메뉴 건너뛰기




Volumn 194, Issue 5, 2012, Pages 1113-1126

Altered regulation of escherichia coli biotin biosynthesis in bira superrepressor mutant strains

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; BACTERIAL DNA; BACTERIAL PROTEIN; BIOTIN; BIOTINOYL ADENYLATE; BIRA PROTEIN; LIGASE; UNCLASSIFIED DRUG;

EID: 84857834296     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06549-11     Document Type: Article
Times cited : (42)

References (47)
  • 1
    • 33846259725 scopus 로고    scopus 로고
    • Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli
    • Abdel-Hamid AM, Cronan JE. 2007. Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli. J. Bacteriol. 189:369-376.
    • (2007) J. Bacteriol. , vol.189 , pp. 369-376
    • Abdel-Hamid, A.M.1    Cronan, J.E.2
  • 2
    • 73649193462 scopus 로고
    • Mode of action of chloramphenicol. VII. Growth and multiplication of Escherichia coli in the presence of chloramphenicol
    • Allison JL, et al. 1962. Mode of action of chloramphenicol. VII. Growth and multiplication of Escherichia coli in the presence of chloramphenicol. J. Bacteriol. 83:609-615.
    • (1962) J. Bacteriol. , vol.83 , pp. 609-615
    • Allison, J.L.1
  • 3
    • 31544450286 scopus 로고    scopus 로고
    • Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection
    • Baba T, et al. 2006. Construction of Escherichia coli K-12 in-frame, singlegene knockout mutants: the Keio collection. Mol. Syst. Biol. 2:2006.0008.
    • (2006) Mol. Syst. Biol. , vol.2
    • Baba, T.1
  • 4
    • 0019482402 scopus 로고
    • The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase
    • Barker DF, Campbell AM. 1981. The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase. J. Mol. Biol. 146:451-467.
    • (1981) J. Mol. Biol. , vol.146 , pp. 451-467
    • Barker, D.F.1    Campbell, A.M.2
  • 5
    • 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 DF, Campbell AM. 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
  • 6
    • 0018946749 scopus 로고
    • Use of bio-lac fusion strains to study regulation of biotin biosynthesis in Escherichia coli
    • Barker DF, Campbell AM. 1980. Use of bio-lac fusion strains to study regulation of biotin biosynthesis in Escherichia coli. J. Bacteriol. 143:789-800.
    • (1980) J. Bacteriol. , vol.143 , pp. 789-800
    • Barker, D.F.1    Campbell, A.M.2
  • 7
    • 41449084503 scopus 로고    scopus 로고
    • Biotin sensing: universal influence of biotin status on transcription
    • Beckett D. 2007. Biotin sensing: universal influence of biotin status on transcription. Annu. Rev. Genet. 41:443-464.
    • (2007) Annu. Rev. Genet. , vol.41 , pp. 443-464
    • Beckett, D.1
  • 8
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett D, Kovaleva E, Schatz PJ. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8:921-929.
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 9
    • 0023708084 scopus 로고
    • -cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing
    • -cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing. Gene 68:139-149.
    • (1988) Gene , vol.68 , pp. 139-149
    • Chambers, S.P.1    Prior, S.E.2    Barstow, D.A.3    Minton, N.P.4
  • 10
    • 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 TW, Wallace JC, Cronan JE, Jr. 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
  • 11
    • 0028108943 scopus 로고
    • Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase
    • Chapman-Smith A, Turner DL, Cronan JE, Jr, Morris TW, Wallace JC. 1994. Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochem. J. 302:881-887.
    • (1994) Biochem. J. , vol.302 , pp. 881-887
    • Chapman-Smith, A.1    Turner, D.L.2    Cronan Jr., J.E.3    Morris, T.W.4    Wallace, J.C.5
  • 12
    • 0042232285 scopus 로고    scopus 로고
    • The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase
    • Choi-Rhee E, Cronan JE. 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
  • 13
    • 7244238404 scopus 로고    scopus 로고
    • Promiscuous protein biotinylation by Escherichia coli biotin protein ligase
    • Choi-Rhee E, Schulman H, Cronan JE. 2004. Promiscuous protein biotinylation by Escherichia coli biotin protein ligase. Protein Sci. 13:3043-3050.
    • (2004) Protein Sci. , vol.13 , pp. 3043-3050
    • Choi-Rhee, E.1    Schulman, H.2    Cronan, J.E.3
  • 14
    • 0024349661 scopus 로고
    • The E. coli bio operon: transcriptional repression by an essential protein modification enzyme
    • Cronan JE, Jr. 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
  • 15
    • 0023679220 scopus 로고
    • Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination
    • Cronan JE, Jr. 1988. Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination. J. Biol. Chem. 263:10332-10336.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10332-10336
    • Cronan Jr., J.E.1
  • 16
    • 0033819032 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo: a useful posttranslational modification for protein analysis
    • Cronan JE, Jr, Reed KE. 2000. Biotinylation of proteins in vivo: a useful posttranslational modification for protein analysis. Methods Enzymol. 326:440-458.
    • (2000) Methods Enzymol. , vol.326 , pp. 440-458
    • Cronan Jr., J.E.1    Reed, K.E.2
  • 17
    • 0028816609 scopus 로고
    • The gene encoding the biotinapoprotein ligase of Saccharomyces cerevisiae
    • Cronan JE, Jr, Wallace JC. 1995. The gene encoding the biotinapoprotein ligase of Saccharomyces cerevisiae. FEMS Microbiol. Lett. 130: 221-229.
    • (1995) FEMS Microbiol. Lett. , vol.130 , pp. 221-229
    • Cronan Jr., J.E.1    Wallace, J.C.2
  • 18
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U. S. A. 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 19
    • 34547131328 scopus 로고    scopus 로고
    • In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis
    • De Lay NR, Cronan JE. 2007. In vivo functional analyses of the type II acyl carrier proteins of fatty acid biosynthesis. J. Biol. Chem. 282:20319-20328.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20319-20328
    • DeLay, N.R.1    Cronan, J.E.2
  • 20
    • 0024102025 scopus 로고
    • The effects of mutations in the ant promoter of phage P22 depend on context
    • Grana D, Gardella T, Susskind MM. 1988. The effects of mutations in the ant promoter of phage P22 depend on context. Genetics 120:319-327.
    • (1988) Genetics , vol.120 , pp. 319-327
    • Grana, D.1    Gardella, T.2    Susskind, M.M.3
  • 21
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman LM, Belin D, Carson MJ, Beckwith J. 1995. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 22
    • 0026499452 scopus 로고
    • The lethal phenotype caused by null mutations in the Escherichia coli htrB gene is suppressed by mutations in the accBC operon, encoding two subunits of acetyl coenzyme A carboxylase
    • Karow M, Fayet O, Georgopoulos C. 1992. The lethal phenotype caused by null mutations in the Escherichia coli htrB gene is suppressed by mutations in the accBC operon, encoding two subunits of acetyl coenzyme A carboxylase. J. Bacteriol. 174:7407-7418.
    • (1992) J. Bacteriol. , vol.174 , pp. 7407-7418
    • Karow, M.1    Fayet, O.2    Georgopoulos, C.3
  • 23
    • 2642639651 scopus 로고
    • Absence of RNase H allows replication of pBR322 in Escherichia coli mutants lacking DNA polymerase I
    • Kogoma T. 1984. Absence of RNase H allows replication of pBR322 in Escherichia coli mutants lacking DNA polymerase I. Proc. Natl. Acad. Sci. U. S. A. 81:7845-7849.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 7845-7849
    • Kogoma, T.1
  • 24
    • 0033846484 scopus 로고    scopus 로고
    • Function of a conserved sequence motif in biotin holoenzyme synthetases
    • Kwon K, 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
  • 25
    • 46649105245 scopus 로고    scopus 로고
    • Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics
    • Laine O, Streaker ED, Nabavi M, Fenselau CC, Beckett D. 2008. Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics. J. Mol. Biol. 381:89-101.
    • (2008) J. Mol. Biol. , vol.381 , pp. 89-101
    • Laine, O.1    Streaker, E.D.2    Nabavi, M.3    Fenselau, C.C.4    Beckett, D.5
  • 27
    • 0015306692 scopus 로고
    • Conditional lethality of recA and recB derivatives of a strain of Escherichia coli K-12 with a temperature-sensitive deoxyribonucleic acid polymerase I
    • Monk M, Kinross J. 1972. Conditional lethality of recA and recB derivatives of a strain of Escherichia coli K-12 with a temperature-sensitive deoxyribonucleic acid polymerase I. J. Bacteriol. 109:971-978.
    • (1972) J. Bacteriol. , vol.109 , pp. 971-978
    • Monk, M.1    Kinross, J.2
  • 28
    • 34548605606 scopus 로고    scopus 로고
    • Nucleation of an allosteric response via ligand-induced loop folding
    • Naganathan S, Beckett D. 2007. Nucleation of an allosteric response via ligand-induced loop folding. J. Mol. Biol. 373:96-111.
    • (2007) J. Mol. Biol. , vol.373 , pp. 96-111
    • Naganathan, S.1    Beckett, D.2
  • 29
    • 0029986466 scopus 로고    scopus 로고
    • Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
    • Nenortas E, Beckett D. 1996. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J. Biol. Chem. 271:7559-7567.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7559-7567
    • Nenortas, E.1    Beckett, D.2
  • 30
    • 0018795188 scopus 로고
    • A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Noel D, Nikaido K, Ames GF. 1979. A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 18:4159-4165.
    • (1979) Biochemistry , vol.18 , pp. 4159-4165
    • Noel, D.1    Nikaido, K.2    Ames, G.F.3
  • 31
    • 0018162576 scopus 로고
    • The regulatory region of the biotin operon in Escherichia coli
    • Otsuka A, Abelson J. 1978. The regulatory region of the biotin operon in Escherichia coli. Nature 276:689-694.
    • (1978) Nature , vol.276 , pp. 689-694
    • Otsuka, A.1    Abelson, J.2
  • 32
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen EF, et al. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 33
    • 0035793573 scopus 로고    scopus 로고
    • Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains
    • Polyak SW, Chapman-Smith A, Mulhern TD, Cronan JE, Jr, Wallace JC. 2001. Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains. J. Biol. Chem. 276:3037-3045.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3037-3045
    • Polyak, S.W.1    Chapman-Smith, A.2    Mulhern, T.D.3    Cronan Jr., J.E.4    Wallace, J.C.5
  • 34
    • 0018538322 scopus 로고
    • Biotinyl 5'-adenylate: corepressor role in the regulation of the biotin genes of Escherichia coli K-12
    • Prakash O, Eisenberg MA. 1979. Biotinyl 5'-adenylate: corepressor role in the regulation of the biotin genes of Escherichia coli K-12. Proc. Natl. Acad. Sci. U. S. A. 76:5592-5595.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 5592-5595
    • Prakash, O.1    Eisenberg, M.A.2
  • 35
    • 0024283925 scopus 로고
    • The nucleotide sequence of pACYC184
    • Rose RE. 1988. The nucleotide sequence of pACYC184. Nucleic Acids Res. 16:355.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 355
    • Rose, R.E.1
  • 37
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz PJ. 1993. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY) 11:1138-1143.
    • (1993) Biotechnology (NY) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 38
    • 75149116205 scopus 로고    scopus 로고
    • The switch regulating transcription of the Escherichia coli biotin operon does not require extensive protein-protein interactions
    • Solbiati J, Cronan JE. 2010. The switch regulating transcription of the Escherichia coli biotin operon does not require extensive protein-protein interactions. Chem. Biol. 17:11-17.
    • (2010) Chem. Biol. , vol.17 , pp. 11-17
    • Solbiati, J.1    Cronan, J.E.2
  • 39
    • 0037474538 scopus 로고    scopus 로고
    • Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding
    • Streaker ED, 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
  • 40
    • 0032525244 scopus 로고    scopus 로고
    • A map of the biotin repressor-biotin operator interface: binding of a winged helix-turn-helix protein dimer to a forty base-pair site
    • Streaker ED, Beckett D. 1998. A map of the biotin repressor-biotin operator interface: binding of a winged helix-turn-helix protein dimer to a forty base-pair site. J. Mol. Biol. 278:787-800.
    • (1998) J. Mol. Biol. , vol.278 , pp. 787-800
    • Streaker, E.D.1    Beckett, D.2
  • 41
    • 0037016018 scopus 로고    scopus 로고
    • The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding
    • Streaker ED, Gupta A, Beckett D. 2002. The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding. Biochemistry 41:14263-14271.
    • (2002) Biochemistry , vol.41 , pp. 14263-14271
    • Streaker, E.D.1    Gupta, A.2    Beckett, D.3
  • 42
    • 39849093502 scopus 로고    scopus 로고
    • Recombineering: genetic engineering in bacteria using homologous recombination
    • Thomason L, et al. 2007. Recombineering: genetic engineering in bacteria using homologous recombination. Curr. Protoc. Mol. Biol. 78:1.16.1-1.16.24.
    • (2007) Curr. Protoc. Mol. Biol. , vol.78
    • Thomason, L.1
  • 43
    • 70449725229 scopus 로고    scopus 로고
    • Characterization of homologs of the small RNA SgrS reveals diversity in function
    • Wadler CS, Vanderpool CK. 2009. Characterization of homologs of the small RNA SgrS reveals diversity in function. Nucleic Acids Res. 37:5477-5485.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5477-5485
    • Wadler, C.S.1    Vanderpool, C.K.2
  • 44
    • 0022917641 scopus 로고
    • Host/vector interactions which affect the viability of recombinant phage lambda clones
    • Wertman KF, Wyman AR, Botstein D. 1986. Host/vector interactions which affect the viability of recombinant phage lambda clones. Gene 49: 253-262.
    • (1986) Gene , vol.49 , pp. 253-262
    • Wertman, K.F.1    Wyman, A.R.2    Botstein, D.3
  • 45
    • 33344466006 scopus 로고    scopus 로고
    • Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution
    • Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW. 2006. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J. Mol. Biol. 357:509-523.
    • (2006) J. Mol. Biol. , vol.357 , pp. 509-523
    • Wood, Z.A.1    Weaver, L.H.2    Brown, P.H.3    Beckett, D.4    Matthews, B.W.5
  • 46
    • 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, 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
  • 47
    • 0028307533 scopus 로고
    • Kinetics of biotinyl-5=-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex
    • Xu Y, Beckett D. 1994. Kinetics of biotinyl-5=-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex. Biochemistry 33:7354-7360.
    • (1994) Biochemistry , vol.33 , pp. 7354-7360
    • Xu, Y.1    Beckett, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.