메뉴 건너뛰기




Volumn 49, Issue 3, 2010, Pages 470-477

The length of the bound fatty acid influences the dynamics of the acyl carrier protein and the stability of the thioester bond

Author keywords

[No Author keywords available]

Indexed keywords

ACYL CARRIER PROTEINS; ACYL-ACP; BIPHASIC; CONFORMATIONAL FLEXIBILITY; DYNAMIC MOTIONS; EXCHANGE RATES; FATTY ACID BINDING; FATTY ACID BIOSYNTHESIS; LINEAR CORRELATION; NMR STRUCTURES; NMR STUDIES; POSITIVE CORRELATIONS; PROTEIN MOTION; RELAXATION DISPERSION; THIOESTERS; TIME-SCALES; TWO-STATE MODEL;

EID: 74949114946     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9014659     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 0027291426 scopus 로고
    • Regulation of fatty acid biosynthesis in Escherichia coli
    • Magnuson, K., Jackowski, S., Rock, C. O., and Cronan, J. E. (1993) Regulation of fatty acid biosynthesis in Escherichia coli. Microbiol. Rev. 57, 522-542.
    • (1993) Microbiol. Rev , vol.57 , pp. 522-542
    • Magnuson, K.1    Jackowski, S.2    Rock, C.O.3    Cronan, J.E.4
  • 2
    • 0022524388 scopus 로고
    • An essential function for acyl carrier protein in the biosynthesis of membrane-derived oligosaccharides of Escherichia coli
    • Therisod, H., Weissborn, A., and Kennedy, E. (1986) An essential function for acyl carrier protein in the biosynthesis of membrane-derived oligosaccharides of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 83, 7236-7240.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 7236-7240
    • Therisod, H.1    Weissborn, A.2    Kennedy, E.3
  • 3
    • 0026651723 scopus 로고
    • Mechanisms of regulation of the biosynthesis of membrane-derived oligosaccharides in Escherichia coli
    • Rumley, M., Therisod, H., Weissborn, A., and Kennedy, E. (1992) Mechanisms of regulation of the biosynthesis of membrane-derived oligosaccharides in Escherichia coli. J. Biol. Chem. 267, 11806-11810.
    • (1992) J. Biol. Chem , vol.267 , pp. 11806-11810
    • Rumley, M.1    Therisod, H.2    Weissborn, A.3    Kennedy, E.4
  • 4
    • 0026747889 scopus 로고
    • Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens tetracenomycin C polyketide synthase
    • Shen, B., Summers, R. G., Gramajo, H., Bibb, M. J., and Hutchinson, C. R. (1992) Purification and characterization of the acyl carrier protein of the Streptomyces glaucescens tetracenomycin C polyketide synthase. J. Bacteriol. 174, 3818-3821.
    • (1992) J. Bacteriol , vol.174 , pp. 3818-3821
    • Shen, B.1    Summers, R.G.2    Gramajo, H.3    Bibb, M.J.4    Hutchinson, C.R.5
  • 5
    • 0029125339 scopus 로고
    • Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: A possible link between fatty acid and polyketide biosynthesis
    • Summers, R. G., Ali, A., Shen, B., Wessel, W. A., and Hutchinson, C. R. (1995) Malonyl-coenzyme A:acyl carrier protein acyltransferase of Streptomyces glaucescens: A possible link between fatty acid and polyketide biosynthesis. Biochemistry 34, 9389-9402.
    • (1995) Biochemistry , vol.34 , pp. 9389-9402
    • Summers, R.G.1    Ali, A.2    Shen, B.3    Wessel, W.A.4    Hutchinson, C.R.5
  • 6
    • 0026432638 scopus 로고
    • Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation
    • Issartel, J., Koronakis, V., and Hughes, C. (1991) Activation of Escherichia coli prohaemolysin to the mature toxin by acyl carrier protein-dependent fatty acylation. Nature 351, 759-761.
    • (1991) Nature , vol.351 , pp. 759-761
    • Issartel, J.1    Koronakis, V.2    Hughes, C.3
  • 7
    • 0025863049 scopus 로고
    • Biosynthesis of the Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine
    • Rusnak, F., Sakaitani, M., Drueckhammer, D., Reichert, J., and Walsh, C. T. (1991) Biosynthesis of the Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine. Biochemistry 30, 2916-2927.
    • (1991) Biochemistry , vol.30 , pp. 2916-2927
    • Rusnak, F.1    Sakaitani, M.2    Drueckhammer, D.3    Reichert, J.4    Walsh, C.T.5
  • 8
    • 33646443205 scopus 로고    scopus 로고
    • Modification of Brassica oil using conventional and transgenic approaches
    • Scarth, R., and Tang, J. (2006) Modification of Brassica oil using conventional and transgenic approaches. Crop Sci. 46, 1225-1236.
    • (2006) Crop Sci , vol.46 , pp. 1225-1236
    • Scarth, R.1    Tang, J.2
  • 9
    • 33644663441 scopus 로고    scopus 로고
    • Architecture of a fungal fatty acid synthase at 5 Å resolution
    • Jenni, S., Leibundgut, M., Maier, T., and Ban, N. (2006) Architecture of a fungal fatty acid synthase at 5 Å resolution. Science 311, 1263-1267.
    • (2006) Science , vol.311 , pp. 1263-1267
    • Jenni, S.1    Leibundgut, M.2    Maier, T.3    Ban, N.4
  • 10
    • 34247353309 scopus 로고    scopus 로고
    • Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase
    • Leibundgut, M., Jenni, S., Frick, C., and Ban, N. (2007) Structural basis for substrate delivery by acyl carrier protein in the yeast fatty acid synthase. Science 316, 288-290.
    • (2007) Science , vol.316 , pp. 288-290
    • Leibundgut, M.1    Jenni, S.2    Frick, C.3    Ban, N.4
  • 11
    • 0023645162 scopus 로고
    • 1H heteronuclear nuclear Overhauser effect studies of the acyl chain-binding site of acyl carrier protein
    • 1H heteronuclear nuclear Overhauser effect studies of the acyl chain-binding site of acyl carrier protein. J. Biol. Chem. 262, 8963-8965.
    • (1987) J. Biol. Chem , vol.262 , pp. 8963-8965
    • Jones, P.J.1    Cioffi, E.A.2    Prestegard, J.H.3
  • 12
    • 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. (2007) 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, 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
  • 13
  • 14
    • 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. (2006) Solution structures of spinach acyl carrier protein with decanoate and stearate. Biochemistry 45, 5217-5227.
    • (2006) Biochemistry , vol.45 , pp. 5217-5227
    • Zornetzer, G.A.1    Fox, B.G.2    Markley, J.L.3
  • 15
    • 0028882690 scopus 로고
    • Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase
    • Lambalot, R. H., and Walsh, C. T. (1995) Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J. Biol. Chem. 270, 24658-24661.
    • (1995) J. Biol. Chem , vol.270 , pp. 24658-24661
    • Lambalot, R.H.1    Walsh, C.T.2
  • 16
    • 0018291891 scopus 로고
    • Solubilization, purification, and salt activation of acyl-acyl carrier protein synthetase from Escherichia coli
    • Rock, C. O., and Cronan, J. E. J. (1979) Solubilization, purification, and salt activation of acyl-acyl carrier protein synthetase from Escherichia coli. J. Biol. Chem. 254, 7116-7122.
    • (1979) J. Biol. Chem , vol.254 , pp. 7116-7122
    • Rock, C.O.1    Cronan, J.E.J.2
  • 17
    • 33645381028 scopus 로고    scopus 로고
    • Preparation of isotopically labeled spinach acyl-acyl carrier protein for NMR structural studies
    • Zornetzer, G. A., White, R. D., Markley, J. L., and Fox, B. G. (2005) Preparation of isotopically labeled spinach acyl-acyl carrier protein for NMR structural studies. Protein Expression Purif. 46, 446-455.
    • (2005) Protein Expression Purif , vol.46 , pp. 446-455
    • Zornetzer, G.A.1    White, R.D.2    Markley, J.L.3    Fox, B.G.4
  • 19
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria, J. P., Rance, M., and Palmer, A. G., III (1999) A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121, 2331-2332.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 20
    • 0032719427 scopus 로고    scopus 로고
    • A TROSY CPMG sequence for characterizing chemical exchange in large proteins
    • Loria, J. P., Rance, M., and Palmer, A. G., III (1999) A TROSY CPMG sequence for characterizing chemical exchange in large proteins. J. Biomol. NMR 15, 151-155.
    • (1999) J. Biomol. NMR , vol.15 , pp. 151-155
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 21
    • 0038068865 scopus 로고    scopus 로고
    • FAST-Model Free: A program for rapid automated analysis of solution NMR spin-relaxation data
    • Cole, R., and Loria, J. P. (2003) FAST-Model Free: A program for rapid automated analysis of solution NMR spin-relaxation data. J. Biomol. NMR 26, 203-213.
    • (2003) J. Biomol. NMR , vol.26 , pp. 203-213
    • Cole, R.1    Loria, J.P.2
  • 22
    • 0022536757 scopus 로고
    • Analysis of biological thiols: Determination of thiol components of disulfides and thioesters
    • Fenton, S. S., and Fahey, R. C. (1986) Analysis of biological thiols: Determination of thiol components of disulfides and thioesters. Anal. Biochem. 154, 34-42.
    • (1986) Anal. Biochem , vol.154 , pp. 34-42
    • Fenton, S.S.1    Fahey, R.C.2
  • 23
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 24
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy
    • Palmer, A. G., III, Rance, M., and Wright, P. E. (1991) Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. J. Am. Chem. Soc. 113, 4371-4380.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 4371-4380
    • Palmer III, A.G.1    Rance, M.2    Wright, P.E.3
  • 25
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G., III (1995) Backbone dynamics of Escherichia coli ribonuclease HI correlations with structure and function in an active enzyme. J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 26
    • 0007074567 scopus 로고
    • AX3 spin system dynamics from forbidden cross peaks in double-quantum two-dimensional NMR experiments writh application to acyl carrier protein
    • Kay, L. E., Holak, T. A., and Prestegard, J. H. (1988)AX3 spin system dynamics from forbidden cross peaks in double-quantum two-dimensional NMR experiments writh application to acyl carrier protein. J. Magn. Reson. 76, 30-40.
    • (1988) J. Magn. Reson , vol.76 , pp. 30-40
    • Kay, L.E.1    Holak, T.A.2    Prestegard, J.H.3
  • 27
    • 0024435205 scopus 로고
    • A dynamic model for the structure of acyl carrier protein in solution
    • Kim, Y., and Prestegard, J. H. (1989) A dynamic model for the structure of acyl carrier protein in solution. Biochemistry 28, 8792-8797.
    • (1989) Biochemistry , vol.28 , pp. 8792-8797
    • Kim, Y.1    Prestegard, J.H.2
  • 28
    • 0025279274 scopus 로고
    • Motional effects on NMR structural data. comparison of spinach and Escherichia coli acyl carrier proteins
    • Kim, Y., Ohlrogge, J. B., and Prestegard, J. H. (1990) Motional effects on NMR structural data. comparison of spinach and Escherichia coli acyl carrier proteins. Biochem. Pharmacol. 40, 7-13.
    • (1990) Biochem. Pharmacol , vol.40 , pp. 7-13
    • Kim, Y.1    Ohlrogge, J.B.2    Prestegard, J.H.3
  • 29
    • 0025087892 scopus 로고
    • Demonstration of a conformational equilibrium in acyl carrier protein from spinach using rotating frame nuclear magnetic resonance spectroscopy
    • Kim, Y., and Prestegard, J. H. (1990) Demonstration of a conformational equilibrium in acyl carrier protein from spinach using rotating frame nuclear magnetic resonance spectroscopy. J. Am. Chem. Soc. 112, 3707-3709.
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 3707-3709
    • Kim, Y.1    Prestegard, J.H.2
  • 30
    • 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. (1995) Amide exchange rates in Escherichia coli acyl carrier protein: Correlation with protein structure and dynamics. Protein Sci. 4, 983-993.
    • (1995) Protein Sci , vol.4 , pp. 983-993
    • Andrec, M.1    Hill, R.B.2    Prestegard, J.H.3
  • 31
    • 0018257119 scopus 로고
    • Acyl carrier protein from Escherichia coli: Characterization by proton and fluorine-19 nuclear magnetic resonance and evidence for restricted mobility of the fatty acid chain in tetradecanoyl-acyl- carrier protein
    • Gally, H. U., Spencer, A. K., Armitage, I. M., Prestegard, J. H., and Cronan, J. E. J. (1978) Acyl carrier protein from Escherichia coli: Characterization by proton and fluorine-19 nuclear magnetic resonance and evidence for restricted mobility of the fatty acid chain in tetradecanoyl-acyl- carrier protein. Biochemistry 17, 5377-5382.
    • (1978) Biochemistry , vol.17 , pp. 5377-5382
    • Gally, H.U.1    Spencer, A.K.2    Armitage, I.M.3    Prestegard, J.H.4    Cronan, J.E.J.5
  • 32
    • 0023270634 scopus 로고
    • NMRpseudoenergy approach to the solution structure of acyl carrier protein
    • Holak, T. A., Prestegard, J. H., and Forman, J. D. (1987) NMRpseudoenergy approach to the solution structure of acyl carrier protein. Biochemistry 26, 4652-4660.
    • (1987) Biochemistry , vol.26 , pp. 4652-4660
    • Holak, T.A.1    Prestegard, J.H.2    Forman, J.D.3
  • 33
    • 0141857473 scopus 로고    scopus 로고
    • Inorganic anionic oxygen-containing α-nucleophiles: Effective acyl group acceptors: Hydroxylamine ranks first among the R-nucleophile series
    • Simanenko, Y., Popov, A., Prokop'eva, T., Karpichev, E., Savelova, V., Suprun, I., and Bunton, C. (2002) Inorganic anionic oxygen-containing α-nucleophiles: Effective acyl group acceptors: Hydroxylamine ranks first among the R-nucleophile series. Russ. J. Org. Chem. 38, 1286-1298.
    • (2002) Russ. J. Org. Chem , vol.38 , pp. 1286-1298
    • Simanenko, Y.1    Popov, A.2    Prokop'eva, T.3    Karpichev, E.4    Savelova, V.5    Suprun, I.6    Bunton, C.7
  • 34
    • 17044401342 scopus 로고    scopus 로고
    • Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis
    • McElheny, D., Schnell, J. R., Lansing, J. C., Dyson, H. J., and Wright, P. E. (2005) Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. Proc. Natl. Acad. Sci. U.S.A. 102, 5032-5037.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 5032-5037
    • McElheny, D.1    Schnell, J.R.2    Lansing, J.C.3    Dyson, H.J.4    Wright, P.E.5
  • 37
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong, H. C., Liu, G., Zhang, Y., Rock, C. O., and Zheng, J. (2002) The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277, 15874-15880.
    • (2002) J. Biol. Chem , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.2    Zhang, Y.3    Rock, C.O.4    Zheng, J.5
  • 38
    • 33644697200 scopus 로고    scopus 로고
    • Architecture of mammalian fatty acid synthase at 4.5 Å resolution
    • Maier, T., Jenni, S., and Ban, N. (2006) Architecture of mammalian fatty acid synthase at 4.5 Å resolution. Science 311, 1258-1262.
    • (2006) Science , vol.311 , pp. 1258-1262
    • Maier, T.1    Jenni, S.2    Ban, N.3
  • 39
    • 34147098650 scopus 로고    scopus 로고
    • The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together
    • Lomakin, I. B., Xiong, Y., and Steitz, T. A. (2007) The crystal structure of yeast fatty acid synthase, a cellular machine with eight active sites working together. Cell 129, 319-332.
    • (2007) Cell , vol.129 , pp. 319-332
    • Lomakin, I.B.1    Xiong, Y.2    Steitz, T.A.3
  • 41
    • 38049136859 scopus 로고    scopus 로고
    • A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains
    • Płoskoń, E., Arthur, C. J., Evans, S. E., Williams, C., Crosby, J., Simpson, T. J., and Crump, M. P. (2008) A mammalian type I fatty acid synthase acyl carrier protein domain does not sequester acyl chains. J. Biol. Chem. 283, 518-528.
    • (2008) J. Biol. Chem , vol.283 , pp. 518-528
    • Płoskoń, E.1    Arthur, C.J.2    Evans, S.E.3    Williams, C.4    Crosby, J.5    Simpson, T.J.6    Crump, M.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.