메뉴 건너뛰기




Volumn 35, Issue 12, 2007, Pages 3945-3952

Efficient and exclusive induction of Tet repressor by the oligopeptide Tip results from co-variation of their interaction site

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINO ACID; OLIGOPEPTIDE; REPRESSOR PROTEIN; TETRACYCLINE; TETRACYCLINE DERIVATIVE; THIOREDOXIN; TRANSCRIPTION FACTOR; HYBRID PROTEIN; PEPBS1 AC PEPTIDE; PEPBS1-AC PEPTIDE; PEPTIDE; TETRACYCLINE RESISTANCE ENCODING TRANSPOSON REPRESSOR PROTEIN; TETRACYCLINE RESISTANCE-ENCODING TRANSPOSON REPRESSOR PROTEIN; UNCLASSIFIED DRUG;

EID: 34547621029     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm357     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 3142582002 scopus 로고    scopus 로고
    • Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: Rotation mechanism for transmembrane signal transduction
    • Ogawa,H., Qiu,Y., Ogata,C.M. and Misono,K.S. (2004) Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. J. Biol. Chem., 279, 28625-28631.
    • (2004) J. Biol. Chem , vol.279 , pp. 28625-28631
    • Ogawa, H.1    Qiu, Y.2    Ogata, C.M.3    Misono, K.S.4
  • 2
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action
    • Rosenfeld,Y., Papo,N. and Shai,Y. (2006) Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action. J. Biol. Chem., 281 1636-1643.
    • (2006) J. Biol. Chem , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3
  • 3
    • 33750634194 scopus 로고    scopus 로고
    • Functional characterization of a three-component regulatory system involved in quorum sensing-based regulation of peptide antibiotic production in Carnobacterium maltaromaticum
    • Rohde,B.H. and Quadri,L.E. (2006) Functional characterization of a three-component regulatory system involved in quorum sensing-based regulation of peptide antibiotic production in Carnobacterium maltaromaticum. BMC Microbiol., 6, 93.
    • (2006) BMC Microbiol , vol.6 , pp. 93
    • Rohde, B.H.1    Quadri, L.E.2
  • 5
    • 5444264830 scopus 로고    scopus 로고
    • Identification by phage display selection of a short peptide able to inhibit only the strand transfer reaction catalyzed by human immunodeficiency virus type 1 integrase
    • Desjobert,C., de Soultrait,V.R., Faure,A., Parissi,V., Litvak,S., Tarrago-Litvak,L. and Fournier,M. (2004) Identification by phage display selection of a short peptide able to inhibit only the strand transfer reaction catalyzed by human immunodeficiency virus type 1 integrase. Biochemistry, 43, 13097-13105.
    • (2004) Biochemistry , vol.43 , pp. 13097-13105
    • Desjobert, C.1    de Soultrait, V.R.2    Faure, A.3    Parissi, V.4    Litvak, S.5    Tarrago-Litvak, L.6    Fournier, M.7
  • 6
    • 0037211265 scopus 로고    scopus 로고
    • Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library
    • Ho,K.L., Yusoff,K., Seow,H.F. and Tan,W.S. (2003) Selection of high affinity ligands to hepatitis B core antigen from a phage-displayed cyclic peptide library. J. Med. Virol., 69, 27-32.
    • (2003) J. Med. Virol , vol.69 , pp. 27-32
    • Ho, K.L.1    Yusoff, K.2    Seow, H.F.3    Tan, W.S.4
  • 9
    • 4143098147 scopus 로고    scopus 로고
    • In vitro selection of a peptide with high selectivity for cardiomyocytes in vivo
    • McGuire,M.J., Samli,K.N., Johnston,S.A. and Brown,K.C. (2004) In vitro selection of a peptide with high selectivity for cardiomyocytes in vivo. J. Mol. Biol., 342, 171-182.
    • (2004) J. Mol. Biol , vol.342 , pp. 171-182
    • McGuire, M.J.1    Samli, K.N.2    Johnston, S.A.3    Brown, K.C.4
  • 10
    • 21644478380 scopus 로고    scopus 로고
    • A peptide triggers allostery in Tet repressor by binding to a unique site
    • Klotzsche,M., Berens,C. and Hillen,W. (2005) A peptide triggers allostery in Tet repressor by binding to a unique site. J. Biol. Chem., 280, 24591-24599.
    • (2005) J. Biol. Chem , vol.280 , pp. 24591-24599
    • Klotzsche, M.1    Berens, C.2    Hillen, W.3
  • 11
    • 7944232688 scopus 로고    scopus 로고
    • Gene regulation by tetracyclines
    • Berens,C. and Hillen,W. (2004) Gene regulation by tetracyclines. Genet. Eng. (N.Y.), 26, 255-277.
    • (2004) Genet. Eng. (N.Y.) , vol.26 , pp. 255-277
    • Berens, C.1    Hillen, W.2
  • 13
    • 0029952367 scopus 로고    scopus 로고
    • Tetracycline analogs affecting binding to Tn10 encoded Tet repressor trigger the same mechanism of induction
    • Lederer,T., Kintrup,M., Takahashi,M., Sum,P.E., Ellestad,G.A. and Hillen,W. (1996) Tetracycline analogs affecting binding to Tn10 encoded Tet repressor trigger the same mechanism of induction. Biochemistry, 35, 7439-7446.
    • (1996) Biochemistry , vol.35 , pp. 7439-7446
    • Lederer, T.1    Kintrup, M.2    Takahashi, M.3    Sum, P.E.4    Ellestad, G.A.5    Hillen, W.6
  • 14
    • 34047092739 scopus 로고    scopus 로고
    • How an agonist peptide mimics the antibiotic tetracycline to induce Tet-repressor
    • Luckner,S.R., Klotzsche,M., Berens,C., Hillen,W. and Muller,Y.A. (2007) How an agonist peptide mimics the antibiotic tetracycline to induce Tet-repressor. J. Mol. Biol., 368, 780-790.
    • (2007) J. Mol. Biol , vol.368 , pp. 780-790
    • Luckner, S.R.1    Klotzsche, M.2    Berens, C.3    Hillen, W.4    Muller, Y.A.5
  • 15
    • 33747335912 scopus 로고    scopus 로고
    • Random insertion of a TetR-inducing peptide tag into Escherichia coli proteins allows analysis of protein levels by induction of reporter gene expression
    • Schlicht,M., Berens,C., Daam,J. and Hillen,W. (2006) Random insertion of a TetR-inducing peptide tag into Escherichia coli proteins allows analysis of protein levels by induction of reporter gene expression. Appl. Environ. Microbiol., 72, 5637-5642.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 5637-5642
    • Schlicht, M.1    Berens, C.2    Daam, J.3    Hillen, W.4
  • 16
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan,D. (1983) Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol., 166, 557-580.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 17
    • 0019586165 scopus 로고
    • Mechanism of action of the lexA gene product
    • Brent,R. and Ptashne,M. (1981) Mechanism of action of the lexA gene product. Proc. Natl Acad. Sci. USA, 78, 4204-4208.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 4204-4208
    • Brent, R.1    Ptashne, M.2
  • 18
    • 0023798660 scopus 로고
    • Mutations in the Tn10 tet repressor that interfere with induction. Location of the tetracycline-binding domain
    • Smith,L.D. and Bertrand,K.P. (1988) Mutations in the Tn10 tet repressor that interfere with induction. Location of the tetracycline-binding domain. J. Mol. Biol., 203, 949-959.
    • (1988) J. Mol. Biol , vol.203 , pp. 949-959
    • Smith, L.D.1    Bertrand, K.P.2
  • 19
    • 0024197658 scopus 로고
    • A threonine to alanine exchange at position 40 of Tet repressor alters the recognition of the sixth base pair of tet operator from GC to AT
    • Altschmied,L., Baumeister,R., Pfleiderer,K. and Hillen,W. (1988) A threonine to alanine exchange at position 40 of Tet repressor alters the recognition of the sixth base pair of tet operator from GC to AT. EMBO J., 7, 4011-4017.
    • (1988) EMBO J , vol.7 , pp. 4011-4017
    • Altschmied, L.1    Baumeister, R.2    Pfleiderer, K.3    Hillen, W.4
  • 20
    • 0025995751 scopus 로고
    • Selection for Tn10 Tet repressor binding to tet operator in Escherichia coli: Isolation of temperature-sensitive mutants and combinatorial mutagenesis in the DNA binding motif
    • Wissmann,A., Wray,L.V.Jr, Somaggio,U., Baumeister,R., Geissendörfer,M. and Hillen,W. (1991) Selection for Tn10 Tet repressor binding to tet operator in Escherichia coli: isolation of temperature-sensitive mutants and combinatorial mutagenesis in the DNA binding motif. Genetics, 128, 225-232.
    • (1991) Genetics , vol.128 , pp. 225-232
    • Wissmann, A.1    Wray Jr, L.V.2    Somaggio, U.3    Baumeister, R.4    Geissendörfer, M.5    Hillen, W.6
  • 22
    • 0030843812 scopus 로고    scopus 로고
    • CCR: A rapid and simple approach for mutation detection
    • Bi,W. and Stambrook,P.J. (1997) CCR: A rapid and simple approach for mutation detection. Nucleic Acids Res., 25, 2949-2951.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2949-2951
    • Bi, W.1    Stambrook, P.J.2
  • 23
    • 0033525890 scopus 로고    scopus 로고
    • Solvent-exposed residues in the Tet repressor (TetR) four-helix bundle contribute to subunit recognition and dimer stability
    • Schnappinger,D., Schubert,P., Berens,C., Pfleiderer,K. and Hillen,W. (1999) Solvent-exposed residues in the Tet repressor (TetR) four-helix bundle contribute to subunit recognition and dimer stability. J. Biol. Chem., 274, 6405-6410.
    • (1999) J. Biol. Chem , vol.274 , pp. 6405-6410
    • Schnappinger, D.1    Schubert, P.2    Berens, C.3    Pfleiderer, K.4    Hillen, W.5
  • 24
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA
    • Miller,J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 25
    • 0023135722 scopus 로고
    • Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
    • Ben-Bassat,A., Bauer,K., Chang,S.Y., Myambo,K., Boosman,A. and Chang,S. (1987) Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol., 169, 751-757.
    • (1987) J. Bacteriol , vol.169 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.Y.3    Myambo, K.4    Boosman, A.5    Chang, S.6
  • 26
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel,P.H., Schmitter,M.J., Dessen,P., Fayat,G. and Blanquet,S. (1989) Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl Acad. Sci. USA, 86, 8247-8251.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 27
    • 0028970885 scopus 로고
    • sbmC, a stationary-phase induced SOS Escherichia coli gene, whose product protects cells from the DNA replication inhibitor microcin B17
    • Baquero,M.R., Bouzon,M., Varea,J. and Moreno,F. (1995) sbmC, a stationary-phase induced SOS Escherichia coli gene, whose product protects cells from the DNA replication inhibitor microcin B17. Mol. Microbiol., 18, 301-311.
    • (1995) Mol. Microbiol , vol.18 , pp. 301-311
    • Baquero, M.R.1    Bouzon, M.2    Varea, J.3    Moreno, F.4
  • 28
    • 0037093641 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli SbmC protein that protects cells from the DNA replication inhibitor microcin B17
    • Romanowski,M.J., Gibney,S.A. and Burley,S.K. (2002) Crystal structure of the Escherichia coli SbmC protein that protects cells from the DNA replication inhibitor microcin B17. Proteins, 47, 403-07.
    • (2002) Proteins , vol.47 , pp. 403-407
    • Romanowski, M.J.1    Gibney, S.A.2    Burley, S.K.3
  • 29
    • 0038813712 scopus 로고    scopus 로고
    • Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells
    • Gupta,S. and Chatterji,D. (2003) Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells. J. Biol. Chem., 278, 5235-5241.
    • (2003) J. Biol. Chem , vol.278 , pp. 5235-5241
    • Gupta, S.1    Chatterji, D.2
  • 30
    • 0028244325 scopus 로고
    • Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance
    • Hinrichs,W., Kisker,C., Düvel,M., Müller,A., Tovar,K., Hillen,W. and Saenger,W. (1994) Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance. Science, 264 418-420.
    • (1994) Science , vol.264 , pp. 418-420
    • Hinrichs, W.1    Kisker, C.2    Düvel, M.3    Müller, A.4    Tovar, K.5    Hillen, W.6    Saenger, W.7
  • 31
    • 0028915778 scopus 로고
    • Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heit capacity of the native protein
    • Ladbury,J.E., Wynn,R., Thomson,J.A. and Sturtevant,J.M. (1995) Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heit capacity of the native protein. Biochemistry, 34, 2148-2152.
    • (1995) Biochemistry , vol.34 , pp. 2148-2152
    • Ladbury, J.E.1    Wynn, R.2    Thomson, J.A.3    Sturtevant, J.M.4
  • 32
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interaction in proteins
    • Nakamura,H. (1996) Roles of electrostatic interaction in proteins. Q. Rev. Biophys., 29, 1-90.
    • (1996) Q. Rev. Biophys , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 33
    • 27144555357 scopus 로고    scopus 로고
    • Regulation of translation via mRNA structure in prokaryotes and eukaryotes
    • Kozak,M. (2005) Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene, 361, 13-37.
    • (2005) Gene , vol.361 , pp. 13-37
    • Kozak, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.