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Volumn 13, Issue 11, 2004, Pages 3043-3050

Promiscuous protein biotinylation by Escherichia coli biotin protein ligase

Author keywords

Acyl adenylate; Biotin protein ligase; Biotinylation; BirA; Protein modification

Indexed keywords

AVIDIN; BACTERIAL ENZYME; BIOTIN; BIOTIN PROTEIN LIGASE; BOVINE SERUM ALBUMIN; CELL PROTEIN; CHLORAMPHENICOL ACETYLTRANSFERASE; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; LIGASE; MUTANT PROTEIN; PROTEIN BIRA; RIBONUCLEASE A; STREPTAVIDIN; UNCLASSIFIED DRUG;

EID: 7244238404     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.04911804     Document Type: Article
Times cited : (209)

References (25)
  • 1
    • 0019473758 scopus 로고
    • Genetic and biochemical characterization of the birA gene and its product: Evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli
    • Barker, D.F. and Campbell, A.M. 1981. Genetic and biochemical characterization of the birA gene and its product: Evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli. J. Mol. Biol. 146: 469-492.
    • (1981) J. Mol. Biol. , vol.146 , pp. 469-492
    • Barker, D.F.1    Campbell, A.M.2
  • 2
    • 0031419676 scopus 로고    scopus 로고
    • Escherichia coli repressor of biotin biosynthesis
    • Beckett, D. and Matthews, B.W. 1997. Escherichia coli repressor of biotin biosynthesis. Methods Enzymol. 279: 362-376.
    • (1997) Methods Enzymol. , vol.279 , pp. 362-376
    • Beckett, D.1    Matthews, B.W.2
  • 3
    • 1642384541 scopus 로고    scopus 로고
    • The biotin repressor: Modulation of allostery by corepressor analogs
    • Brown, P.H., Cronan, J.E., Grotli, M., and Beckett, D. 2004. The biotin repressor: Modulation of allostery by corepressor analogs. J. Mol. Biol. 337: 857-869.
    • (2004) J. Mol. Biol. , vol.337 , pp. 857-869
    • Brown, P.H.1    Cronan, J.E.2    Grotli, M.3    Beckett, D.4
  • 4
    • 0033199782 scopus 로고    scopus 로고
    • The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity
    • Chapman-Smith, A. and Cronan Jr., J.E. 1999. The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity. Trends Biochem. Sci. 24: 359-363.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 359-363
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 5
    • 0033555541 scopus 로고    scopus 로고
    • Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase
    • Chapman-Smith, A., Morris, T.W., Wallace, J.C., and Cronan Jr., J.E. 1999. Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase. J. Biol. Chem. 274: 1449-1457.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1449-1457
    • Chapman-Smith, A.1    Morris, T.W.2    Wallace, J.C.3    Cronan Jr., J.E.4
  • 6
    • 0042232285 scopus 로고    scopus 로고
    • The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase
    • Choi-Rhee, E., and Cronan, J.E. 2003. The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 278: 30806-30812.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30806-30812
    • Choi-Rhee, E.1    Cronan, J.E.2
  • 7
    • 0024349661 scopus 로고
    • The E. coli bio operon: Transcriptional repression by an essential protein modification enzyme
    • Cronan Jr., J.E. 1989. The E. coli bio operon: Transcriptional repression by an essential protein modification enzyme. Cell 58: 427-429.
    • (1989) Cell , vol.58 , pp. 427-429
    • Cronan Jr., J.E.1
  • 8
    • 0242659212 scopus 로고    scopus 로고
    • Cosmid-based system for transient expression and absolute off-to-on transcriptional control of Escherichia coli genes
    • Cronan, J.E. 2003. Cosmid-based system for transient expression and absolute off-to-on transcriptional control of Escherichia coli genes. J. Bacteriol. 185: 6522-6529.
    • (2003) J. Bacteriol. , vol.185 , pp. 6522-6529
    • Cronan, J.E.1
  • 9
    • 0034646227 scopus 로고    scopus 로고
    • The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: Sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates
    • Ehmann, D.E., Shaw-Reid, C.A., Losey, H.C., and Walsh, C.T. 2000. The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: Sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates. Proc. Natl. Acad. Sci. 97: 2509-2514.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 2509-2514
    • Ehmann, D.E.1    Shaw-Reid, C.A.2    Losey, H.C.3    Walsh, C.T.4
  • 10
    • 0030711763 scopus 로고    scopus 로고
    • Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: Identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry
    • Gillet, S., Hountondji, C., Schmitter, J.M., and Blanquet, S. 1997. Covalent methionylation of Escherichia coli methionyl-tRNA synthethase: Identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry. Protein Sci. 6: 2426-2435.
    • (1997) Protein Sci. , vol.6 , pp. 2426-2435
    • Gillet, S.1    Hountondji, C.2    Schmitter, J.M.3    Blanquet, S.4
  • 12
    • 0034468380 scopus 로고    scopus 로고
    • Enzyme-induced covalent modification of methionyl-tRNA synthetase from Bacillus stearothermophilus by methionyl-adenylate: Identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry
    • Hountondji, C., Beauvallet, C., Pernollet, J.C., and Blanquet, S. 2000. Enzyme-induced covalent modification of methionyl-tRNA synthetase from Bacillus stearothermophilus by methionyl-adenylate: Identification of the labeled amino acid residues by matrix-assisted laser desorption-ionization mass spectrometry. J. Protein Chem. 19: 563-568.
    • (2000) J. Protein Chem. , vol.19 , pp. 563-568
    • Hountondji, C.1    Beauvallet, C.2    Pernollet, J.C.3    Blanquet, S.4
  • 13
    • 0033846484 scopus 로고    scopus 로고
    • Function of a conserved sequence motif in biotin holoenzyme synthetases
    • Kwon, K., and Beckett, D. 2000. Function of a conserved sequence motif in biotin holoenzyme synthetases. Protein Sci. 9: 1530-1539.
    • (2000) Protein Sci. , vol.9 , pp. 1530-1539
    • Kwon, K.1    Beckett, D.2
  • 14
    • 0034671258 scopus 로고    scopus 로고
    • Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor
    • Kwon, K., Streaker, E.D., Ruparelia, S., and Beckett, D. 2000. Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor. J. Mol. Biol. 304: 821-833.
    • (2000) J. Mol. Biol. , vol.304 , pp. 821-833
    • Kwon, K.1    Streaker, E.D.2    Ruparelia, S.3    Beckett, D.4
  • 15
    • 0036176908 scopus 로고    scopus 로고
    • Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase
    • Kwon, K., Streaker, E.D., and Beckett, D. 2002. Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase. Protein Sci. 11: 558-570.
    • (2002) Protein Sci. , vol.11 , pp. 558-570
    • Kwon, K.1    Streaker, E.D.2    Beckett, D.3
  • 16
    • 0014027648 scopus 로고
    • Further studies on the properties of liver propionyl coenzyme A holocarboxylase synthetase and the specificity of holocarboxylase formation
    • McAllister, H.C., and Coon, M.J. 1966. Further studies on the properties of liver propionyl coenzyme A holocarboxylase synthetase and the specificity of holocarboxylase formation. J. Biol Chem. 241: 2855-2861.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2855-2861
    • McAllister, H.C.1    Coon, M.J.2
  • 17
    • 0032007565 scopus 로고    scopus 로고
    • Selectivity of post-translational modification in biotinylated proteins: The carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli
    • Reche, P., Li, Y.L., Fuller, C., Eichhorn, K., and Perham, R.N. 1998. Selectivity of post-translational modification in biotinylated proteins: The carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli. Biochem. J. 329 (Pt. 3): 589-596.
    • (1998) Biochem. J. , vol.329 , Issue.3 PART , pp. 589-596
    • Reche, P.1    Li, Y.L.2    Fuller, C.3    Eichhorn, K.4    Perham, R.N.5
  • 18
    • 0000041171 scopus 로고    scopus 로고
    • High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii
    • Reddy, D.V., Shenoy, B.C., Carey, P.R., and Sonnichsen, F.D. 2000. High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry 39: 2509-2516.
    • (2000) Biochemistry , vol.39 , pp. 2509-2516
    • Reddy, D.V.1    Shenoy, B.C.2    Carey, P.R.3    Sonnichsen, F.D.4
  • 20
    • 0037474538 scopus 로고    scopus 로고
    • Coupling of protein assembly and DNA binding: Biotin repressor dimerization precedes biotin operator binding
    • Streaker, E.D. and Beckett, D. 2003. Coupling of protein assembly and DNA binding: Biotin repressor dimerization precedes biotin operator binding. J. Mol. Biol. 325: 937-948.
    • (2003) J. Mol. Biol. , vol.325 , pp. 937-948
    • Streaker, E.D.1    Beckett, D.2
  • 21
    • 0035190710 scopus 로고    scopus 로고
    • Competing protein:protein interactions are proposed to control the biological switch of the E. coli biotin repressor
    • Weaver, L.H., Kwon, K., Beckett, D., and Matthews, B.W. 2001a. Competing protein:protein interactions are proposed to control the biological switch of the E. coli biotin repressor. Protein Sci. 10: 2618-2622.
    • (2001) Protein Sci. , vol.10 , pp. 2618-2622
    • Weaver, L.H.1    Kwon, K.2    Beckett, D.3    Matthews, B.W.4
  • 22
    • 0035932977 scopus 로고    scopus 로고
    • Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator
    • _. 2001b. Corepressor-induced organization and assembly of the biotin repressor: A model for allosteric activation of a transcriptional regulator. Proc. Natl. Acad. Sci. 98: 6045-6050.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 6045-6050
  • 23
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains
    • Wilson, K.P., Shewchuk, L.M., Brennan, R.G., Otsuka, A.J., and Matthews, B.W. 1992. Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc. Natl. Acad. Sci. 89: 9257-9261.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 24
    • 0030060228 scopus 로고    scopus 로고
    • Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant
    • Xu, Y. and Beckett, D. 1996. Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant. Biochemistry 35: 1783-1792.
    • (1996) Biochemistry , vol.35 , pp. 1783-1792
    • Xu, Y.1    Beckett, D.2
  • 25
    • 0031419426 scopus 로고    scopus 로고
    • Biotinyl-5′-adenylate synthesis catalyzed by Escherichia coli repressor of biotin biosynthesis
    • _. 1997. Biotinyl-5′-adenylate synthesis catalyzed by Escherichia coli repressor of biotin biosynthesis. Methods Enzymol. 279: 405-421.
    • (1997) Methods Enzymol. , vol.279 , pp. 405-421


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.