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Volumn 188, Issue 1, 2006, Pages 223-230

The AidB component of the Escherichia coli adaptive response to alkylating agents is a flavin-containing, DNA-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATING AGENT; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; FLAVINE ADENINE NUCLEOTIDE; AIDB PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; ISOVALERYL COENZYME A DEHYDROGENASE;

EID: 33644905598     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.1.223-230.2006     Document Type: Article
Times cited : (30)

References (47)
  • 1
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • Adamczak, R., A. Porollo, and J. Meller. 2005. Combining prediction of secondary structure and solvent accessibility in proteins. Proteins Struct. Funct. Genet. 59:467-475.
    • (2005) Proteins Struct. Funct. Genet. , vol.59 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 3
    • 0032559602 scopus 로고    scopus 로고
    • Human long chain, very long chain and medium chain acyl-CoA dehydrogenases are specific for the S-enantiomer of 2-methylpentadecanoyl-CoA
    • Battaile, K. P., M. McBurney, P. P. Van Veldhoven, and J. Vockley. 1998. Human long chain, very long chain and medium chain acyl-CoA dehydrogenases are specific for the S-enantiomer of 2-methylpentadecanoyl-CoA. Biochim. Biophys. Acta 1390:333-338.
    • (1998) Biochim. Biophys. Acta , vol.1390 , pp. 333-338
    • Battaile, K.P.1    McBurney, M.2    Van Veldhoven, P.P.3    Vockley, J.4
  • 4
    • 11244346037 scopus 로고    scopus 로고
    • A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1
    • Chirabau, C. B., C. Sandu, M. Fraavje, E. Schiltz, and R. Brandsch. 2004. A novel γ-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur. J. Biochem. 271:4677-4684.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4677-4684
    • Chirabau, C.B.1    Sandu, C.2    Fraavje, M.3    Schiltz, E.4    Brandsch, R.5
  • 5
    • 0017669272 scopus 로고
    • Measurement of binding constants for protein-DNA interactions by DNA-cellulose chromatography
    • deHaseth, P. L., C. A. Gross, R. R. Burgess, and M. T. Record, Jr. 1977. Measurement of binding constants for protein-DNA interactions by DNA-cellulose chromatography. Biochemistry 16:4777-4783.
    • (1977) Biochemistry , vol.16 , pp. 4777-4783
    • DeHaseth, P.L.1    Gross, C.A.2    Burgess, R.R.3    Record Jr., M.T.4
  • 7
    • 0030920569 scopus 로고    scopus 로고
    • Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation
    • Eder, M., F. Krautle, V. Dong, P. Vock, V. Kieweg, J. J. Kim, A. W. Strauss, and S. Ghisla. 1997. Characterization of human and pig kidney long-chain-acyl-CoA dehydrogenases and their role in beta-oxidation. Eur. J. Biochem. 245:600-607.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 600-607
    • Eder, M.1    Krautle, F.2    Dong, V.3    Vock, P.4    Kieweg, V.5    Kim, J.J.6    Strauss, A.W.7    Ghisla, S.8
  • 8
    • 0000239154 scopus 로고
    • Butyro-CoA dehydrogenase from Megasphaera elsdenii
    • Engel, P. C. 1981. Butyro-CoA dehydrogenase from Megasphaera elsdenii. Methods Enzymol. 71:359-366.
    • (1981) Methods Enzymol. , vol.71 , pp. 359-366
    • Engel, P.C.1
  • 9
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla, S., and C. Thorpe. 2004. Acyl-CoA dehydrogenases. A mechanistic overview. Eur. J. Biochem. 271:494-508.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 10
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: A simple approach to improve protein structure predictions
    • Ginalski, K., A. Elofsson, D. Fisher, and L. Rychlewski. 2003. 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 19:1015-1018.
    • (2003) Bioinformatics , vol.19 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fisher, D.3    Rychlewski, L.4
  • 11
    • 12244253706 scopus 로고    scopus 로고
    • Identification of the covalent flavin adenine dinucleotide-binding region in pyranose 2-oxidase from Trametes multicolor
    • Halada, P., C. Leitner, P. Sedmera, D. Haltrich, and J. Vole. 2003. Identification of the covalent flavin adenine dinucleotide-binding region in pyranose 2-oxidase from Trametes multicolor. Anal. Biochem. 314:235-242.
    • (2003) Anal. Biochem. , vol.314 , pp. 235-242
    • Halada, P.1    Leitner, C.2    Sedmera, P.3    Haltrich, D.4    Vole, J.5
  • 12
    • 0022366089 scopus 로고
    • Spectroscopic analysis of the interaction of rat liver short-chain, medium-chain, and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates
    • Ikeda, Y., K. Okamura-Ikeda, and K. Tanaka. 1985. Spectroscopic analysis of the interaction of rat liver short-chain, medium-chain, and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates. Biochemistry 24:7192-7199.
    • (1985) Biochemistry , vol.24 , pp. 7192-7199
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 14
    • 0043166919 scopus 로고    scopus 로고
    • A sensitive two-color electrophoretic mobility shift assay for detecting both nucleic acids and protein in gels
    • Jing, D., J. Agnew, W. F. Patton, J. Hendrickson, and J. M. Beechem. 2003. A sensitive two-color electrophoretic mobility shift assay for detecting both nucleic acids and protein in gels. Proteomics 3:1172-1180.
    • (2003) Proteomics , vol.3 , pp. 1172-1180
    • Jing, D.1    Agnew, J.2    Patton, W.F.3    Hendrickson, J.4    Beechem, J.M.5
  • 15
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones, D. T. 1999. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292:195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 17
    • 0037417756 scopus 로고    scopus 로고
    • Tautomeric rearrangement of a dihydroflavin bound to monomeric sarcosine oxidase or N-methyltryptophan oxidase
    • Khanna, P., and M. S. Jorns. 2003. Tautomeric rearrangement of a dihydroflavin bound to monomeric sarcosine oxidase or N-methyltryptophan oxidase. Biochemistry 42:864-869.
    • (2003) Biochemistry , vol.42 , pp. 864-869
    • Khanna, P.1    Jorns, M.S.2
  • 18
    • 0842265784 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences
    • Kim, J.-J. P., and R. Miura. 2004. Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences. Eur. J. Biochem. 271:483-493.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 483-493
    • Kim, J.-J.P.1    Miura, R.2
  • 20
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., M. Billeter, and K. Wüthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics Modeling 14:51-55.
    • (1996) J. Mol. Graphics Modeling , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0028063267 scopus 로고
    • Structure and transcriptional regulation of the Escherichia coli adaptive response gene aidB
    • Landini, P., L. I. Hajec, and M. R. Volkert. 1994. Structure and transcriptional regulation of the Escherichia coli adaptive response gene aidB. J. Bacteriol. 176:6583-6589.
    • (1994) J. Bacteriol. , vol.176 , pp. 6583-6589
    • Landini, P.1    Hajec, L.I.2    Volkert, M.R.3
  • 23
    • 0028905277 scopus 로고
    • Transcriptional activation of the Escherichia coli adaptive response gene aidB is mediated by binding of methylated Ada protein
    • Landini, P., and M. R. Volkert. 1995. Transcriptional activation of the Escherichia coli adaptive response gene aidB is mediated by binding of methylated Ada protein. J. Biol. Chem. 270:8285-8289.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8285-8289
    • Landini, P.1    Volkert, M.R.2
  • 24
    • 0037432631 scopus 로고    scopus 로고
    • Yeast Fms1 is a FAD-utilizing polyamine oxidase
    • Landry, J., and R. Sternglanz. 2003. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem. Biophys. Res. Commun. 303:771-776.
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 771-776
    • Landry, J.1    Sternglanz, R.2
  • 25
    • 0022980720 scopus 로고
    • The purification and characterization of glutaryl-coenzyme a dehydrogenase from porcine and human liver
    • Lenich, A. C., and S. I. Goodman. 1986. The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver. J. Biol. Chem. 261:4090-4096.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4090-4096
    • Lenich, A.C.1    Goodman, S.I.2
  • 26
    • 0030811135 scopus 로고    scopus 로고
    • Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps
    • Martinez, A., and R. Kolter. 1997. Protection of DNA during oxidative stress by the nonspecific DNA-binding protein Dps. J. Bacteriol. 179:5188-5194.
    • (1997) J. Bacteriol. , vol.179 , pp. 5188-5194
    • Martinez, A.1    Kolter, R.2
  • 27
    • 0019023686 scopus 로고
    • Active site probes of flavoproteins
    • Massey, V., and P. Hemmerich. 1980. Active site probes of flavoproteins. Biochem. Soc. Trans. 8:246-257.
    • (1980) Biochem. Soc. Trans. , vol.8 , pp. 246-257
    • Massey, V.1    Hemmerich, P.2
  • 28
    • 0017817482 scopus 로고
    • Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins
    • Massey, V., and P. Hemmerich. 1978. Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins. Biochemistry 17:9-16.
    • (1978) Biochemistry , vol.17 , pp. 9-16
    • Massey, V.1    Hemmerich, P.2
  • 30
    • 0017855692 scopus 로고
    • Light-mediated reduction of flavoproteins with flavins as catalysts
    • Massey, V., M. Stankovich, and P. Hemmerich. 1978. Light-mediated reduction of flavoproteins with flavins as catalysts. Biochemistry 17:1-8.
    • (1978) Biochemistry , vol.17 , pp. 1-8
    • Massey, V.1    Stankovich, M.2    Hemmerich, P.3
  • 31
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. 1987. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 32
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., K. Bryson, and D. T. Jones. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 33
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane protein and globular proteins at high levels
    • Miroux, B., and J. E. Walker. 1996. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane protein and globular proteins at high levels. J. Mol. Biol. 260:289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 36
    • 0036221422 scopus 로고    scopus 로고
    • Three-dimensional structure of the flavoenzyme acyl-CoA oxidase II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase
    • Nakajima, Y., I. Miyahara, K. Hirotsu, Y. Nishima, K. Shiga, C. Setoyama, H. Tamaoki, and R. Miura. 2002. Three-dimensional structure of the flavoenzyme acyl-CoA oxidase II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase. J. Biochem. 131:365-374.
    • (2002) J. Biochem. , vol.131 , pp. 365-374
    • Nakajima, Y.1    Miyahara, I.2    Hirotsu, K.3    Nishima, Y.4    Shiga, K.5    Setoyama, C.6    Tamaoki, H.7    Miura, R.8
  • 37
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., K. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11:281-296.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 38
    • 0343092819 scopus 로고
    • A new chemical method for synthesizing and recycling acyl coenzyme A thioesters
    • Ouyang, T., and D. R. Walt. 1991. A new chemical method for synthesizing and recycling acyl coenzyme A thioesters. J. Org. Chem. 56:3752-3755.
    • (1991) J. Org. Chem. , vol.56 , pp. 3752-3755
    • Ouyang, T.1    Walt, D.R.2
  • 39
    • 0035782925 scopus 로고    scopus 로고
    • Review: Protein secondary structure prediction continues to rise
    • Rost, B. 2001. Review: protein secondary structure prediction continues to rise. J. Struct. Biol. 134:204-218.
    • (2001) J. Struct. Biol. , vol.134 , pp. 204-218
    • Rost, B.1
  • 40
    • 0037115934 scopus 로고    scopus 로고
    • Recent progress on the Ada response for inducible repair of DNA alkylation damage
    • Sedgwick, B., and T. Lindahl. 2002. Recent progress on the Ada response for inducible repair of DNA alkylation damage. Oncogene 21:8886-8894.
    • (2002) Oncogene , vol.21 , pp. 8886-8894
    • Sedgwick, B.1    Lindahl, T.2
  • 42
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • Trewick, S. C., T. F. Henshaw, R. P. Hausinger, T. Lindahl, and B. Sedgwick. 2002. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 419:174-178.
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 43
    • 0023853497 scopus 로고
    • Adaptive response of Escherichia coli to alkylation damage
    • Volkert, M. R. 1988. Adaptive response of Escherichia coli to alkylation damage. Environ. Mol. Mutagen. 11:241-255.
    • (1988) Environ. Mol. Mutagen. , vol.11 , pp. 241-255
    • Volkert, M.R.1
  • 44
    • 0024538236 scopus 로고
    • Expression of DNA damage-inducible genes of Escherichia coli upon treatment with methylating, ethylating and propylating agents
    • Volkert, M. R., F. H. Gately, and L. I. Hajec. 1989. Expression of DNA damage-inducible genes of Escherichia coli upon treatment with methylating, ethylating and propylating agents. Mutat. Res. 217:109-115.
    • (1989) Mutat. Res. , vol.217 , pp. 109-115
    • Volkert, M.R.1    Gately, F.H.2    Hajec, L.I.3
  • 45
    • 0021137399 scopus 로고
    • Induction of specific Escherichia coli genes by sublethal treatments with alkylating agents
    • Volkert, M. R., and D. C. Nguyen. 1984. Induction of specific Escherichia coli genes by sublethal treatments with alkylating agents. Proc. Natl. Acad. Sci. USA 81:4110-4114.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4110-4114
    • Volkert, M.R.1    Nguyen, D.C.2
  • 46
    • 0022597008 scopus 로고
    • Escherichia coli gene induction by alkylation treatment
    • Volkert, M. R., D. C. Nguyen, and K. C. Beard. 1986. Escherichia coli gene induction by alkylation treatment. Genetics 112:11-26.
    • (1986) Genetics , vol.112 , pp. 11-26
    • Volkert, M.R.1    Nguyen, D.C.2    Beard, K.C.3
  • 47
    • 0242663236 scopus 로고    scopus 로고
    • Crystal structure of an acyl-ACP dehydrogenase from the FK520 polyketide biosynthetic pathway: Insights into extender unit biosynthesis
    • Watanabe, K., C. Khosla, R. M. Stroud, and S.-C. Tsai. 2003. Crystal structure of an acyl-ACP dehydrogenase from the FK520 polyketide biosynthetic pathway: insights into extender unit biosynthesis. J. Mol. Biol. 334:435-444.
    • (2003) J. Mol. Biol. , vol.334 , pp. 435-444
    • Watanabe, K.1    Khosla, C.2    Stroud, R.M.3    Tsai, S.-C.4


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