메뉴 건너뛰기




Volumn 5, Issue 12, 2010, Pages

Specificity of the E. coli LysR-type transcriptional regulators

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN; PROTEIN LYSR TYPE TRANSCRIPTIONAL REGULATOR; THIOREDOXIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA; HYBRID PROTEIN; LYSR PROTEIN, BACTERIA; TRANSCRIPTION FACTOR;

EID: 78650890765     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015189     Document Type: Article
Times cited : (25)

References (28)
  • 3
    • 0027446708 scopus 로고
    • Molecular biology of the LysR family of transcriptional regulators
    • Schell MA (1993) Molecular biology of the LysR family of transcriptional regulators. Annu Rev Microbiol 47: 597-626.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 597-626
    • Schell, M.A.1
  • 4
    • 0342333739 scopus 로고
    • OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins
    • Christman MF, Storz G, Ames BN (1989) OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci USA 86: 3484-3488.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3484-3488
    • Christman, M.F.1    Storz, G.2    Ames, B.N.3
  • 5
    • 0031958208 scopus 로고    scopus 로고
    • Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcrip-tional activator
    • Collier LS, Gaines GL, 3rd, Neidle EL (1998) Regulation of benzoate degradation in Acinetobacter sp. strain ADP1 by BenM, a LysR-type transcrip-tional activator. J Bacteriol 180: 2493-2501.
    • (1998) J Bacteriol , vol.180 , pp. 2493-2501
    • Collier, L.S.1    Gaines, G.L.2    Neidle, E.L.3
  • 6
    • 0028865450 scopus 로고
    • CatM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus
    • Romero-Arroyo CE, Schell MA, Gaines GL, 3rd, Neidle EL (1995) catM encodes a LysR-type transcriptional activator regulating catechol degradation in Acinetobacter calcoaceticus. J Bacteriol 177: 5891-5898.
    • (1995) J Bacteriol , vol.177 , pp. 5891-5898
    • Romero-Arroyo, C.E.1    Schell, M.A.2    Gaines, G.L.3    Neidle, E.L.4
  • 8
    • 0032798521 scopus 로고    scopus 로고
    • A Vibrio cholerae LysR homolog, AphB, cooperates with AphA at the tcpPH promoter to activate expression of the ToxR virulence cascade
    • Kovacikova G, Skorupski K (1999) A Vibrio cholerae LysR homolog, AphB, cooperates with AphA at the tcpPH promoter to activate expression of the ToxR virulence cascade. J Bacteriol 181: 4250-4256.
    • (1999) J Bacteriol , vol.181 , pp. 4250-4256
    • Kovacikova, G.1    Skorupski, K.2
  • 9
    • 33751376744 scopus 로고    scopus 로고
    • MvfR, a key Pseudomonas aeruginosa pathogenicity LTTR-class regulatory protein, has dual ligands
    • Xiao G, Deziel E, He J, Lepine F, Lesic B, et al. (2006) MvfR, a key Pseudomonas aeruginosa pathogenicity LTTR-class regulatory protein, has dual ligands. Mol Microbiol 62: 1689-1699.
    • (2006) Mol Microbiol , vol.62 , pp. 1689-1699
    • Xiao, G.1    Deziel, E.2    He, J.3    Lepine, F.4    Lesic, B.5
  • 10
    • 33745269562 scopus 로고    scopus 로고
    • Mutation analysis of the Pseudomonas aeruginosa mvfR and pqsABCDE gene promoters demonstrates complex quorum-sensing circuitry
    • Xiao G, He J, Rahme LG (2006) Mutation analysis of the Pseudomonas aeruginosa mvfR and pqsABCDE gene promoters demonstrates complex quorum-sensing circuitry. Microbiology 152: 1679-1686.
    • (2006) Microbiology , vol.152 , pp. 1679-1686
    • Xiao, G.1    He, J.2    Rahme, L.G.3
  • 11
    • 58949097886 scopus 로고    scopus 로고
    • Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins
    • Maddocks SE, Oyston PC (2008) Structure and function of the LysR-type transcriptional regulator (LTTR) family proteins. Microbiology 154: 3609-3623.
    • (2008) Microbiology , vol.154 , pp. 3609-3623
    • Maddocks, S.E.1    Oyston, P.C.2
  • 12
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, et al. (2001) Structural basis of the redox switch in the OxyR transcription factor. Cell 105: 103-113.
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5
  • 13
    • 1142267975 scopus 로고    scopus 로고
    • Crystallization of the effector-binding domains of BenM and CatM, LysR-type transcriptional regulators from Acinetobacter sp. ADP1
    • Clark T, Haddad S, Neidle E, Momany C (2004) Crystallization of the effector-binding domains of BenM and CatM, LysR-type transcriptional regulators from Acinetobacter sp. ADP1. Acta Crystallogr D Biol Crystallogr 60: 105-108.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 105-108
    • Clark, T.1    Haddad, S.2    Neidle, E.3    Momany, C.4
  • 14
    • 0344406163 scopus 로고    scopus 로고
    • Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: Unusual combination of two subunit forms and molecular bases for causing and changing DNA bend
    • Muraoka S, Okumura R, Ogawa N, Nonaka T, Miyashita K, et al. (2003) Crystal structure of a full-length LysR-type transcriptional regulator, CbnR: unusual combination of two subunit forms and molecular bases for causing and changing DNA bend. J Mol Biol 328: 555-566.
    • (2003) J Mol Biol , vol.328 , pp. 555-566
    • Muraoka, S.1    Okumura, R.2    Ogawa, N.3    Nonaka, T.4    Miyashita, K.5
  • 15
    • 2942741120 scopus 로고    scopus 로고
    • Development of a bacterial biosensor for nitrotoluenes: The crystal structure of the transcriptional regulator DntR
    • Smirnova IA, Dian C, Leonard GA, McSweeney S, Birse D, et al. (2004) Development of a bacterial biosensor for nitrotoluenes: the crystal structure of the transcriptional regulator DntR. J Mol Biol 340: 405-418.
    • (2004) J Mol Biol , vol.340 , pp. 405-418
    • Smirnova, I.A.1    Dian, C.2    Leonard, G.A.3    McSweeney, S.4    Birse, D.5
  • 16
    • 33751222901 scopus 로고    scopus 로고
    • Structural basis of the sulphate starvation response in E. coli: Crystal structure and mutational analysis of the cofactor-binding domain of the Cbl transcriptional regulator
    • Stec E, Witkowska-Zimny M, Hryniewicz MM, Neumann P, Wilkinson AJ, et al. (2006) Structural basis of the sulphate starvation response in E. coli: crystal structure and mutational analysis of the cofactor-binding domain of the Cbl transcriptional regulator. J Mol Biol 364: 309-322.
    • (2006) J Mol Biol , vol.364 , pp. 309-322
    • Stec, E.1    Witkowska-Zimny, M.2    Hryniewicz, M.M.3    Neumann, P.4    Wilkinson, A.J.5
  • 17
    • 0031571642 scopus 로고    scopus 로고
    • The structure of the cofactor-binding fragment of the LysR family member, CysB: A familiar fold with a surprising subunit arrangement
    • Tyrrell R, Verschueren KH, Dodson EJ, Murshudov GN, Addy C, et al. (1997) The structure of the cofactor-binding fragment of the LysR family member, CysB: a familiar fold with a surprising subunit arrangement. Structure 5: 1017-1032.
    • (1997) Structure , vol.5 , pp. 1017-1032
    • Tyrrell, R.1    Verschueren, K.H.2    Dodson, E.J.3    Murshudov, G.N.4    Addy, C.5
  • 18
  • 19
    • 0030929788 scopus 로고    scopus 로고
    • Buried asparagines determine the dimerization specificities of leucine zipper mutants
    • Zeng X, Herndon AM, Hu JC (1997) Buried asparagines determine the dimerization specificities of leucine zipper mutants. Proc Natl Acad Sci USA 94: 3673-3678.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3673-3678
    • Zeng, X.1    Herndon, A.M.2    Hu, J.C.3
  • 20
    • 10744222824 scopus 로고    scopus 로고
    • Identification and mapping of self-assembling protein domains encoded by the Escherichia coli K-12 genome by use of lambda repressor fusions
    • Marino-Ramirez L, Minor JL, Reading N, Hu JC (2004) Identification and mapping of self-assembling protein domains encoded by the Escherichia coli K-12 genome by use of lambda repressor fusions. J Bacteriol 186: 1311-1319.
    • (2004) J Bacteriol , vol.186 , pp. 1311-1319
    • Marino-Ramirez, L.1    Minor, J.L.2    Reading, N.3    Hu, J.C.4
  • 21
    • 70350474995 scopus 로고    scopus 로고
    • The oligomerization of CynR in Escherichia coli
    • Knapp GS, Hu JC (2009) The oligomerization of CynR in Escherichia coli. Protein Sci 18: 2307-2315.
    • (2009) Protein Sci , vol.18 , pp. 2307-2315
    • Knapp, G.S.1    Hu, J.C.2
  • 22
    • 58149460239 scopus 로고    scopus 로고
    • The oligomerization of OxyR in Escherichia coli
    • Knapp GS, Tsai JW, Hu JC (2009) The oligomerization of OxyR in Escherichia coli. Protein Sci 18: 101-107.
    • (2009) Protein Sci , vol.18 , pp. 101-107
    • Knapp, G.S.1    Tsai, J.W.2    Hu, J.C.3
  • 24
    • 0021282250 scopus 로고
    • Cloning vectors that yield high levels of single-stranded DNA for rapid DNA sequencing
    • Zagursky RJ, Berman ML (1984) Cloning vectors that yield high levels of single-stranded DNA for rapid DNA sequencing. Gene 27: 183-191.
    • (1984) Gene , vol.27 , pp. 183-191
    • Zagursky, R.J.1    Berman, M.L.2
  • 25
    • 0037209208 scopus 로고    scopus 로고
    • Screening peptide/protein libraries fused to the lambda repressor DNA-binding domain in
    • Marino-Ramirez L, Campbell L, Hu JC (2003) Screening peptide/protein libraries fused to the lambda repressor DNA-binding domain in E. coli cells. Methods Mol Biol 205: 235-250.
    • (2003) E. Coli Cells. Methods Mol Biol , vol.205 , pp. 235-250
    • Marino-Ramirez, L.1    Campbell, L.2    Hu, J.C.3
  • 26
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban MJ, Cohen SN (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol 138: 179-207.
    • (1980) J Mol Biol , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 28
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.