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Volumn 1784, Issue 11, 2008, Pages 1835-1843

Tryptophan fluorescence reveals induced folding of Vibrio harveyi acyl carrier protein upon interaction with partner enzymes

Author keywords

Acyl carrier protein; Acylation; Circular dichroism; Electrophoresis; Fluorescence; Natively unfolded protein

Indexed keywords

ACRYLAMIDE; ACYL CARRIER PROTEIN; FATTY ACID; MAGNESIUM; TRYPTOPHAN;

EID: 54049114203     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.07.017     Document Type: Article
Times cited : (8)

References (47)
  • 1
    • 38849098884 scopus 로고    scopus 로고
    • Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family
    • Byers D.M., and Gong H. Acyl carrier protein: structure-function relationships in a conserved multifunctional protein family. Biochem. Cell Biol. 85 (2007) 649-662
    • (2007) Biochem. Cell Biol. , vol.85 , pp. 649-662
    • Byers, D.M.1    Gong, H.2
  • 2
    • 22244466130 scopus 로고    scopus 로고
    • The structural biology of type II fatty acid biosynthesis
    • White S.W., Zheng J., Zhang Y.M., and Rock C.O. The structural biology of type II fatty acid biosynthesis. Annu. Rev. Biochem. 74 (2005) 791-831
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 791-831
    • White, S.W.1    Zheng, J.2    Zhang, Y.M.3    Rock, C.O.4
  • 3
    • 0020351537 scopus 로고
    • Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo
    • Rock C.O., and Jackowski S. Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo. J. Biol. Chem. 257 (1982) 10759-10765
    • (1982) J. Biol. Chem. , vol.257 , pp. 10759-10765
    • Rock, C.O.1    Jackowski, S.2
  • 4
    • 0023654454 scopus 로고
    • Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine
    • Anderson M.S., and Raetz C.R. Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. J. Biol. Chem. 262 (1987) 5159-5169
    • (1987) J. Biol. Chem. , vol.262 , pp. 5159-5169
    • Anderson, M.S.1    Raetz, C.R.2
  • 5
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan S.W., and Cronan Jr. J.E. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272 (1997) 17903-17906
    • (1997) J. Biol. Chem. , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan Jr., J.E.2
  • 6
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel J.P., Koronakis V., and Hughes C. Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351 (1991) 759-761
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.P.1    Koronakis, V.2    Hughes, C.3
  • 7
    • 0029817781 scopus 로고    scopus 로고
    • Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein
    • Schaefer A.L., Val D.L., Hanzelka B.L., Cronan Jr. J.E., and Greenberg E.P. Generation of cell-to-cell signals in quorum sensing: acyl homoserine lactone synthase activity of a purified Vibrio fischeri LuxI protein. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 9505-9509
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 9505-9509
    • Schaefer, A.L.1    Val, D.L.2    Hanzelka, B.L.3    Cronan Jr., J.E.4    Greenberg, E.P.5
  • 8
    • 0022410208 scopus 로고
    • Acyl-acyl carrier protein as a source of fatty acids for bacterial bioluminescence
    • Byers D.M., and Meighen E.A. Acyl-acyl carrier protein as a source of fatty acids for bacterial bioluminescence. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 6085-6089
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 6085-6089
    • Byers, D.M.1    Meighen, E.A.2
  • 9
    • 33845562808 scopus 로고    scopus 로고
    • Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis
    • Lai J.R., Koglin A., and Walsh C.T. Carrier protein structure and recognition in polyketide and nonribosomal peptide biosynthesis. Biochemistry 45 (2006) 14869-14879
    • (2006) Biochemistry , vol.45 , pp. 14869-14879
    • Lai, J.R.1    Koglin, A.2    Walsh, C.T.3
  • 11
    • 33745817391 scopus 로고    scopus 로고
    • Inhibiting bacterial fatty acid synthesis
    • Zhang Y.M., White S.W., and Rock C.O. Inhibiting bacterial fatty acid synthesis. J. Biol. Chem. 281 (2006) 17541-17544
    • (2006) J. Biol. Chem. , vol.281 , pp. 17541-17544
    • Zhang, Y.M.1    White, S.W.2    Rock, C.O.3
  • 12
    • 0025613125 scopus 로고
    • Refinement of the NMR structures for acyl carrier protein with scalar coupling data
    • Kim Y., and Prestegard J.H. Refinement of the NMR structures for acyl carrier protein with scalar coupling data. Proteins 8 (1990) 377-385
    • (1990) Proteins , vol.8 , pp. 377-385
    • Kim, Y.1    Prestegard, J.H.2
  • 13
    • 33751512907 scopus 로고    scopus 로고
    • Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates
    • Roujeinikova A., Simon W.J., Gilroy J., Rice D.W., Rafferty J.B., and Slabas A.R. Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates. J. Mol. Biol. 365 (2007) 135-145
    • (2007) J. Mol. Biol. , vol.365 , pp. 135-145
    • Roujeinikova, A.1    Simon, W.J.2    Gilroy, J.3    Rice, D.W.4    Rafferty, J.B.5    Slabas, A.R.6
  • 15
    • 33645968397 scopus 로고    scopus 로고
    • Solution structures of spinach acyl carrier protein with decanoate and stearate
    • Zornetzer G.A., Fox B.G., and Markley J.L. Solution structures of spinach acyl carrier protein with decanoate and stearate. Biochemistry 45 (2006) 5217-5227
    • (2006) Biochemistry , vol.45 , pp. 5217-5227
    • Zornetzer, G.A.1    Fox, B.G.2    Markley, J.L.3
  • 17
    • 0018787017 scopus 로고
    • Preparative enzymatic synthesis and hydrophobic chromatography of acyl-acyl carrier protein
    • Rock C.O., and Garwin J.L. Preparative enzymatic synthesis and hydrophobic chromatography of acyl-acyl carrier protein. J. Biol. Chem. 254 (1979) 7123-7128
    • (1979) J. Biol. Chem. , vol.254 , pp. 7123-7128
    • Rock, C.O.1    Garwin, J.L.2
  • 18
    • 0020478991 scopus 로고
    • Molecular properties of short chain acyl thioesters of acyl carrier protein
    • Cronan Jr. J.E. Molecular properties of short chain acyl thioesters of acyl carrier protein. J. Biol. Chem. 257 (1982) 5013-5017
    • (1982) J. Biol. Chem. , vol.257 , pp. 5013-5017
    • Cronan Jr., J.E.1
  • 19
    • 31744434177 scopus 로고    scopus 로고
    • NMR studies of Escherichia coli acyl carrier protein: dynamic and structural differences of the apo- and holo-forms
    • Kim Y., Kovrigin E.L., and Eletr Z. NMR studies of Escherichia coli acyl carrier protein: dynamic and structural differences of the apo- and holo-forms. Biochem. Biophys. Res. Commun. 341 (2006) 776-783
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 776-783
    • Kim, Y.1    Kovrigin, E.L.2    Eletr, Z.3
  • 20
    • 0028943591 scopus 로고
    • Amide exchange rates in Escherichia coli acyl carrier protein: correlation with protein structure and dynamics
    • Andrec M., Hill R.B., and Prestegard J.H. Amide exchange rates in Escherichia coli acyl carrier protein: correlation with protein structure and dynamics. Protein Sci. 4 (1995) 983-993
    • (1995) Protein Sci. , vol.4 , pp. 983-993
    • Andrec, M.1    Hill, R.B.2    Prestegard, J.H.3
  • 21
    • 0034662753 scopus 로고    scopus 로고
    • Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
    • Parris K.D., Lin L., Tam A., Mathew R., Hixon J., Stahl M., Fritz C.C., Seehra J., and Somers W.S. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Structure 8 (2000) 883-895
    • (2000) Structure , vol.8 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5    Stahl, M.6    Fritz, C.C.7    Seehra, J.8    Somers, W.S.9
  • 23
    • 0037238269 scopus 로고    scopus 로고
    • The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase
    • Zhang Y.M., Marrakchi H., White S.W., and Rock C.O. The application of computational methods to explore the diversity and structure of bacterial fatty acid synthase. J. Lipid Res. 44 (2003) 1-10
    • (2003) J. Lipid Res. , vol.44 , pp. 1-10
    • Zhang, Y.M.1    Marrakchi, H.2    White, S.W.3    Rock, C.O.4
  • 24
    • 0035896547 scopus 로고    scopus 로고
    • Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III
    • Zhang Y.M., Rao M.S., Heath R.J., Price A.C., Olson A.J., Rock C.O., and White S.W. Identification and analysis of the acyl carrier protein (ACP) docking site on beta-ketoacyl-ACP synthase III. J. Biol. Chem. 276 (2001) 8231-8238
    • (2001) J. Biol. Chem. , vol.276 , pp. 8231-8238
    • Zhang, Y.M.1    Rao, M.S.2    Heath, R.J.3    Price, A.C.4    Olson, A.J.5    Rock, C.O.6    White, S.W.7
  • 25
    • 0037435617 scopus 로고    scopus 로고
    • Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions
    • Worsham L.M., Earls L., Jolly C., Langston K.G., Trent M.S., and Ernst-Fonberg M.L. Amino acid residues of Escherichia coli acyl carrier protein involved in heterologous protein interactions. Biochemistry 42 (2003) 167-176
    • (2003) Biochemistry , vol.42 , pp. 167-176
    • Worsham, L.M.1    Earls, L.2    Jolly, C.3    Langston, K.G.4    Trent, M.S.5    Ernst-Fonberg, M.L.6
  • 26
    • 0037470457 scopus 로고    scopus 로고
    • Glutamate-41 of Vibrio harveyi acyl carrier protein is essential for fatty acid synthase but not acyl-ACP synthetase activity
    • Gong H., and Byers D.M. Glutamate-41 of Vibrio harveyi acyl carrier protein is essential for fatty acid synthase but not acyl-ACP synthetase activity. Biochem. Biophys. Res. Commun. 302 (2003) 35-40
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 35-40
    • Gong, H.1    Byers, D.M.2
  • 27
    • 33947504254 scopus 로고    scopus 로고
    • Neutralization of acidic residues in helix II stabilizes the folded conformation of acyl carrier protein and variably alters its function with different enzymes
    • Gong H., Murphy A., McMaster C.R., and Byers D.M. Neutralization of acidic residues in helix II stabilizes the folded conformation of acyl carrier protein and variably alters its function with different enzymes. J. Biol. Chem. 282 (2007) 4494-4503
    • (2007) J. Biol. Chem. , vol.282 , pp. 4494-4503
    • Gong, H.1    Murphy, A.2    McMaster, C.R.3    Byers, D.M.4
  • 28
    • 0023731129 scopus 로고
    • Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR
    • Frederick A.F., Kay L.E., and Prestegard J.H. Location of divalent ion sites in acyl carrier protein using relaxation perturbed 2D NMR. FEBS Lett. 238 (1988) 43-48
    • (1988) FEBS Lett. , vol.238 , pp. 43-48
    • Frederick, A.F.1    Kay, L.E.2    Prestegard, J.H.3
  • 29
    • 0025359364 scopus 로고
    • Divalent cation binding to reduced and octanoyl acyl-carrier protein
    • Tener D.M., and Mayo K.H. Divalent cation binding to reduced and octanoyl acyl-carrier protein. Eur. J. Biochem. 189 (1990) 559-565
    • (1990) Eur. J. Biochem. , vol.189 , pp. 559-565
    • Tener, D.M.1    Mayo, K.H.2
  • 30
    • 0016628149 scopus 로고
    • On the structure-function relationship of acyl carrier protein of Escherichia coli
    • Schulz H. On the structure-function relationship of acyl carrier protein of Escherichia coli. J. Biol. Chem. 250 (1975) 2299-2304
    • (1975) J. Biol. Chem. , vol.250 , pp. 2299-2304
    • Schulz, H.1
  • 31
    • 0035929665 scopus 로고    scopus 로고
    • Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity
    • Flaman A.S., Chen J.M., Van Iderstine S.C., and Byers D.M. Site-directed mutagenesis of acyl carrier protein (ACP) reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity. J. Biol. Chem. 276 (2001) 35934-35939
    • (2001) J. Biol. Chem. , vol.276 , pp. 35934-35939
    • Flaman, A.S.1    Chen, J.M.2    Van Iderstine, S.C.3    Byers, D.M.4
  • 32
    • 1942488270 scopus 로고    scopus 로고
    • pH-induced conformational transition of H. pylori acyl carrier protein: insight into the unfolding of local structure
    • Park S.J., Kim J.S., Son W.S., and Lee B.J. pH-induced conformational transition of H. pylori acyl carrier protein: insight into the unfolding of local structure. J. Biochem. 135 (2004) 337-346
    • (2004) J. Biochem. , vol.135 , pp. 337-346
    • Park, S.J.1    Kim, J.S.2    Son, W.S.3    Lee, B.J.4
  • 33
    • 0031419005 scopus 로고    scopus 로고
    • Holo-[acyl-carrier-protein] synthase of Escherichia coli
    • Lambalot R.H., and Walsh C.T. Holo-[acyl-carrier-protein] synthase of Escherichia coli. Methods Enzymol. 279 (1997) 254-262
    • (1997) Methods Enzymol. , vol.279 , pp. 254-262
    • Lambalot, R.H.1    Walsh, C.T.2
  • 34
    • 0027403760 scopus 로고
    • Purification and characterization of fatty acyl-acyl carrier protein synthetase from Vibrio harveyi
    • Fice D., Shen Z., and Byers D.M. Purification and characterization of fatty acyl-acyl carrier protein synthetase from Vibrio harveyi. J. Bacteriol. 175 (1993) 1865-1870
    • (1993) J. Bacteriol. , vol.175 , pp. 1865-1870
    • Fice, D.1    Shen, Z.2    Byers, D.M.3
  • 35
    • 0019887843 scopus 로고
    • Molecular properties of acyl carrier protein derivatives
    • Rock C.O., Cronan Jr. J.E., and Armitage I.M. Molecular properties of acyl carrier protein derivatives. J. Biol. Chem. 256 (1981) 2669-2674
    • (1981) J. Biol. Chem. , vol.256 , pp. 2669-2674
    • Rock, C.O.1    Cronan Jr., J.E.2    Armitage, I.M.3
  • 37
    • 0037121453 scopus 로고    scopus 로고
    • Identification of a key residue in the conformational stability of acyl carrier protein
    • Keating M.M., Gong H., and Byers D.M. Identification of a key residue in the conformational stability of acyl carrier protein. Biochim. Biophys. Acta 1601 (2002) 208-214
    • (2002) Biochim. Biophys. Acta , vol.1601 , pp. 208-214
    • Keating, M.M.1    Gong, H.2    Byers, D.M.3
  • 38
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian J.T., and Callis P.R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J. 80 (2001) 2093-2109
    • (2001) Biophys. J. , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 39
    • 0027304442 scopus 로고
    • UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable
    • Anderson M.S., Bull H.G., Galloway S.M., Kelly T.M., Mohan S., Radika K., and Raetz C.R. UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable. J. Biol. Chem. 268 (1993) 19858-19865
    • (1993) J. Biol. Chem. , vol.268 , pp. 19858-19865
    • Anderson, M.S.1    Bull, H.G.2    Galloway, S.M.3    Kelly, T.M.4    Mohan, S.5    Radika, K.6    Raetz, C.R.7
  • 40
    • 0033955033 scopus 로고    scopus 로고
    • Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli
    • Flugel R.S., Hwangbo Y., Lambalot R.H., Cronan Jr. J.E., and Walsh C.T. Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli. J. Biol. Chem. 275 (2000) 959-968
    • (2000) J. Biol. Chem. , vol.275 , pp. 959-968
    • Flugel, R.S.1    Hwangbo, Y.2    Lambalot, R.H.3    Cronan Jr., J.E.4    Walsh, C.T.5
  • 41
    • 6344231261 scopus 로고    scopus 로고
    • Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein
    • Jain N.U., Wyckoff T.J., Raetz C.R., and Prestegard J.H. Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein. J. Mol. Biol. 343 (2004) 1379-1389
    • (2004) J. Mol. Biol. , vol.343 , pp. 1379-1389
    • Jain, N.U.1    Wyckoff, T.J.2    Raetz, C.R.3    Prestegard, J.H.4
  • 42
    • 0034886054 scopus 로고    scopus 로고
    • Solution structure of B. subtilis acyl carrier protein
    • Xu G.Y., Tam A., Lin L., Hixon J., Fritz C.C., and Powers R. Solution structure of B. subtilis acyl carrier protein. Structure 9 (2001) 277-287
    • (2001) Structure , vol.9 , pp. 277-287
    • Xu, G.Y.1    Tam, A.2    Lin, L.3    Hixon, J.4    Fritz, C.C.5    Powers, R.6
  • 43
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 45
    • 0021929046 scopus 로고
    • Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
    • Alatossava T., Jutte H., Kuhn A., and Kellenberger E. Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187. J. Bacteriol. 162 (1985) 413-419
    • (1985) J. Bacteriol. , vol.162 , pp. 413-419
    • Alatossava, T.1    Jutte, H.2    Kuhn, A.3    Kellenberger, E.4
  • 46
    • 34447624326 scopus 로고    scopus 로고
    • Electrospray ionization mass spectra of acyl carrier protein are insensitive to its solution phase conformation
    • Murphy P.W., Rowland E.E., and Byers D.M. Electrospray ionization mass spectra of acyl carrier protein are insensitive to its solution phase conformation. J. Am. Soc. Mass Spectrom. 18 (2007) 1525-1532
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1525-1532
    • Murphy, P.W.1    Rowland, E.E.2    Byers, D.M.3


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