메뉴 건너뛰기




Volumn 37, Issue 13, 2009, Pages 4407-4419

The DNA-recognition mode shared by archaeal feast/famine-regulatory proteins revealed by the DNA-binding specificities of TvFL3, FL10, FL11 and Ss-LrpB

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; FEAST FAMINE REGULATORY PROTEIN; GENE PRODUCT; GLYCINE; PROTEIN FL10; PROTEIN FL11; PROTEIN SS LRPB; PROTEIN TVFL3; REGULATOR PROTEIN; THREONINE; THYMINE; UNCLASSIFIED DRUG;

EID: 68049084862     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp378     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 1042302417 scopus 로고    scopus 로고
    • Structure and function of the feast/famine regulatory proteins, FFRPs
    • Suzuki,M. (2003) Structure and function of the feast/famine regulatory proteins, FFRPs. Proc. Jpn Acad., B79, 274-289.
    • (2003) Proc. Jpn Acad , vol.B79 , pp. 274-289
    • Suzuki, M.1
  • 5
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein: A global regulator of metabolism in Escherichia coli
    • Calvo,J.M. and Matthews,R.G. (1994) The leucine-responsive regulatory protein: A global regulator of metabolism in Escherichia coli. Microbiol. Rev., 58, 466-490.
    • (1994) Microbiol. Rev , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.G.2
  • 6
    • 0028835104 scopus 로고
    • Leucine-responsive regulatory protein: A global regulator of gene expression in E. coli
    • Newman,E.B. and Lin,R. (1995) Leucine-responsive regulatory protein: A global regulator of gene expression in E. coli. Ann. Rev. Microbiol. 49, 747-775.
    • (1995) Ann. Rev. Microbiol , vol.49 , pp. 747-775
    • Newman, E.B.1    Lin, R.2
  • 7
    • 58049200606 scopus 로고    scopus 로고
    • Genome-scale reconstruction of the Lrp regulatory network in Escherichia coli
    • Cho,B.-K., Barrett,C.L., Knight,E.M., Park, Y.S. and Palsson,B.Ø. (2008) Genome-scale reconstruction of the Lrp regulatory network in Escherichia coli. Proc. Natl Acad. Sci. USA, 105, 19462-19467.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 19462-19467
    • Cho, B.-K.1    Barrett, C.L.2    Knight, E.M.3    Park, Y.S.4    Palsson, B.5
  • 8
    • 36749036126 scopus 로고    scopus 로고
    • Feast/famine regulation by transcription factor FL11 for the survival of the hyperthermophilic archaeon Pyrococcus OT3
    • Yokoyama,K., Ishijima,S.A., Koike,H., Kurihara,C., Shimowasa,A., Kabasawa,M., Kawashima,T. and Suzuki,M. (2007) Feast/famine regulation by transcription factor FL11 for the survival of the hyperthermophilic archaeon Pyrococcus OT3. Structure, 15, 1542-1554.
    • (2007) Structure , vol.15 , pp. 1542-1554
    • Yokoyama, K.1    Ishijima, S.A.2    Koike, H.3    Kurihara, C.4    Shimowasa, A.5    Kabasawa, M.6    Kawashima, T.7    Suzuki, M.8
  • 9
    • 24944558886 scopus 로고    scopus 로고
    • Modulation of the sensitivity of FimB recombination to branched-chain amino acids and alanine in Escherichia coli K-12
    • Lahooti,M., Roesch,P.L. and Blomfield,I.C. (2005) Modulation of the sensitivity of FimB recombination to branched-chain amino acids and alanine in Escherichia coli K-12. J. Bacteriol., 187, 6273-6280.
    • (2005) J. Bacteriol , vol.187 , pp. 6273-6280
    • Lahooti, M.1    Roesch, P.L.2    Blomfield, I.C.3
  • 10
    • 35148829988 scopus 로고    scopus 로고
    • A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands
    • Okamura,H., Yokoyama,K., Koike,H., Yamada,M., Shimowasa,A., Kabasawa,M., Kawashima,T. and Suzuki,M. (2007) A structural code for discriminating between transcription signals revealed by the feast/famine regulatory protein DM1 in complex with ligands. Structure, 15, 1325-1338.
    • (2007) Structure , vol.15 , pp. 1325-1338
    • Okamura, H.1    Yokoyama, K.2    Koike, H.3    Yamada, M.4    Shimowasa, A.5    Kabasawa, M.6    Kawashima, T.7    Suzuki, M.8
  • 11
    • 59449096414 scopus 로고    scopus 로고
    • Interactions between the archaeal transcription repressor FL11 and its coregulatots lysine and arginine
    • Yamada,M., Ishijima,S.A. and Suzuki,M. (2009) Interactions between the archaeal transcription repressor FL11 and its coregulatots lysine and arginine. Proteins, 74, 520-525.
    • (2009) Proteins , vol.74 , pp. 520-525
    • Yamada, M.1    Ishijima, S.A.2    Suzuki, M.3
  • 12
    • 33846839291 scopus 로고    scopus 로고
    • Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly
    • de los Rios,S. and Perona,J.J. (2007) Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly. J. Mol. Biol., 366, 1589-1602.
    • (2007) J. Mol. Biol , vol.366 , pp. 1589-1602
    • de los1    Rios, S.2    Perona, J.J.3
  • 14
    • 0036464506 scopus 로고    scopus 로고
    • A Pyrococcus homolog of the leucine-responsive regulatory protein, LrpA, inhibits transcription by abrogating RNA polymerase recruitment
    • Dahlke,I. and Thomm,M. (2002) A Pyrococcus homolog of the leucine-responsive regulatory protein, LrpA, inhibits transcription by abrogating RNA polymerase recruitment. Nucleic Acids Res., 30 701-710.
    • (2002) Nucleic Acids Res , vol.30 , pp. 701-710
    • Dahlke, I.1    Thomm, M.2
  • 15
    • 0035863076 scopus 로고    scopus 로고
    • A thermostable platform for transcription regulation: The DNA-binding properties of two Lrp homologs from the hyperthermophilic archaeon Methanococcus jannaschiii
    • Ouhammouch,M. and Geiduschek,E.P. (2001) A thermostable platform for transcription regulation: The DNA-binding properties of two Lrp homologs from the hyperthermophilic archaeon Methanococcus jannaschiii. EMBO J., 20, 146-156.
    • (2001) EMBO J , vol.20 , pp. 146-156
    • Ouhammouch, M.1    Geiduschek, E.P.2
  • 16
    • 0037119358 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability
    • Brinkman,A.B., Bell,S.D., Lebbink,R.J., de Vos, W.M. and van der Oost,J. (2002) The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability. J. Biol. Chem., 277, 29537-29549.
    • (2002) J. Biol. Chem , vol.277 , pp. 29537-29549
    • Brinkman, A.B.1    Bell, S.D.2    Lebbink, R.J.3    de Vos, W.M.4    van der Oost, J.5
  • 17
    • 0036034720 scopus 로고    scopus 로고
    • High resolution contact probing of the Lrp-like DNA-binding protein Ss-Lrp from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2
    • Enoru-Eta,J., Gigot,D., Glansdorff,N. and Charlier,D. (2002) High resolution contact probing of the Lrp-like DNA-binding protein Ss-Lrp from the hyperthermoacidophilic crenarchaeote Sulfolobus solfataricus P2. Mol. Microbiol., 45, 1541-1555.
    • (2002) Mol. Microbiol , vol.45 , pp. 1541-1555
    • Enoru-Eta, J.1    Gigot, D.2    Glansdorff, N.3    Charlier, D.4
  • 18
    • 6344272907 scopus 로고    scopus 로고
    • Ss-LrpB, a novel Lrp-like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region
    • Peeters,E., Thia-Toong,T.L., Gigot,D., Maes,D. and Charlier,D. (2004) Ss-LrpB, a novel Lrp-like regulator of Sulfolobus solfataricus P2, binds cooperatively to three conserved targets in its own control region. Mol. Microbiol., 54, 321-336.
    • (2004) Mol. Microbiol , vol.54 , pp. 321-336
    • Peeters, E.1    Thia-Toong, T.L.2    Gigot, D.3    Maes, D.4    Charlier, D.5
  • 19
    • 33846913874 scopus 로고    scopus 로고
    • Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing
    • Peeters,E., Wartel,C., Maes,D. and Charlier,D. (2007) Analysis of the DNA-binding sequence specificity of the archaeal transcriptional regulator Ss-LrpB from Sulfolobus solfataricus by systematic mutagenesis and high resolution contact probing. Nucleic Acids Res. 35, 623-633.
    • (2007) Nucleic Acids Res , vol.35 , pp. 623-633
    • Peeters, E.1    Wartel, C.2    Maes, D.3    Charlier, D.4
  • 20
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk,C. and Gold,L. (1990) Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 249, 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 21
    • 11144313963 scopus 로고
    • Thermoplasma acidophilum and Thermoplasma volcanium sp. nov. from solfatara fields
    • Segerer,A., Langworthy,T.A. and Stetter,K.O. (1988) Thermoplasma acidophilum and Thermoplasma volcanium sp. nov. from solfatara fields. Syst. Appl. Microbiol., 10, 161-171.
    • (1988) Syst. Appl. Microbiol , vol.10 , pp. 161-171
    • Segerer, A.1    Langworthy, T.A.2    Stetter, K.O.3
  • 25
    • 33644606221 scopus 로고    scopus 로고
    • Comparison of foot-prints of FFRPs on promoters designed for autoregulation: FL10 (pot0377090, LrpA), FL11 (pot0434017), and Ss/Sa-Lrp
    • Suzuki,M. (2005) Comparison of foot-prints of FFRPs on promoters designed for autoregulation: FL10 (pot0377090, LrpA), FL11 (pot0434017), and Ss/Sa-Lrp. Proc. Jpn Acad., B81, 403-409.
    • (2005) Proc. Jpn Acad , vol.B81 , pp. 403-409
    • Suzuki, M.1
  • 26
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi,R., Krummel,B. and Saiki,R.K. (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acids Res., 16, 7351-7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 28
    • 0027377202 scopus 로고
    • The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility
    • König,P. and Richmond,T.J. (1993) The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol., 233, 139-154.
    • (1993) J. Mol. Biol , vol.233 , pp. 139-154
    • König, P.1    Richmond, T.J.2
  • 29
    • 0028773281 scopus 로고
    • A framework for the DNA-protein recognition code of the probe helix in transcription factors: The chemical and stereochemical rules
    • Suzuki,M. (1994) A framework for the DNA-protein recognition code of the probe helix in transcription factors: The chemical and stereochemical rules. Structure, 2, 317-326.
    • (1994) Structure , vol.2 , pp. 317-326
    • Suzuki, M.1
  • 31
    • 0000127073 scopus 로고
    • Sequence-specific recognition of double helical nucleic acids by proteins
    • Seeman,N.C., Rosenberg,J.M. and Rich,A. (1976) Sequence-specific recognition of double helical nucleic acids by proteins. Proc. Natl Acad. Sci. USA, 73, 804-808.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 804-808
    • Seeman, N.C.1    Rosenberg, J.M.2    Rich, A.3
  • 32
    • 0029041940 scopus 로고
    • Stereochemical basis of DNA bending by transcription factors
    • Suzuki,M. and Yagi,N. (1995) Stereochemical basis of DNA bending by transcription factors. Nucleic Acids Res., 23, 2083-2091.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2083-2091
    • Suzuki, M.1    Yagi, N.2
  • 33
    • 0029127850 scopus 로고
    • A consensus sequence for binding of Lrp to DNA
    • Cui,Y., Wang,Q., Stormo,G.D. and Calvo,J.M. (1995) A consensus sequence for binding of Lrp to DNA. J. Bacteriol., 177, 4872-4880.
    • (1995) J. Bacteriol , vol.177 , pp. 4872-4880
    • Cui, Y.1    Wang, Q.2    Stormo, G.D.3    Calvo, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.