메뉴 건너뛰기




Volumn 409, Issue 3, 2011, Pages 311-332

The design involved in PapI and Lrp regulation of the pap operon

Author keywords

dam; deoxyadenosine methylase; heteronuclear single quantum coherence; HSQC; leucine responsive regulatory protein; Lrp; Lrp DNA binding domain; LrpDBD; NOE; NOE spectroscopy; NOESY; nuclear Overhauser enhancement; pap; pyelonephritis associated pili

Indexed keywords

DNA BINDING PROTEIN; LEUCINE RESPONSIVE REGULATORY PROTEIN; PROTEIN PAPI; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 79956133928     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.01.058     Document Type: Article
Times cited : (11)

References (43)
  • 1
    • 0028835104 scopus 로고
    • Leucine-responsive regulatory protein: A global regulator of gene expression in E. coli
    • Newman E.B. Leucine-responsive regulatory protein: a global regulator of gene expression in E. coli Annu. Rev. Microbiol. 49 1995 747 775
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 747-775
    • Newman, E.B.1
  • 2
    • 0028111825 scopus 로고
    • The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli
    • Calvo J.M., and Matthews R.G. The leucine-responsive regulatory protein, a global regulator of metabolism in Escherichia coli Microbiol. Rev. 58 1995 466 490
    • (1995) Microbiol. Rev. , vol.58 , pp. 466-490
    • Calvo, J.M.1    Matthews, R.G.2
  • 3
    • 0037174983 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12
    • Hung S.P., Baldi P., and Hatfield G.W. Global gene expression profiling in Escherichia coli K12 J. Biol. Chem. 277 2002 40309 40323
    • (2002) J. Biol. Chem. , vol.277 , pp. 40309-40323
    • Hung, S.P.1    Baldi, P.2    Hatfield, G.W.3
  • 4
    • 33846839291 scopus 로고    scopus 로고
    • Structure of the Escherichia coli Leucine-responsive Regulatory Protein Lrp Reveals a Novel Octameric Assembly
    • DOI 10.1016/j.jmb.2006.12.032, PII S0022283606017074
    • de los Rios S., and Perona J.J. Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly J. Mol. Biol. 366 2007 1589 1602 (Pubitemid 46215612)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.5 , pp. 1589-1602
    • De Los Rios, S.1    Perona, J.J.2
  • 6
    • 0027537042 scopus 로고
    • Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine
    • Platko J., and Calvo J.M. Mutations affecting the ability of Escherichia coli Lrp to bind DNA, activate transcription, or respond to leucine J. Bacteriol. 175 1993 1110 1117 (Pubitemid 23060149)
    • (1993) Journal of Bacteriology , vol.175 , Issue.4 , pp. 1110-1117
    • Platko, J.V.1    Calvo, J.M.2
  • 7
    • 0027461910 scopus 로고
    • Lrp, a global regulatory protein of Escherichia coli, binds co-operatively to multiple sites and activates transcription of ilvIH
    • DOI 10.1006/jmbi.1993.1036
    • Wang Q., and Calvo J.M. Lrp, a global regulatory protein of Escherichia coli, binds co-operatively to multiple sites and activates transcription of ilvIH J. Mol. Biol. 229 1993 306 318 (Pubitemid 23080382)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.2 , pp. 306-318
    • Wang, Q.1    Calvo, J.M.2
  • 8
    • 0027516833 scopus 로고
    • Organization of Lrp-binding sites upstream of ilvIH in Salmonella typhimurium
    • Wang Q., Sacco M., Ricca E., Lago C.T., De Felice M., and Calvo J.M. Organization of Lrp-binding sites upstream of ilvIH in Salmonella typhimurium Mol. Microbiol. 7 1993 883 891 (Pubitemid 23101401)
    • (1993) Molecular Microbiology , vol.7 , Issue.6 , pp. 883-891
    • Wang, Q.1    Sacco, M.2    Ricca, E.3    Lago, C.T.4    DeFelice, M.5    Calvo, J.M.6
  • 9
    • 0029127850 scopus 로고
    • A consensus sequence for binding of Lrp to DNA
    • Cui Y., Wang Q., Stormo G.D., and Calvo J.M. A consensus sequence for binding of Lrp to DNA J. Bacteriol. 177 1995 4872 4880
    • (1995) J. Bacteriol. , vol.177 , pp. 4872-4880
    • Cui, Y.1    Wang, Q.2    Stormo, G.D.3    Calvo, J.M.4
  • 12
    • 0027417863 scopus 로고
    • Regulation of pyelonephritis-associated pili phase-variation in Escherichia coli: Binding of the PapI and the Lrp regulatory proteins is controlled by DNA methylation
    • DOI 10.1111/j.1365-2958.1993.tb01145.x
    • Nou X., Skinner B., Braaten B., Blyn L., Hirsch D., and Low D. Regulation of pyelonephritis-associated pili phase-variation in Escherichia coli: binding of the PapI and the Lrp regulatory proteins is controlled by DNA methylation Mol. Microbiol. 7 1993 545 553 (Pubitemid 23062581)
    • (1993) Molecular Microbiology , vol.7 , Issue.4 , pp. 545-553
    • Nou, X.1    Skinner, B.2    Braaten, B.3    Blyn, L.4    Hirsch, D.5    Low, D.6
  • 13
    • 0028089165 scopus 로고
    • Methylation patterns in pap regulatory DNA control pyelonephritis- associated pili phase variation in E. coli
    • Braaten B.A., Nou X., Kaltenbach L.S., and Low D.A. Methylation patterns in pap regulatory DNA control pyelonephritis-associated pili phase variation in E. coli Cell 76 1994 577 588
    • (1994) Cell , vol.76 , pp. 577-588
    • Braaten, B.A.1    Nou, X.2    Kaltenbach, L.S.3    Low, D.A.4
  • 14
    • 0026073299 scopus 로고
    • Evidence for a methylation-blocking factor (mbf) locus involved in pap pilus expression and phase variation in Escherichia coli
    • Braaten B.A., Blyn L.B., Skinner B.S., and Low D.A. Evidence for a methylation-blocking factor (mbf) locus involved in pap pilus expression and phase variation in Escherichia coli J. Bacteriol. 173 1991 1789 1800
    • (1991) J. Bacteriol. , vol.173 , pp. 1789-1800
    • Braaten, B.A.1    Blyn, L.B.2    Skinner, B.S.3    Low, D.A.4
  • 15
    • 0028845957 scopus 로고
    • Differential binding of Lrp to two sets of pap DNA binding sites mediated by Pap i regulates Pap phase variation in Escherichia coli
    • Nou X., Braaten B., Kaltenbach L., and Low D.A. Differential binding of Lrp to two sets of pap DNA binding sites mediated by Pap I regulates Pap phase variation in Escherichia coli EMBO J. 14 1995 5785 5797
    • (1995) EMBO J. , vol.14 , pp. 5785-5797
    • Nou, X.1    Braaten, B.2    Kaltenbach, L.3    Low, D.A.4
  • 16
    • 0028798948 scopus 로고
    • Specific binding of PapI to Lrp-pap DNA complexes
    • Kaltenbach L.S., Braaten B.A., and Low D.A. Specific binding of PapI to Lrp-pap DNA complexes J. Bacteriol. 177 1995 6449 6455
    • (1995) J. Bacteriol. , vol.177 , pp. 6449-6455
    • Kaltenbach, L.S.1    Braaten, B.A.2    Low, D.A.3
  • 17
    • 0022435178 scopus 로고
    • Transcriptional activation of a Pap pilus virulence operon from uropathogenic Escherichia coli
    • Baga M., Goransson M., Normark S., and Uhlin B.E. Transcriptional activation of a Pap pilus virulence operon from uropathogenic Escherichia coli EMBO J. 4 1985 3887 3893
    • (1985) EMBO J. , vol.4 , pp. 3887-3893
    • Baga, M.1    Goransson, M.2    Normark, S.3    Uhlin, B.E.4
  • 18
    • 33845782496 scopus 로고    scopus 로고
    • Solution Structure of Escherichia coli PapI, a Key Regulator of the Pap Pili Phase Variation
    • DOI 10.1016/j.jmb.2006.10.066, PII S002228360601446X
    • Kawamura T., Le L.U., Zhou H., and Dahlquist F.W. Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation J. Mol. Biol. 365 2007 1130 1142 (Pubitemid 46014187)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.4 , pp. 1130-1142
    • Kawamura, T.1    Le, L.U.K.2    Zhou, H.3    Dahlquist, F.W.4
  • 19
    • 36749036126 scopus 로고    scopus 로고
    • Feast/Famine Regulation by Transcription Factor FL11 for the Survival of the Hyperthermophilic Archaeon Pyrococcus OT3
    • DOI 10.1016/j.str.2007.10.015, PII S0969212607004200
    • Yokoyama K., Ishijima S.A., Koike H., Kurihara C., Shimowasa A., and Kabasawa M. Feast/famine regulation by transcription factor FL11 for the survival of the hyperthermophilic archaeon Pyrococcus OT3 Structure 15 2007 1542 1554 (Pubitemid 350213417)
    • (2007) Structure , vol.15 , Issue.12 , 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
  • 20
    • 0242266619 scopus 로고    scopus 로고
    • The mechanism by which DNA adenine methylase and PapI activate the Pap epigenetic switch
    • DOI 10.1016/S1097-2765(03)00383-6
    • Hernday A.D., Braaten B.A., and Low D.A. The mechanism by which DNA adenine methylase and PapI activate the pap epigenetic switch Mol. Cell 12 2004 947 957 (Pubitemid 37352787)
    • (2003) Molecular Cell , vol.12 , Issue.4 , pp. 947-957
    • Hernday, A.D.1    Braaten, B.A.2    Low, D.A.3
  • 21
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer E.P., and Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J. Am. Chem. Soc. 114 1992 10663 10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, E.P.2    Saarinen, T.3
  • 23
    • 68049084862 scopus 로고    scopus 로고
    • The DNA-recognition mode shared by archaeal feast/famine-regulatory protein revealed by the DNA-binding specificities of TvFL3, FL10, FL11 and Ss-LrpB
    • Yokoyama K., Nogami H., Kabasawa M., Ebihara S., Shimowasa A., and Hashimoto K. The DNA-recognition mode shared by archaeal feast/famine-regulatory protein revealed by the DNA-binding specificities of TvFL3, FL10, FL11 and Ss-LrpB Nucl. Acids Res. 37 2009 4407 4419
    • (2009) Nucl. Acids Res. , vol.37 , pp. 4407-4419
    • Yokoyama, K.1    Nogami, H.2    Kabasawa, M.3    Ebihara, S.4    Shimowasa, A.5    Hashimoto, K.6
  • 24
    • 0019152420 scopus 로고
    • The Pk antigen as receptor for the haemagglutinin of pyelonephritic Escherichia coli
    • DOI 10.1111/j.1574-6941.1980.tb01608.x
    • k antigen as receptor for the haemagglutinin of pyelonephritic Escherichia coli FEMS Microbiol. Lett. 7 1980 297 302 (Pubitemid 10049597)
    • (1980) FEMS Microbiology Letters , vol.7 , Issue.4 , pp. 297-302
    • Kallenius, G.1    Mollby, R.2    Svenson, S.B.3
  • 25
    • 0019221850 scopus 로고
    • Chemical identification of a glycosphingolipid receptor for Escherichia coli attaching to human urinary tract epithelial cells and agglutinating human erythrocytes
    • DOI 10.1016/0378-1097(80)90015-4
    • Leffler H., and Svanborg Edén C. Chemical identification of a glycosphingolipid receptor for Escherichia coli attaching to human urinary tract epithelial cells and agglutinating human erythrocytes FEMS Microbiol. Lett. 8 1980 127 134 (Pubitemid 10057684)
    • (1980) FEMS Microbiology Letters , vol.8 , Issue.3 , pp. 127-134
    • Leffler, H.1    Svanborg Eden, C.2
  • 26
    • 0035697276 scopus 로고    scopus 로고
    • Structural studies of Ets-1/Pax5 complex formation on DNA
    • DOI 10.1016/S1097-2765(01)00410-5
    • Garvie C.W., Hagman J., and Wolberger C. Structural studies of Ets-1/Pax5 complex formation on DNA Mol. Cell 8 2001 1267 1276 (Pubitemid 34084998)
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1267-1276
    • Garvie, C.W.1    Hagman, J.2    Wolberger, C.3
  • 27
    • 0027285868 scopus 로고
    • Lrp, a major regulatory protein in Escherichia coli, bends DNA and can organize the assembly of a higher-order nucleoprotein structure
    • Wang Q., and Calvo J.M. Lrp, a major regulatory protein in Escherichia coli, bends DNA and can organize the assembly of a higher-order nucleoprotein structure EMBO J. 12 1993 2495 2501 (Pubitemid 23194200)
    • (1993) EMBO Journal , vol.12 , Issue.6 , pp. 2495-2501
    • Wang, Q.1    Calvo, J.M.2
  • 28
    • 0001748180 scopus 로고
    • Resolution enhancement and spectral editing of uniformly 13C enriched proteins by homonuclear broadband 13C-13C decoupling
    • G.W. Vuister, and A. Bax Resolution enhancement and spectral editing of uniformly 13C enriched proteins by homonuclear broadband 13C-13C decoupling J. Magn. Reson. 98 1992 428 435
    • (1992) J. Magn. Reson. , vol.98 , pp. 428-435
    • Vuister, G.W.1    Bax, A.2
  • 29
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram D.R., and Kay L.E. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity J. Magn. Reson., Ser. B 103 1994 203 216
    • (1994) J. Magn. Reson., Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 30
    • 84890928276 scopus 로고
    • An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically- enriched proteins
    • Montelione G.T., Lyons B.A., Emerson S.D., and Tashiro M. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically-enriched proteins J. Am. Chem. Soc. 114 1992 10974 10975
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10974-10975
    • Montelione, G.T.1    Lyons, B.A.2    Emerson, S.D.3    Tashiro, M.4
  • 32
    • 0027568083 scopus 로고
    • A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments
    • Logan T.M., Olejniczak E.T., Xu R.X., and Fesik S.W. A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments J. Biomol. NMR 3 1993 225 231
    • (1993) J. Biomol. NMR , vol.3 , pp. 225-231
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 37
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • DOI 10.1016/0263-7855(96)00009-4
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 14 1996 51 55 (Pubitemid 26152976)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 39
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl Acad. Sci. USA 94 1997 12366 12371
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 41
    • 0001250026 scopus 로고
    • 1H 2D NMR spectra by interactive graphics
    • 1H 2D NMR spectra by interactive graphics J. Magn. Reson. 84 1989 627 633
    • (1989) J. Magn. Reson. , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 42
    • 0028204451 scopus 로고
    • Solution structure and dynamics of Ras p21·GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • Kraulis P.J., Domaille P.J., Campbell-Burk S.L., van Aken T., and Laue E.D. Solution structure and dynamics of Ras p21•GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy Biochemistry 33 1994 3515 3531 (Pubitemid 24115999)
    • (1994) Biochemistry , vol.33 , Issue.12 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 43
    • 0004062749 scopus 로고    scopus 로고
    • Wolfram Research, Inc. Version 6.0, Champaign, IL.
    • Wolfram Research, Inc. (2007). Mathematica, Version 6.0, Champaign, IL.
    • (2007) Mathematica


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.