메뉴 건너뛰기




Volumn 25, Issue 12, 2006, Pages 2930-2939

Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM

Author keywords

Conjugation; Crystal structure; F plasmid; Protonation; TraM

Indexed keywords

REGULATOR PROTEIN;

EID: 33745518716     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/sj.emboj.7601151     Document Type: Article
Times cited : (28)

References (57)
  • 1
    • 0027301892 scopus 로고
    • Repression of the traM gene of plasmid R100 by its own product and integration host factor at one of the two promoters
    • Abo T, Ohtsubo E (1993) Repression of the traM gene of plasmid R100 by its own product and integration host factor at one of the two promoters. J Bacteriol 175: 4466-4474
    • (1993) J Bacteriol , vol.175 , pp. 4466-4474
    • Abo, T.1    Ohtsubo, E.2
  • 3
    • 4944235151 scopus 로고    scopus 로고
    • Thirty-eight C-terminal amino acids of the coupling protein TraD of the F-like conjugative resistance plasmid R1 are required and sufficient to confer binding to the substrate selector protein TraM
    • Beranek A, Zettl M, Lorenzoni K, Schauer A, Manhart M, Koraimann G (2004) Thirty-eight C-terminal amino acids of the coupling protein TraD of the F-like conjugative resistance plasmid R1 are required and sufficient to confer binding to the substrate selector protein TraM. J Bacteriol 186: 6999-7006
    • (2004) J Bacteriol , vol.186 , pp. 6999-7006
    • Beranek, A.1    Zettl, M.2    Lorenzoni, K.3    Schauer, A.4    Manhart, M.5    Koraimann, G.6
  • 4
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC (1994) Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371: 37-43
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 5
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan DC, Fass D, Berger JM, Kim PS (1997) Core structure of gp41 from the HIV envelope glycoprotein. Cell 89: 263-273
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 7
    • 8544244142 scopus 로고    scopus 로고
    • Concomitant reconstitution of Tral-catalyzed DNA transesterase and DNA helicase activity in vitro
    • Csitkovits VC, Dermic D, Zechner EL (2004) Concomitant reconstitution of Tral-catalyzed DNA transesterase and DNA helicase activity in vitro. J Biol Chem 279: 45477-45484
    • (2004) J Biol Chem , vol.279 , pp. 45477-45484
    • Csitkovits, V.C.1    Dermic, D.2    Zechner, E.L.3
  • 8
    • 0026761399 scopus 로고
    • The TraM protein of the conjugative plasmid F binds to the origin of transfer of the F and ColE1 plasmids
    • Di Laurenzio L, Frost LS, Paranchych W (1992) The TraM protein of the conjugative plasmid F binds to the origin of transfer of the F and ColE1 plasmids. Mol Microbiol 6: 2951-2959
    • (1992) Mol Microbiol , vol.6 , pp. 2951-2959
    • Di Laurenzio, L.1    Frost, L.S.2    Paranchych, W.3
  • 9
    • 0039702020 scopus 로고    scopus 로고
    • The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro
    • Disque-Kochem C, Dreiseikelmann B (1997) The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro. J Bacteriol 179: 6133-6137
    • (1997) J Bacteriol , vol.179 , pp. 6133-6137
    • Disque-Kochem, C.1    Dreiseikelmann, B.2
  • 10
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol 276: 523-530
    • (1997) Methods Enzymol , vol.276 , pp. 523-530
    • Doublie, S.1
  • 11
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM, Kim PS (2001) Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 70: 777-810
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 12
    • 0019324561 scopus 로고
    • Characterisation of an in vivo system for nicking at the origin of conjugal DNA transfer of the sex factor F
    • Everett R, Willetts N (1980) Characterisation of an in vivo system for nicking at the origin of conjugal DNA transfer of the sex factor F. J Mol Biol 136: 129-150
    • (1980) J Mol Biol , vol.136 , pp. 129-150
    • Everett, R.1    Willetts, N.2
  • 13
    • 0033917122 scopus 로고    scopus 로고
    • Mobilization of chimeric oriT plasmids by F and R100-1: Role of relaxosome formation in defining plasmid specificity
    • Fekete RA, Frost LS (2000) Mobilization of chimeric oriT plasmids by F and R100-1: role of relaxosome formation in defining plasmid specificity. J Bacteriol 182: 4022-4027
    • (2000) J Bacteriol , vol.182 , pp. 4022-4027
    • Fekete, R.A.1    Frost, L.S.2
  • 14
    • 0037053306 scopus 로고    scopus 로고
    • Characterizing the DNA contacts and cooperative binding of F plasmid TraM to its cognate sites at oriT
    • Fekete RA, Frost LS (2002) Characterizing the DNA contacts and cooperative binding of F plasmid TraM to its cognate sites at oriT. J Biol Chem 277: 16705-16711
    • (2002) J Biol Chem , vol.277 , pp. 16705-16711
    • Fekete, R.A.1    Frost, L.S.2
  • 15
    • 0028335140 scopus 로고
    • Analysis of the sequence and gene products of the transfer region of the F sex factor
    • Frost LS, Ippen-Ihler K, Skurray RA (1994) Analysis of the sequence and gene products of the transfer region of the F sex factor. Microbiol Rev 58: 162-210
    • (1994) Microbiol Rev , vol.58 , pp. 162-210
    • Frost, L.S.1    Ippen-Ihler, K.2    Skurray, R.A.3
  • 16
    • 0026073992 scopus 로고
    • Deletion analysis of the F plasmid oriT locus
    • Fu YH, Tsai MM, Luo YN, Deonier RC (1991) Deletion analysis of the F plasmid oriT locus. J Bacteriol 173: 1012-1020
    • (1991) J Bacteriol , vol.173 , pp. 1012-1020
    • Fu, Y.H.1    Tsai, M.M.2    Luo, Y.N.3    Deonier, R.C.4
  • 18
    • 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
  • 19
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T (1993) A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262: 1401-1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 20
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 21
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • Holton J, Alber T (2004) Automated protein crystal structure determination using ELVES. Proc Natl Acad Sci USA 101: 1537-1542
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 22
    • 0028867005 scopus 로고
    • Stepwise assembly of a relaxosome at the F plasmid origin of transfer
    • Howard MT, Nelson WC, Matson SW (1995) Stepwise assembly of a relaxosome at the F plasmid origin of transfer. J Biol Chem 270: 28381-28386
    • (1995) J Biol Chem , vol.270 , pp. 28381-28386
    • Howard, M.T.1    Nelson, W.C.2    Matson, S.W.3
  • 23
    • 0035156081 scopus 로고    scopus 로고
    • Transfer protein TraY of plasmid R1 stimulates TraI-catalyzed oriT cleavage in vivo
    • Karl W, Bamberger M, Zechner EL (2001) Transfer protein TraY of plasmid R1 stimulates TraI-catalyzed oriT cleavage in vivo. J Bacteriol 183: 909-914
    • (2001) J Bacteriol , vol.183 , pp. 909-914
    • Karl, W.1    Bamberger, M.2    Zechner, E.L.3
  • 25
    • 0029007928 scopus 로고
    • DNA processing reactions in bacterial conjugation
    • Lanka E, Wilkins BM (1995) DNA processing reactions in bacterial conjugation. Annu Rev Biochem 64: 141-169
    • (1995) Annu Rev Biochem , vol.64 , pp. 141-169
    • Lanka, E.1    Wilkins, B.M.2
  • 26
    • 0038280138 scopus 로고    scopus 로고
    • A rapid screen for functional mutants of TraM, an autoregulatory protein required for F conjugation
    • Lu J, Fekete RA, Frost LS (2003) A rapid screen for functional mutants of TraM, an autoregulatory protein required for F conjugation. Mol Genet Genomics 269: 227-233
    • (2003) Mol Genet Genomics , vol.269 , pp. 227-233
    • Lu, J.1    Fekete, R.A.2    Frost, L.S.3
  • 27
    • 21844449126 scopus 로고    scopus 로고
    • Mutations in the C-terminal region of TraM provide evidence for in vivo TraM-TraD interactions during F-plasmid conjugation
    • Lu J, Frost LS (2005) Mutations in the C-terminal region of TraM provide evidence for in vivo TraM-TraD interactions during F-plasmid conjugation. J Bacteriol 187: 4767-4773
    • (2005) J Bacteriol , vol.187 , pp. 4767-4773
    • Lu, J.1    Frost, L.S.2
  • 29
    • 11244306408 scopus 로고    scopus 로고
    • Mutational analysis of TraM correlates oligomerization and DNA binding with autoregulation and conjugative DNA transfer
    • Lu J, Zhao W, Frost LS (2004) Mutational analysis of TraM correlates oligomerization and DNA binding with autoregulation and conjugative DNA transfer. J Biol Chem 279: 55324-55333
    • (2004) J Biol Chem , vol.279 , pp. 55324-55333
    • Lu, J.1    Zhao, W.2    Frost, L.S.3
  • 30
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A (1996) Coiled coils: new structures and new functions. Trends Biochem Sci 21: 375-382
    • (1996) Trends Biochem Sci , vol.21 , pp. 375-382
    • Lupas, A.1
  • 31
    • 0035951778 scopus 로고    scopus 로고
    • F plasmid conjugative DNA transfer: The TraI helicase activity is essential for DNA strand transfer
    • Matson SW, Sampson JK, Byrd DR (2001) F plasmid conjugative DNA transfer: the TraI helicase activity is essential for DNA strand transfer. J Biol Chem 276: 2372-2379
    • (2001) J Biol Chem , vol.276 , pp. 2372-2379
    • Matson, S.W.1    Sampson, J.K.2    Byrd, D.R.3
  • 32
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee DE (1999) XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J Struct Biol 125: 156-165
    • (1999) J Struct Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 33
    • 0037855774 scopus 로고    scopus 로고
    • Evidence for a monomeric intermediate in the reversible unfolding of F factor TraM
    • Miller DL, Schildbach JF (2003) Evidence for a monomeric intermediate in the reversible unfolding of F factor TraM. J Biol Chem 278: 10400-10407
    • (2003) J Biol Chem , vol.278 , pp. 10400-10407
    • Miller, D.L.1    Schildbach, J.F.2
  • 35
    • 0023404786 scopus 로고
    • Analysis of transfer genes and gene products within the traB-traC region of the Escherichia coli fertility factor, F
    • Moore D, Wu JH, Kathir P, Hamilton CM, Ippen-Ihler K (1987) Analysis of transfer genes and gene products within the traB-traC region of the Escherichia coli fertility factor, F. J Bacteriol 169: 3994-4002
    • (1987) J Bacteriol , vol.169 , pp. 3994-4002
    • Moore, D.1    Wu, J.H.2    Kathir, P.3    Hamilton, C.M.4    Ippen-Ihler, K.5
  • 36
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris RJ, Perrakis A, Lamzin VS (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374: 229-244
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 37
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53: 240-255
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 38
    • 0028784315 scopus 로고
    • The traY gene product and integration host factor stimulate Escherichia coli DNA helicase I-catalyzed nicking at the F plasmid oriT
    • Nelson WC, Howard MT, Sherman JA, Matson SW (1995) The traY gene product and integration host factor stimulate Escherichia coli DNA helicase I-catalyzed nicking at the F plasmid oriT. J Biol Chem 270: 28374-28380
    • (1995) J Biol Chem , vol.270 , pp. 28374-28380
    • Nelson, W.C.1    Howard, M.T.2    Sherman, J.A.3    Matson, S.W.4
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski L, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, L.1    Minor, W.2
  • 40
    • 0029916145 scopus 로고    scopus 로고
    • Regulation of the expression of the traM gene of the F sex factor of Escherichia coli
    • Penfold SS, Simon J, Frost LS (1996) Regulation of the expression of the traM gene of the F sex factor of Escherichia coli. Mol Microbiol 20: 549-558
    • (1996) Mol Microbiol , vol.20 , pp. 549-558
    • Penfold, S.S.1    Simon, J.2    Frost, L.S.3
  • 42
    • 0031765579 scopus 로고    scopus 로고
    • The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer
    • Sastre JI, Cabezon E, de la Cruz F (1998) The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer. J Bacteriol 180: 6039-6042
    • (1998) J Bacteriol , vol.180 , pp. 6039-6042
    • Sastre, J.I.1    Cabezon, E.2    De La Cruz, F.3
  • 43
    • 0026088818 scopus 로고
    • The TraM protein of plasmid R1 is a DNA-binding protein
    • Schwab M, Gruber H, Hogenauer G (1991) The TraM protein of plasmid R1 is a DNA-binding protein. Mol Microbiol 5: 439-446
    • (1991) Mol Microbiol , vol.5 , pp. 439-446
    • Schwab, M.1    Gruber, H.2    Hogenauer, G.3
  • 45
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S, Richardson CC (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc Natl Acad Sci USA 82: 1074-1078
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 46
    • 20444431234 scopus 로고    scopus 로고
    • TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase
    • Tato I, Zunzunegui S, de la Cruz F, Cabezon E (2005) TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase. Proc Natl Acad Sci USA 102: 8156-8161
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8156-8161
    • Tato, I.1    Zunzunegui, S.2    De La Cruz, F.3    Cabezon, E.4
  • 47
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger TC (2000) Maximum-likelihood density modification. Acta Crystallogr D 56 (Part 8): 965-972
    • (2000) Acta Crystallogr D , vol.56 , Issue.8 PART , pp. 965-972
    • Terwilliger, T.C.1
  • 48
    • 0036848846 scopus 로고    scopus 로고
    • Automated structure solution, density modification and model building
    • Terwilliger TC (2002) Automated structure solution, density modification and model building. Acta Crystallogr D 58: 1937-1940
    • (2002) Acta Crystallogr D , vol.58 , pp. 1937-1940
    • Terwilliger, T.C.1
  • 49
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger TC, Berendzen J (1999) Automated MAD and MIR structure solution. Acta Crystallogr D 55 (Part 4): 849-861
    • (1999) Acta Crystallogr D , vol.55 , Issue.4 PART , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 50
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Crystallogr 30: 1022-1025
    • (1997) J Appl Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 52
    • 0017287870 scopus 로고
    • Temperature dependence of mating-pair formation in Escherichia coli
    • Walmsley RH (1976) Temperature dependence of mating-pair formation in Escherichia coli. J Bacteriol 126: 222-224
    • (1976) J Bacteriol , vol.126 , pp. 222-224
    • Walmsley, R.H.1
  • 54
    • 7644241959 scopus 로고    scopus 로고
    • The role of H-NS in silencing the F transfer region during entry into stationary phase
    • Will WR, Lu J, Frost LS (2004) The role of H-NS in silencing the F transfer region during entry into stationary phase. Mol Microbiol 54: 769-782
    • (2004) Mol Microbiol , vol.54 , pp. 769-782
    • Will, W.R.1    Lu, J.2    Frost, L.S.3
  • 55
    • 0021319941 scopus 로고
    • Processing of plasmid DNA during bacterial conjugation
    • Willetts N, Wilkins B (1984) Processing of plasmid DNA during bacterial conjugation. Microbiol Rev 48: 24-41
    • (1984) Microbiol Rev , vol.48 , pp. 24-41
    • Willetts, N.1    Wilkins, B.2
  • 56
    • 0014828875 scopus 로고
    • Characteristics of E. coli K12 strains carrying both an F prime and an R factor
    • Willetts NS, Finnegan DJ (1970) Characteristics of E. coli K12 strains carrying both an F prime and an R factor. Genet Res 16: 113-122
    • (1970) Genet Res , vol.16 , pp. 113-122
    • Willetts, N.S.1    Finnegan, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.