rao, R.N. Schoner, B.E. (1992) Plasmid cloning vectors for the conjugal transfer of DNA from Escherichia coli to Streptomyces spp. Gene 116 : 43 49.
    • (1992) Gene , vol.116 , pp. 43-49
    • Bierman, M.1    Logan, R.2    O'Brien, K.3    Seno, E.T.4    Rao, R.N.5    Schoner, B.E.6
  • 6
    • 0032568168 scopus 로고    scopus 로고
    • The NB-ARC domain: A novel signalling motif shared by plant resistance gene products and regulators of cell death in animals
    • van der Biezen, E.A. Jones, J.D. (1998) The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals. Curr Biol 8 : R226 R227.
    • (1998) Curr Biol , vol.8
    • Van Der Biezen, E.A.1    Jones, J.D.2
  • 7
    • 0032850662 scopus 로고    scopus 로고
    • Molecular characterization of co-transcribed genes from Streptomyces tendae Tu901 involved in the biosynthesis of the peptidyl moiety of the peptidyl nucleoside antibiotic nikkomycin
    • Bruntner, C., Lauer, B., Schwarz, W., Mohrle, V. Bormann, C. (1999) Molecular characterization of co-transcribed genes from Streptomyces tendae Tu901 involved in the biosynthesis of the peptidyl moiety of the peptidyl nucleoside antibiotic nikkomycin. Mol Gen Genet 262 : 102 114.
    • (1999) Mol Gen Genet , vol.262 , pp. 102-114
    • Bruntner, C.1    Lauer, B.2    Schwarz, W.3    Mohrle, V.4    Bormann, C.5
  • 8
    • 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
  • 9
    • 67449094184 scopus 로고    scopus 로고
    • Characterization of the polyoxin biosynthetic gene cluster from Streptomyces cacaoi and engineered production of Polyoxin H
    • Chen, W., Huang, T., He, X., Meng, Q., You, D., Bai, L., et al. (2009) Characterization of the polyoxin biosynthetic gene cluster from Streptomyces cacaoi and engineered production of Polyoxin H. J Biol Chem 284 : 10627 10638.
    • (2009) J Biol Chem , vol.284 , pp. 10627-10638
    • Chen, W.1    Huang, T.2    He, X.3    Meng, Q.4    You, D.5    Bai, L.6
  • 10
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F. Duguet, M. (1995) A 200-amino acid ATPase module in search of a basic function. Bioessays 17 : 639 650.
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 11
    • 0017110209 scopus 로고
    • Regulation and biosynthesis of secondary metabolites. XVIII. Adenylate level and chlorotetracycline production in Streptomyces aureofaciens
    • Curdova, E., Kremen, A., Vanek, Z. Hostalek, Z. (1976) Regulation and biosynthesis of secondary metabolites. XVIII. Adenylate level and chlorotetracycline production in Streptomyces aureofaciens. Folia Microbiol (Praha) 21 : 481 487.
    • (1976) Folia Microbiol (Praha) , vol.21 , pp. 481-487
    • Curdova, E.1    Kremen, A.2    Vanek, Z.3    Hostalek, Z.4
  • 12
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea, L.D. Regan, L. (2003) TPR proteins: the versatile helix. Trends Biochem Sci 28 : 655 662.
    • (2003) Trends Biochem Sci , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 13
    • 0029762312 scopus 로고    scopus 로고
    • AfsR is a pleiotropic but conditionally required regulatory gene for antibiotic production in Streptomyces coelicolor A3(2)
    • Floriano, B. Bibb, M. (1996) afsR is a pleiotropic but conditionally required regulatory gene for antibiotic production in Streptomyces coelicolor A3(2). Mol Microbiol 21 : 385 396.
    • (1996) Mol Microbiol , vol.21 , pp. 385-396
    • Floriano, B.1    Bibb, M.2
  • 15
    • 0029440560 scopus 로고
    • Genetics of antibiotic production in Streptomyces coelicolor A3(2), a model streptomycete
    • Hopwood, D.A., Chater, K.F. Bibb, M.J. (1995) Genetics of antibiotic production in Streptomyces coelicolor A3(2), a model streptomycete. Biotechnology 28 : 65 102.
    • (1995) Biotechnology , vol.28 , pp. 65-102
    • Hopwood, D.A.1    Chater, K.F.2    Bibb, M.J.3
  • 16
    • 0141594679 scopus 로고    scopus 로고
    • AfsR as an integrator of signals that are sensed by multiple serine/threonine kinases in Streptomyces coelicolor A3(2)
    • Horinouchi, S. (2003) AfsR as an integrator of signals that are sensed by multiple serine/threonine kinases in Streptomyces coelicolor A3(2). J Ind Microbiol Biotechnol 30 : 462 467.
    • (2003) J Ind Microbiol Biotechnol , vol.30 , pp. 462-467
    • Horinouchi, S.1
  • 17
    • 0025250635 scopus 로고
    • Primary structure of AfsR, a global regulatory protein for secondary metabolite formation in Streptomyces coelicolor A3(2)
    • Horinouchi, S., Kito, M., Nishiyama, M., Furuya, K., Hong, S.K., Miyake, K. Beppu, T. (1990) Primary structure of AfsR, a global regulatory protein for secondary metabolite formation in Streptomyces coelicolor A3(2). Gene 95 : 49 56.
    • (1990) Gene , vol.95 , pp. 49-56
    • Horinouchi, S.1    Kito, M.2    Nishiyama, M.3    Furuya, K.4    Hong, S.K.5    Miyake, K.6    Beppu, T.7
  • 18
    • 0035734689 scopus 로고    scopus 로고
    • The A-factor regulatory cascade and cAMP in the regulation of physiological and morphological development in Streptomyces griseus
    • Horinouchi, S., Ohnishi, Y. Kang, D.K. (2001) The A-factor regulatory cascade and cAMP in the regulation of physiological and morphological development in Streptomyces griseus. J Ind Microbiol Biotechnol 27 : 177 182.
    • (2001) J Ind Microbiol Biotechnol , vol.27 , pp. 177-182
    • Horinouchi, S.1    Ohnishi, Y.2    Kang, D.K.3
  • 19
    • 4444329170 scopus 로고    scopus 로고
    • Widespread activation of antibiotic biosynthesis by S-adenosylmethionine in streptomycetes
    • Huh, J.H., Kim, D.J., Zhao, X.Q., Li, M., Jo, Y.Y., Yoon, T.M., et al. (2004) Widespread activation of antibiotic biosynthesis by S-adenosylmethionine in streptomycetes. FEMS Microbiol Lett 238 : 439 447.
    • (2004) FEMS Microbiol Lett , vol.238 , pp. 439-447
    • Huh, J.H.1    Kim, D.J.2    Zhao, X.Q.3    Li, M.4    Jo, Y.Y.5    Yoon, T.M.6
  • 20
    • 0032946589 scopus 로고    scopus 로고
    • Possible involvement of cAMP in aerial mycelium formation and secondary metabolism in Streptomyces griseus
    • Kang, D.K., Li, X.M., Ochi, K. Horinouchi, S. (1999) Possible involvement of cAMP in aerial mycelium formation and secondary metabolism in Streptomyces griseus. Microbiology 145 : 1161 1172.
    • (1999) Microbiology , vol.145 , pp. 1161-1172
    • Kang, D.K.1    Li, X.M.2    Ochi, K.3    Horinouchi, S.4
  • 22
    • 0037224691 scopus 로고    scopus 로고
    • Accumulation of S-adenosyl-L-methionine enhances production of actinorhodin but inhibits sporulation in Streptomyces lividans TK23
    • Kim, D.J., Huh, J.H., Yang, Y.Y., Kang, C.M., Lee, I.H., Hyun, C.G., et al. (2003) Accumulation of S-adenosyl-L-methionine enhances production of actinorhodin but inhibits sporulation in Streptomyces lividans TK23. J Bacteriol 185 : 592 600.
    • (2003) J Bacteriol , vol.185 , pp. 592-600
    • Kim, D.J.1    Huh, J.H.2    Yang, Y.Y.3    Kang, C.M.4    Lee, I.H.5    Hyun, C.G.6
  • 23
    • 0025967413 scopus 로고
    • Plasmid cloning vectors that integrate site-specifically in Streptomyces spp
    • Kuhstoss, S., Richardson, M.A. Rao, R.N. (1991) Plasmid cloning vectors that integrate site-specifically in Streptomyces spp. Gene 97 : 143 146.
    • (1991) Gene , vol.97 , pp. 143-146
    • Kuhstoss, S.1    Richardson, M.A.2    Rao, R.N.3
  • 24
    • 0036268103 scopus 로고    scopus 로고
    • AfsS is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3(2)
    • Lee, P.C., Umeyama, T. Horinouchi, S. (2002) afsS is a target of AfsR, a transcriptional factor with ATPase activity that globally controls secondary metabolism in Streptomyces coelicolor A3(2). Mol Microbiol 43 : 1413 1430.
    • (2002) Mol Microbiol , vol.43 , pp. 1413-1430
    • Lee, P.C.1    Umeyama, T.2    Horinouchi, S.3
  • 25
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • Leipe, D.D., Koonin, E.V. Aravind, L. (2004) STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer. J Mol Biol 343 : 1 28.
    • (2004) J Mol Biol , vol.343 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 26
    • 0026029699 scopus 로고
    • TTA codons in some genes prevent their expression in a class of developmental, antibiotic-negative, Streptomyces mutants
    • Leskiw, B.K., Lawlor, E.J., Fernandez-Abalos, J.M. Chater, K.F. (1991) TTA codons in some genes prevent their expression in a class of developmental, antibiotic-negative, Streptomyces mutants. Proc Natl Acad Sci USA 88 : 2461 2465.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2461-2465
    • Leskiw, B.K.1    Lawlor, E.J.2    Fernandez-Abalos, J.M.3    Chater, K.F.4
  • 27
    • 47849088463 scopus 로고    scopus 로고
    • Effects of extracellular ATP on the physiology of Streptomyces coelicolor A3(2)
    • Li, M., Kim, T.J., Kwon, H.J. Suh, J.W. (2008) Effects of extracellular ATP on the physiology of Streptomyces coelicolor A3(2). FEMS Microbiol Lett 286 : 24 31.
    • (2008) FEMS Microbiol Lett , vol.286 , pp. 24-31
    • Li, M.1    Kim, T.J.2    Kwon, H.J.3    Suh, J.W.4
  • 28
    • 67650759674 scopus 로고    scopus 로고
    • PolR, a pathway-specific transcriptional regulatory gene, positively controls polyoxin biosynthesis in Streptomyces cacaoi subsp
    • Li, R., Xie, Z., Tian, Y., Yang, H., Chen, W., You, D., et al. (2009) polR, a pathway-specific transcriptional regulatory gene, positively controls polyoxin biosynthesis in Streptomyces cacaoi subsp. Asoensis Microbiol 155 : 1819 1831.
    • (2009) Asoensis Microbiol , vol.155 , pp. 1819-1831
    • Li, R.1    Xie, Z.2    Tian, Y.3    Yang, H.4    Chen, W.5    You, D.6
  • 29
    • 15944401749 scopus 로고    scopus 로고
    • A pathway-specific transcriptional regulatory gene for nikkomycin biosynthesis in Streptomyces ansochromogenes that also influences colony development
    • Liu, G., Tian, Y., Yang, H. Tan, H. (2005) A pathway-specific transcriptional regulatory gene for nikkomycin biosynthesis in Streptomyces ansochromogenes that also influences colony development. Mol Microbiol 55 : 1855 1866.
    • (2005) Mol Microbiol , vol.55 , pp. 1855-1866
    • Liu, G.1    Tian, Y.2    Yang, H.3    Tan, H.4
  • 30
    • 0029912156 scopus 로고    scopus 로고
    • Regulation of spiramycin synthesis in Streptomyces ambofaciens: Effects of glucose and inorganic phosphate
    • Lounes, A., Lebrihi, A., Benslimane, C., Lefebvre, G. Germain, P. (1996) Regulation of spiramycin synthesis in Streptomyces ambofaciens: effects of glucose and inorganic phosphate. Appl Microbiol Biotechnol 45 : 204 211.
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 204-211
    • Lounes, A.1    Lebrihi, A.2    Benslimane, C.3    Lefebvre, G.4    Germain, P.5
  • 31
    • 34250310872 scopus 로고    scopus 로고
    • Cloning and heterologous expression of the aranciamycin biosynthetic gene cluster revealed a new flexible glycosyltransferase
    • Luzhetskyy, A., Mayer, A., Hoffmann, J., Pelzer, S., Holzenkamper, M., Schmitt, B., et al. (2007) Cloning and heterologous expression of the aranciamycin biosynthetic gene cluster revealed a new flexible glycosyltransferase. Chembiochem 8 : 599 602.
    • (2007) Chembiochem , vol.8 , pp. 599-602
    • Luzhetskyy, A.1    Mayer, A.2    Hoffmann, J.3    Pelzer, S.4    Holzenkamper, M.5    Schmitt, B.6
  • 32
    • 0030602821 scopus 로고    scopus 로고
    • 54-dependent activator XylR triggers a protein multimerization cycle catalysed by UAS DNA
    • 54-dependent activator XylR triggers a protein multimerization cycle catalysed by UAS DNA. Cell 86 : 331 339.
    • (1996) Cell , vol.86 , pp. 331-339
    • Perez-Martin, J.1    De Lorenzo, V.2
  • 33
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M.W. (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29 : e45.
    • (2001) Nucleic Acids Res , vol.29 , pp. 45
    • Pfaffl, M.W.1
  • 34
    • 0035839553 scopus 로고    scopus 로고
    • Roles of glucitol in the GutR-mediated transcription activation process in Bacillus subtilis: Glucitol induces GutR to change its conformation and to bind ATP
    • Poon, K.K., Chu, J.C. Wong, S.L. (2001) Roles of glucitol in the GutR-mediated transcription activation process in Bacillus subtilis: glucitol induces GutR to change its conformation and to bind ATP. J Biol Chem 276 : 29819 29825.
    • (2001) J Biol Chem , vol.276 , pp. 29819-29825
    • Poon, K.K.1    Chu, J.C.2    Wong, S.L.3
  • 36
    • 0035947655 scopus 로고    scopus 로고
    • Atpase activity and multimer formation of Pilq protein are required for thin pilus biogenesis in plasmid R64
    • Sakai, D., Horiuchi, T. Komano, T. (2001) Atpase activity and multimer formation of Pilq protein are required for thin pilus biogenesis in plasmid R64. J Biol Chem 276 : 17968 17975.
    • (2001) J Biol Chem , vol.276 , pp. 17968-17975
    • Sakai, D.1    Horiuchi, T.2    Komano, T.3
  • 37
    • 0025048136 scopus 로고
    • The P-loop - A common motif in ATP- and GTP-binding proteins
    • Saraste, M., Sibbald, P.R. Wittinghofer, A. (1990) The P-loop - a common motif in ATP- and GTP-binding proteins. Trends Biochem Sci 15 : 430 434.
    • (1990) Trends Biochem Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 38
    • 0033585068 scopus 로고    scopus 로고
    • Self association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP
    • Schreiber, V. Richet, E. (1999) Self association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP. J Biol Chem 274 : 33220 33226.
    • (1999) J Biol Chem , vol.274 , pp. 33220-33226
    • Schreiber, V.1    Richet, E.2
  • 39
    • 0036229192 scopus 로고    scopus 로고
    • Mapping the DNA-binding domain and target sequences of the Streptomyces peucetius daunorubicin biosynthesis regulatory protein, DnrI
    • Sheldon, P.J., Busarow, S.B. Hutchinson, C.R. (2002) Mapping the DNA-binding domain and target sequences of the Streptomyces peucetius daunorubicin biosynthesis regulatory protein, DnrI. Mol Microbiol 44 : 449 460.
    • (2002) Mol Microbiol , vol.44 , pp. 449-460
    • Sheldon, P.J.1    Busarow, S.B.2    Hutchinson, C.R.3
  • 40
    • 33646723495 scopus 로고    scopus 로고
    • S-adenosylmethionine activates adpA transcription and promotes streptomycin biosynthesis in Streptomyces griseus
    • Shin, S.K., Xu, D., Kwon, H.J. Suh, J.W. (2006) S-adenosylmethionine activates adpA transcription and promotes streptomycin biosynthesis in Streptomyces griseus. FEMS Microbiol Lett 259 : 53 59.
    • (2006) FEMS Microbiol Lett , vol.259 , pp. 53-59
    • Shin, S.K.1    Xu, D.2    Kwon, H.J.3    Suh, J.W.4
  • 41
    • 34247604950 scopus 로고    scopus 로고
    • AfsR recruits RNA polymerase to the afsS promoter: A model for transcriptional activation by SARPs
    • Tanaka, A., Takano, Y., Ohnishi, Y. Horinouchi, S. (2007) AfsR recruits RNA polymerase to the afsS promoter: a model for transcriptional activation by SARPs. J Mol Biol 369 : 322 333.
    • (2007) J Mol Biol , vol.369 , pp. 322-333
    • Tanaka, A.1    Takano, Y.2    Ohnishi, Y.3    Horinouchi, S.4
  • 42
    • 0028279385 scopus 로고
    • The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites
    • Traut, T.W. (1994) The functions and consensus motifs of nine types of peptide segments that form different types of nucleotide-binding sites. Eur J Biochem 222 : 9 19.
    • (1994) Eur J Biochem , vol.222 , pp. 9-19
    • Traut, T.W.1
  • 43
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J.E., Saraste, M., Runswick, M.J. Gay, N.J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1 : 945 951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 44
    • 0030929313 scopus 로고    scopus 로고
    • A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold
    • Wietzorrek, A. Bibb, M. (1997) A novel family of proteins that regulates antibiotic production in streptomycetes appears to contain an OmpR-like DNA-binding fold. Mol Microbiol 25 : 1181 1184.
    • (1997) Mol Microbiol , vol.25 , pp. 1181-1184
    • Wietzorrek, A.1    Bibb, M.2
  • 45
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman, C., Rombel, I., North, A.K., Bustamante, C. Kustu, S. (1997) Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 275 : 1658 1661.
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamante, C.4    Kustu, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.