메뉴 건너뛰기




Volumn 2, Issue 9, 2006, Pages 494-502

Biosynthesis of Dictyostelium discoideum differentiation-inducing factor by a hybrid type I fatty acid-type III polyketide synthase

Author keywords

[No Author keywords available]

Indexed keywords

DIFFERENTIATION INDUCING FACTOR; FATTY ACID; FATTY ACID SYNTHASE; HYBRID PROTEIN; PHLOROGLUCINOL; POLYKETIDE; POLYKETIDE SYNTHASE; THIOL ESTER HYDROLASE;

EID: 33747598945     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio811     Document Type: Article
Times cited : (96)

References (40)
  • 1
    • 0003968192 scopus 로고    scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Kessin, R.H. Dictyostelium (Cambridge University Press, Cambridge, UK, 2001).
    • (2001) Dictyostelium
    • Kessin, R.H.1
  • 2
    • 0023240287 scopus 로고
    • Chemical structure of the morphogen differentiation inducing factor from Dictyostelium discoideum
    • Morris, H.R., Taylor, G.W., Masento, M.S., Jermyn, K.A. & Kay, R.R. Chemical structure of the morphogen differentiation inducing factor from Dictyostelium discoideum. Nature 328, 811-814 (1987).
    • (1987) Nature , vol.328 , pp. 811-814
    • Morris, H.R.1    Taylor, G.W.2    Masento, M.S.3    Jermyn, K.A.4    Kay, R.R.5
  • 3
    • 0034517148 scopus 로고    scopus 로고
    • The role of DIF-1 signaling in Dictyostelium development
    • Thompson, C.R. & Kay, R.R. The role of DIF-1 signaling in Dictyostelium development. Mol. Cell 6, 1509-1514 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1509-1514
    • Thompson, C.R.1    Kay, R.R.2
  • 4
    • 23044435107 scopus 로고    scopus 로고
    • Structural requirements of Dictyostelium differentiation-inducing factors for their stalk-cell-inducing activity in Dictyostelium cells and anti-proliferative activity in K562 human leukemic cells
    • Gokan, N. et al. Structural requirements of Dictyostelium differentiation-inducing factors for their stalk-cell-inducing activity in Dictyostelium cells and anti-proliferative activity in K562 human leukemic cells. Biochem. Pharmacol. 70, 676-685 (2005).
    • (2005) Biochem. Pharmacol. , vol.70 , pp. 676-685
    • Gokan, N.1
  • 5
    • 0032579553 scopus 로고    scopus 로고
    • The biosynthesis of differentiation-inducing factor, a chlorinated signal molecule regulating Dictyostelium development
    • Kay, R.R. The biosynthesis of differentiation-inducing factor, a chlorinated signal molecule regulating Dictyostelium development. J. Biol. Chem. 273, 2669-2675 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2669-2675
    • Kay, R.R.1
  • 6
    • 0032805888 scopus 로고    scopus 로고
    • Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis
    • Ferrer, J.L., Jez, J.M., Bowman, M.E., Dixon, R.A. & Noel, J.P. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Nat. Struct. Biol. 6, 775-784 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 775-784
    • Ferrer, J.L.1    Jez, J.M.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 7
    • 0001834930 scopus 로고    scopus 로고
    • The family of chalcone synthase-related proteins: Functional diversity and evolution
    • Schröder, J. The family of chalcone synthase-related proteins: functional diversity and evolution. Recent Adv. Phytochem. 34, 55-89 (2000).
    • (2000) Recent Adv. Phytochem. , vol.34 , pp. 55-89
    • Schröder, J.1
  • 8
    • 0037319699 scopus 로고    scopus 로고
    • The chalcone synthase superfamily of type III polyketide synthases
    • Austin, M.B. & Noel, J.P. The chalcone synthase superfamily of type III polyketide synthases. Nat. Prod. Rep. 20, 79-110 (2003).
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 79-110
    • Austin, M.B.1    Noel, J.P.2
  • 9
    • 18344395923 scopus 로고    scopus 로고
    • The genome of the social amoeba Dictyostelium discoideum
    • Eichinger, L. et al. The genome of the social amoeba Dictyostelium discoideum. Nature 435, 43-57 (2005).
    • (2005) Nature , vol.435 , pp. 43-57
    • Eichinger, L.1
  • 10
    • 12344283741 scopus 로고    scopus 로고
    • Structure and function of animal fatty acid synthase
    • Chirala, S.S. & Wakil, S.J. Structure and function of animal fatty acid synthase. Lipids 39, 1045-1053 (2004).
    • (2004) Lipids , vol.39 , pp. 1045-1053
    • Chirala, S.S.1    Wakil, S.J.2
  • 11
    • 17844385334 scopus 로고    scopus 로고
    • Structure and molecular organization of mammalian fatty acid synthase
    • Asturias, F.J. et al. Structure and molecular organization of mammalian fatty acid synthase. Nat. Struct. Mol. Biol. 12, 225-232 (2005).
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 225-232
    • Asturias, F.J.1
  • 12
    • 33644697200 scopus 로고    scopus 로고
    • Architecture of mammalian fatty synthase at 4.5 A resolution
    • Maier, T., Jenni, S. & Ban, N. Architecture of mammalian fatty synthase at 4.5 A resolution. Science 311, 1258-1262 (2006).
    • (2006) Science , vol.311 , pp. 1258-1262
    • Maier, T.1    Jenni, S.2    Ban, N.3
  • 14
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • Staunton, J. & Weissman, K.J. Polyketide biosynthesis: a millennium review. Nat. Prod. Rep. 18, 380-416 (2001).
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 15
    • 0034526571 scopus 로고    scopus 로고
    • Structural control of polyketide formation in plant-specific polyketide synthases
    • Jez, J.M. et al. Structural control of polyketide formation in plant-specific polyketide synthases. Chem. Biol. 7, 919-930 (2000).
    • (2000) Chem. Biol. , vol.7 , pp. 919-930
    • Jez, J.M.1
  • 16
    • 0035846573 scopus 로고    scopus 로고
    • Structure-guided programming of polyketide chain-length determination in chalcone synthase
    • Jez, J.M., Bowman, M.E. & Noel, J.P. Structure-guided programming of polyketide chain-length determination in chalcone synthase. Biochemistry 40, 14829-14838 (2001).
    • (2001) Biochemistry , vol.40 , pp. 14829-14838
    • Jez, J.M.1    Bowman, M.E.2    Noel, J.P.3
  • 17
    • 0035845638 scopus 로고    scopus 로고
    • Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro
    • Rangan, V.S., Joshi, A.K. & Smith, S. Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 40, 10792-10799 (2001).
    • (2001) Biochemistry , vol.40 , pp. 10792-10799
    • Rangan, V.S.1    Joshi, A.K.2    Smith, S.3
  • 18
    • 0033780306 scopus 로고    scopus 로고
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: An integrated peptide-polyketide synthetase system
    • Tillett, D. et al. Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC7806: an integrated peptide-polyketide synthetase system. Chem. Biol. 7, 753-764 (2000).
    • (2000) Chem. Biol. , vol.7 , pp. 753-764
    • Tillett, D.1
  • 19
    • 0035909913 scopus 로고    scopus 로고
    • Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel
    • Tsai, S.C. et al. Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel. Proc. Natl. Acad. Sci. USA 98, 14808-14813 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14808-14813
    • Tsai, S.C.1
  • 20
    • 0020027102 scopus 로고
    • Developmental regulation of stalk cell differentiation-inducing factor in Dictyostelium discoideum
    • Brookman, J.J., Town, C.D., Jermyn, K.A. & Kay, R.R. Developmental regulation of stalk cell differentiation-inducing factor in Dictyostelium discoideum. Dev. Biol. 91, 191-196 (1982).
    • (1982) Dev. Biol. , vol.91 , pp. 191-196
    • Brookman, J.J.1    Town, C.D.2    Jermyn, K.A.3    Kay, R.R.4
  • 21
    • 0028925391 scopus 로고
    • The proximal pathway of metabolism of the chlorinated signal molecule differentiation-inductin factor-1 (DIF-1) in the cellular slime mould Dictyostelium
    • Morandini, P. et al. The proximal pathway of metabolism of the chlorinated signal molecule differentiation-inductin factor-1 (DIF-1) in the cellular slime mould Dictyostelium. Biochem. J. 306, 735-743 (1995).
    • (1995) Biochem. J. , vol.306 , pp. 735-743
    • Morandini, P.1
  • 22
    • 4644270018 scopus 로고    scopus 로고
    • An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketides synthases
    • Austin, M.B., Bowman, M.E., Ferrer, J., Schröder, J. & Noel, J.P. An aldol switch discovered in stilbene synthases mediates cyclization specificity of type III polyketides synthases. Chem. Biol. 11, 1179-1194 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 1179-1194
    • Austin, M.B.1    Bowman, M.E.2    Ferrer, J.3    Schröder, J.4    Noel, J.P.5
  • 23
    • 7244239181 scopus 로고    scopus 로고
    • Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates
    • Austin, M.B. et al. Crystal structure of a bacterial type III polyketide synthase and enzymatic control of reactive polyketide intermediates. J. Biol. Chem. 279, 45162-45174 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 45162-45174
    • Austin, M.B.1
  • 24
    • 4344585355 scopus 로고    scopus 로고
    • A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites
    • Sankaranarayanan, R. et al. A novel tunnel in mycobacterial type III polyketide synthase reveals the structural basis for generating diverse metabolites. Nat. Struct. Mol. Biol. 11, 894-900 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 894-900
    • Sankaranarayanan, R.1
  • 25
    • 17444429231 scopus 로고    scopus 로고
    • Discovery of a novel superfamily of type III polyketide synthases in Aspergillus oryzae
    • Seshime, Y., Juvvadi, P.R., Fujii, I. & Kitamoto, K. Discovery of a novel superfamily of type III polyketide synthases in Aspergillus oryzae. Biochem. Biophys. Res. Commun. 331, 253-260 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 253-260
    • Seshime, Y.1    Juvvadi, P.R.2    Fujii, I.3    Kitamoto, K.4
  • 26
    • 0023955045 scopus 로고
    • Structure elucidation of two differentiation inducing factors (DIF-2 and DIF-3) from the cellular slime mould Dictyostelium discoideum
    • Morris, H.R., Masento, M.S., Taylor, G.W., Jermyn, K.A. & Kay, R.R. Structure elucidation of two differentiation inducing factors (DIF-2 and DIF-3) from the cellular slime mould Dictyostelium discoideum. Biochem. J. 249, 903-906 (1988).
    • (1988) Biochem. J. , vol.249 , pp. 903-906
    • Morris, H.R.1    Masento, M.S.2    Taylor, G.W.3    Jermyn, K.A.4    Kay, R.R.5
  • 27
    • 20444409115 scopus 로고    scopus 로고
    • New prestalk and prespore inducing signals in Dictyostelium
    • Serafimidis, I. & Kay, R.R. New prestalk and prespore inducing signals in Dictyostelium. Dev. Biol. 282, 432-441 (2005).
    • (2005) Dev. Biol. , vol.282 , pp. 432-441
    • Serafimidis, I.1    Kay, R.R.2
  • 28
    • 0034712329 scopus 로고    scopus 로고
    • Novel acyl alpha-pyronoids, dictyopyrone A, B, and C, from Dictyostelium cellular slime molds
    • Takaya, Y. et al. Novel acyl alpha-pyronoids, dictyopyrone A, B, and C, from Dictyostelium cellular slime molds. J. Org. Chem. 65, 985-989 (2000).
    • (2000) J. Org. Chem. , vol.65 , pp. 985-989
    • Takaya, Y.1
  • 29
    • 10644281452 scopus 로고    scopus 로고
    • Head-to-head coiled arrangement of the subunits of the animal fatty acid synthase
    • Witkowski, A. et al. Head-to-head coiled arrangement of the subunits of the animal fatty acid synthase. Chem. Biol. 11, 1667-1676 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 1667-1676
    • Witkowski, A.1
  • 30
    • 27144509740 scopus 로고    scopus 로고
    • Combinatorial polyketide biosynthesis by de novo design and rearrangement of modular polyketide synthase genes
    • Menzella, H.G. et al. Combinatorial polyketide biosynthesis by de novo design and rearrangement of modular polyketide synthase genes. Nat. Biotechnol. 23, 1171-1176 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1171-1176
    • Menzella, H.G.1
  • 31
    • 1642299704 scopus 로고    scopus 로고
    • The first plant type III polyketide synthase that catalyzes formation of aromatic heptaketide
    • Abe, I., Utsumi, Y., Oguro, S. & Noguchi, H. The first plant type III polyketide synthase that catalyzes formation of aromatic heptaketide. FEBS Lett. 562, 171-176 (2004).
    • (2004) FEBS Lett. , vol.562 , pp. 171-176
    • Abe, I.1    Utsumi, Y.2    Oguro, S.3    Noguchi, H.4
  • 32
    • 13444282087 scopus 로고    scopus 로고
    • A plant type III polyketide synthase that produces pentaketide chromone
    • Abe, I. et al. A plant type III polyketide synthase that produces pentaketide chromone. J. Am. Chem. Soc. 127, 1362-1363 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1362-1363
    • Abe, I.1
  • 33
    • 4644250460 scopus 로고    scopus 로고
    • Enzymatic formation of long-chain polyketide pyrones by plant type III polyketide synthases
    • Abe, I., Watanabe, T. & Noguchi, H. Enzymatic formation of long-chain polyketide pyrones by plant type III polyketide synthases. Phytochemistry 65, 2447-2453 (2004).
    • (2004) Phytochemistry , vol.65 , pp. 2447-2453
    • Abe, I.1    Watanabe, T.2    Noguchi, H.3
  • 34
    • 0034620559 scopus 로고    scopus 로고
    • Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase
    • Jez, J.M., Ferrer, J.L., Bowman, M.E., Dixon, R.A. & Noel, J.P. Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry 39, 890-902 (2000).
    • (2000) Biochemistry , vol.39 , pp. 890-902
    • Jez, J.M.1    Ferrer, J.L.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 35
    • 0037085447 scopus 로고    scopus 로고
    • Properties and substrate specificity of RppA, a chalcone synthase- related polyketide synthase in Streptomyces griseus
    • Funa, N., Ohnishi, Y., Ebizuka, Y. & Horinouchi, S. Properties and substrate specificity of RppA, a chalcone synthase- related polyketide synthase in Streptomyces griseus. J. Biol. Chem. 277, 4628-4635 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 4628-4635
    • Funa, N.1    Ohnishi, Y.2    Ebizuka, Y.3    Horinouchi, S.4
  • 36
    • 0023063763 scopus 로고
    • Cell differentiation in monolayers and the investigation of slime mold morphogens
    • Kay, R.R. Cell differentiation in monolayers and the investigation of slime mold morphogens. Methods Cell Biol. 28, 433-448 (1987).
    • (1987) Methods Cell Biol. , vol.28 , pp. 433-448
    • Kay, R.R.1
  • 37
    • 1542395142 scopus 로고    scopus 로고
    • Rapid generation of gene disruption constructs by in vitro transposition and identification of a Dictyostelium protein kinase that regulates its rate of growth and development
    • Abe, T., Langenick, J. & Williams, J.G. Rapid generation of gene disruption constructs by in vitro transposition and identification of a Dictyostelium protein kinase that regulates its rate of growth and development. Nucleic Acids Res. 31, e107 (2003).
    • (2003) Nucleic Acids Res. , vol.31
    • Abe, T.1    Langenick, J.2    Williams, J.G.3
  • 38
    • 0033568918 scopus 로고    scopus 로고
    • Identification of delta5-fatty acid desaturase from the cellular slime mold Dictyostelium discoideum
    • Saito, T. & Ochiai, H. Identification of delta5-fatty acid desaturase from the cellular slime mold Dictyostelium discoideum. Eur. J. Biochem. 265, 809-814 (1999).
    • (1999) Eur. J. Biochem. , vol.265 , pp. 809-814
    • Saito, T.1    Ochiai, H.2
  • 39
    • 0023791673 scopus 로고
    • Differentiation-inducing factor from the slime mould Dictyostelium discoideum and its analogues
    • Masento, M.S. et al. Differentiation-inducing factor from the slime mould Dictyostelium discoideum and its analogues. Biochem. J. 256, 23-28 (1988).
    • (1988) Biochem. J. , vol.256 , pp. 23-28
    • Masento, M.S.1
  • 40
    • 0030841590 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4: Providing programs for protein crystallography
    • Dodson, E.J., Winn, M. & Ralph, A. Collaborative Computational Project, Number 4: providing programs for protein crystallography. Methods Enzymol. 277, 620-633 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 620-633
    • Dodson, E.J.1    Winn, M.2    Ralph, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.