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Volumn 17, Issue 1, 2008, Pages 34-42

DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: Implications for active site communication

Author keywords

Acetyl CoA carboxylase; Biotin; Carboxyltransferase; DNA binding; Zinc finger

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; BIOCYTIN; CARBOXYLTRANSFERASE; DOUBLE STRANDED DNA; HEPARIN; MALONYL COENZYME A; SINGLE STRANDED DNA;

EID: 37549033454     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073186408     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 0037033115 scopus 로고    scopus 로고
    • Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and Pim1p protease
    • Bateman, J.M., Iacovino, M., Perlman, P.S., and Butow, R.A. 2002a. Mitochondrial DNA instability mutants of the bifunctional protein Ilv5p have altered organization in mitochondria and are targeted for degradation by Hsp78 and Pim1p protease. J. Biol. Chem. 277: 47946-47953.
    • (2002) J. Biol. Chem , vol.277 , pp. 47946-47953
    • Bateman, J.M.1    Iacovino, M.2    Perlman, P.S.3    Butow, R.A.4
  • 2
    • 0036021361 scopus 로고    scopus 로고
    • Mutational bisection of the mitochondrial DNA stability and amino acid biosynthetic functions of Ilv5p of budding yeast
    • Bateman, J.M., Perlman, P.S., and Butow, R.A. 2002b. Mutational bisection of the mitochondrial DNA stability and amino acid biosynthetic functions of Ilv5p of budding yeast. Genetics 161: 1043-1052.
    • (2002) Genetics , vol.161 , pp. 1043-1052
    • Bateman, J.M.1    Perlman, P.S.2    Butow, R.A.3
  • 3
    • 21344433010 scopus 로고    scopus 로고
    • The Escherichia coli biotin regulatory system: A transcriptional switch
    • Beckett, D. 2005. The Escherichia coli biotin regulatory system: A transcriptional switch. J. Nutr. Biochem. 16: 411-415
    • (2005) J. Nutr. Biochem , vol.16 , pp. 411-415
    • Beckett, D.1
  • 4
    • 32344447009 scopus 로고    scopus 로고
    • The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme
    • Bilder, P., Lightle, S., Bainbridge, G., Ohren, J., Finzel, B., Sun, F., Holley, S., Al-Kassim, L., and Spessard, C. 2006. The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45: 1712-1722.
    • (2006) Biochemistry , vol.45 , pp. 1712-1722
    • Bilder, P.1    Lightle, S.2    Bainbridge, G.3    Ohren, J.4    Finzel, B.5    Sun, F.6    Holley, S.7    Al-Kassim, L.8    Spessard, C.9
  • 5
    • 0032563087 scopus 로고    scopus 로고
    • Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase
    • Blanchard, C.Z. and Waldrop, G.L. 1998. Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase. J. Biol. Chem. 273: 19140-19145.
    • (1998) J. Biol. Chem , vol.273 , pp. 19140-19145
    • Blanchard, C.Z.1    Waldrop, G.L.2
  • 6
    • 0023645566 scopus 로고
    • Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene
    • Bognar, A.L., Osborne, C., and Shane, B. 1987. Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene. J. Biol. Chem. 262: 12337-12343.
    • (1987) J. Biol. Chem , vol.262 , pp. 12337-12343
    • Bognar, A.L.1    Osborne, C.2    Shane, B.3
  • 7
    • 0026690379 scopus 로고
    • Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli
    • Brown, E. and Wood, J.M. 1992. Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli. J. Biol. Chem. 267: 13086-13092.
    • (1992) J. Biol. Chem , vol.267 , pp. 13086-13092
    • Brown, E.1    Wood, J.M.2
  • 8
    • 0022852279 scopus 로고
    • Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis
    • Cha, T.A. and Alberts, B.M. 1986. Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis. J. Biol. Chem. 261: 7001-7010.
    • (1986) J. Biol. Chem , vol.261 , pp. 7001-7010
    • Cha, T.A.1    Alberts, B.M.2
  • 9
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W.W. 1979. Statistical analysis of enzyme kinetic data. Methods Enzymol. 63: 103-138.
    • (1979) Methods Enzymol , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 10
    • 77956902884 scopus 로고
    • Steady-state kinetics
    • eds. D.S. Sigman and P.D. Boyer, pp, Academic Press, San Diego, CA
    • Cleland, W.W. 1990. Steady-state kinetics. In The enzymes. (eds. D.S. Sigman and P.D. Boyer), pp. 117-119. Academic Press, San Diego, CA.
    • (1990) The enzymes , pp. 117-119
    • Cleland, W.W.1
  • 11
    • 0037007223 scopus 로고    scopus 로고
    • Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA
    • Cochkareva, E., Korolev, S., Lees-Miller, S.P., and Bochkarev, A. 2002. Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. EMBO J. 21: 1855-1863.
    • (2002) EMBO J , vol.21 , pp. 1855-1863
    • Cochkareva, E.1    Korolev, S.2    Lees-Miller, S.P.3    Bochkarev, A.4
  • 12
    • 0035827346 scopus 로고    scopus 로고
    • Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution
    • Cramer, P., Bushnell, D.A., and Kornberg, R.D. 2003. Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. Science 292: 1863-1876.
    • (2003) Science , vol.292 , pp. 1863-1876
    • Cramer, P.1    Bushnell, D.A.2    Kornberg, R.D.3
  • 13
    • 0036018143 scopus 로고    scopus 로고
    • Multi-subunit acetyl-CoA carboxylases
    • Cronan Jr., J.E. and Waldrop, G.L. 2002. Multi-subunit acetyl-CoA carboxylases. Prog. Lipid Res. 41: 407-435.
    • (2002) Prog. Lipid Res , vol.41 , pp. 407-435
    • Cronan Jr., J.E.1    Waldrop, G.L.2
  • 14
    • 0035142840 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein
    • Davis, M.S. and Cronan Jr., J.E. 2001. Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein. J. Bacteriol. 183: 1499-1503.
    • (2001) J. Bacteriol , vol.183 , pp. 1499-1503
    • Davis, M.S.1    Cronan Jr., J.E.2
  • 15
    • 8344220571 scopus 로고    scopus 로고
    • Crystal structure of the β-subunit of acyl-CoA carboxylase: Structure-based engineering of substrate specificity
    • Diacovich, L., Mitchell, D.L., Pham, H., Gago, G., Melgar, M.M., Khosla, C., Gramajo, H., and Tsai, S.C. 2004. Crystal structure of the β-subunit of acyl-CoA carboxylase: Structure-based engineering of substrate specificity. Biochemistry 43: 14027-14036.
    • (2004) Biochemistry , vol.43 , pp. 14027-14036
    • Diacovich, L.1    Mitchell, D.L.2    Pham, H.3    Gago, G.4    Melgar, M.M.5    Khosla, C.6    Gramajo, H.7    Tsai, S.C.8
  • 16
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica, K. and Rouvieìre-Yaniv, J. 1987. Histone-like proteins of bacteria. Microbiol. Rev. 51: 301-319.
    • (1987) Microbiol. Rev , vol.51 , pp. 301-319
    • Drlica, K.1    Rouvieìre-Yaniv, J.2
  • 17
    • 0026705508 scopus 로고
    • The role of integration host factor in gene expression in Escherichia coli
    • Freundlich, M., Ramani, N., Mathew, E., Sirko, A., and Tsui, P. 1992. The role of integration host factor in gene expression in Escherichia coli. Mol. Microbiol. 6: 2557-2563.
    • (1992) Mol. Microbiol , vol.6 , pp. 2557-2563
    • Freundlich, M.1    Ramani, N.2    Mathew, E.3    Sirko, A.4    Tsui, P.5
  • 18
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt, J.A. and Babbitt, P.C. 2001. Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies. Annu. Rev. Biochem. 70: 209-246.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 19
    • 0030581147 scopus 로고    scopus 로고
    • Localized DNA flexibility contributes to target site selection by DNA-bending proteins
    • Grove, A., Galeone, A., Mayol, L., and Geiduschek, E.P. 1996. Localized DNA flexibility contributes to target site selection by DNA-bending proteins. J. Mol. Biol. 260: 120-125.
    • (1996) J. Mol. Biol , vol.260 , pp. 120-125
    • Grove, A.1    Galeone, A.2    Mayol, L.3    Geiduschek, E.P.4
  • 20
    • 3843135240 scopus 로고    scopus 로고
    • Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme
    • Gu, D., Zhou, Y., Kallhoff, V., Baban, B., Tanner, J.J., and Becker, D.F. 2004. Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme. J. Biol. Chem. 279: 31171-31176.
    • (2004) J. Biol. Chem , vol.279 , pp. 31171-31176
    • Gu, D.1    Zhou, Y.2    Kallhoff, V.3    Baban, B.4    Tanner, J.J.5    Becker, D.F.6
  • 21
    • 0016285541 scopus 로고
    • Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components
    • Guchhait, R.B., Polakis, S.E., Dimroth, P., Stoll, E., Moss, J., and Lane, M.D. 1974. Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components. J. Biol. Chem. 249: 6633-6645.
    • (1974) J. Biol. Chem , vol.249 , pp. 6633-6645
    • Guchhait, R.B.1    Polakis, S.E.2    Dimroth, P.3    Stoll, E.4    Moss, J.5    Lane, M.D.6
  • 22
    • 0028238186 scopus 로고
    • Determining the DNA sequence elements required for binding integration host factor to two different target sites
    • Hales, L.M., Gumport, R.I., and Gardner, J.F. 1994. Determining the DNA sequence elements required for binding integration host factor to two different target sites. J. Bacteriol. 176: 2999-3006.
    • (1994) J. Bacteriol , vol.176 , pp. 2999-3006
    • Hales, L.M.1    Gumport, R.I.2    Gardner, J.F.3
  • 23
    • 0029870997 scopus 로고    scopus 로고
    • Examining the contribution of a dA+dT element to the conformation of Escherichia coli integration host factor-DNA complexes
    • Hales, L.M., Gumport, R.I., and Gardner, J.F. 1996. Examining the contribution of a dA+dT element to the conformation of Escherichia coli integration host factor-DNA complexes. Nucleic Acids Res. 24: 1780-1786.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1780-1786
    • Hales, L.M.1    Gumport, R.I.2    Gardner, J.F.3
  • 24
    • 5644229499 scopus 로고    scopus 로고
    • Regulation of gene expression by a metabolic enzyme
    • Hall, D.A., Zhu, H., Zhu, X., Royce, T., Gerstein, M., and Snyder, M. 2004. Regulation of gene expression by a metabolic enzyme. Science 306: 482-484.
    • (2004) Science , vol.306 , pp. 482-484
    • Hall, D.A.1    Zhu, H.2    Zhu, X.3    Royce, T.4    Gerstein, M.5    Snyder, M.6
  • 27
    • 0036296417 scopus 로고    scopus 로고
    • A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase
    • Levert, K.L. and Waldrop, G.L. 2002. A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase. Biochem. Biophys. Res. Commun. 291: 1213-1217.
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 1213-1217
    • Levert, K.L.1    Waldrop, G.L.2
  • 28
    • 0027389215 scopus 로고
    • Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis
    • Li, S.J. and Cronan Jr., J.E. 1993. Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis. J. Bacteriol. 175: 332-340.
    • (1993) J. Bacteriol , vol.175 , pp. 332-340
    • Li, S.J.1    Cronan Jr., J.E.2
  • 29
    • 27644587253 scopus 로고    scopus 로고
    • A novel plant cysteine protease has a dual function as a regulator of 1-aminocyclopropane-1-carboxylic acid synthase gene expression
    • Matarasso, N., Schuster, S., and Avni, A. 2005. A novel plant cysteine protease has a dual function as a regulator of 1-aminocyclopropane-1-carboxylic acid synthase gene expression. Plant Cell 17: 1205-1216.
    • (2005) Plant Cell , vol.17 , pp. 1205-1216
    • Matarasso, N.1    Schuster, S.2    Avni, A.3
  • 30
    • 0026356394 scopus 로고
    • Requirements for primer synthesis by bacteriophage T7 63-kDa gene 4 protein. Roles of template sequence and T7 56-kDa gene 4 protein
    • Mendelman, L.V. and Richardson, C.C. 1991. Requirements for primer synthesis by bacteriophage T7 63-kDa gene 4 protein. Roles of template sequence and T7 56-kDa gene 4 protein. J. Biol. Chem. 266: 23240-23250.
    • (1991) J. Biol. Chem , vol.266 , pp. 23240-23250
    • Mendelman, L.V.1    Richardson, C.C.2
  • 31
    • 0033551040 scopus 로고    scopus 로고
    • The Cys4 zinc finger of bacteriophage T7 primase in sequence-specific single-stranded DNA recognition
    • Mendelman, L., Kusakabe, T., Hine, A., Hyberts, S.G., and Richardson, C.C. 1999. The Cys4 zinc finger of bacteriophage T7 primase in sequence-specific single-stranded DNA recognition. Proc. Natl. Acad. Sci. 96: 4295-4300.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 4295-4300
    • Mendelman, L.1    Kusakabe, T.2    Hine, A.3    Hyberts, S.G.4    Richardson, C.C.5
  • 32
    • 3042681300 scopus 로고    scopus 로고
    • Information content and complexity in the high-order organization of DNA
    • Minsky, A. 2004. Information content and complexity in the high-order organization of DNA. Annu. Rev. Biophys. Biomol. Struct. 33: 317-342.
    • (2004) Annu. Rev. Biophys. Biomol. Struct , vol.33 , pp. 317-342
    • Minsky, A.1
  • 33
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 35
    • 0015735116 scopus 로고
    • Stringent control of fatty acid synthesis in Escherichia coli
    • Polakis, S.E., Guchhait, R.B., and Lane, M.D. 1973. Stringent control of fatty acid synthesis in Escherichia coli. J. Biol. Chem. 248: 7957-7966.
    • (1973) J. Biol. Chem , vol.248 , pp. 7957-7966
    • Polakis, S.E.1    Guchhait, R.B.2    Lane, M.D.3
  • 36
    • 0027371187 scopus 로고
    • Novel zinc finger motif in the basal transcriptional machinery: Three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS
    • Qian, X., Gozani, S., Yoon, H., Jeon, C., Agarwal, K., and Weiss, M.A. 1993. Novel zinc finger motif in the basal transcriptional machinery: Three-dimensional NMR studies of the nucleic acid binding domain of transcriptional elongation factor TFIIS. Biochemistry 32: 9944-9959.
    • (1993) Biochemistry , vol.32 , pp. 9944-9959
    • Qian, X.1    Gozani, S.2    Yoon, H.3    Jeon, C.4    Agarwal, K.5    Weiss, M.A.6
  • 38
    • 0016830820 scopus 로고
    • Acetyl-coenzyme-A carboxylase from rat liver. Subunit structure and proteolytic modification
    • Tanabe, T., Wada, K., Okazaki, T., and Numa, S. 1975. Acetyl-coenzyme-A carboxylase from rat liver. Subunit structure and proteolytic modification. Eur. J. Biochem. 57: 15-24.
    • (1975) Eur. J. Biochem , vol.57 , pp. 15-24
    • Tanabe, T.1    Wada, K.2    Okazaki, T.3    Numa, S.4
  • 41
    • 0000957077 scopus 로고
    • Studies on liver alcohol hydrogenase complex 3. Multiple inhibition kinetics in the presence of two competitive inhibitors
    • Yonetani, T. and Theorell, H. 1964. Studies on liver alcohol hydrogenase complex 3. Multiple inhibition kinetics in the presence of two competitive inhibitors. Arch. Biochem. Biophys. 106: 243-251.
    • (1964) Arch. Biochem. Biophys , vol.106 , pp. 243-251
    • Yonetani, T.1    Theorell, H.2
  • 42
    • 0037470947 scopus 로고    scopus 로고
    • Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase
    • Zhang, H., Yang, Z., Shen, Y., and Tong, L. 2003. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science 299: 2064-2067.
    • (2003) Science , vol.299 , pp. 2064-2067
    • Zhang, H.1    Yang, Z.2    Shen, Y.3    Tong, L.4


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