메뉴 건너뛰기




Volumn 16, Issue 6, 2006, Pages 744-752

Cut and move: protein machinery for DNA processing in bacterial conjugation

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; DNA; HELICASE; INTEGRATION HOST FACTOR;

EID: 33751512976     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.10.004     Document Type: Review
Times cited : (31)

References (67)
  • 1
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • Ochman H., Lawrence J.G., and Groisman E.A. Lateral gene transfer and the nature of bacterial innovation. Nature 405 (2000) 299-304
    • (2000) Nature , vol.405 , pp. 299-304
    • Ochman, H.1    Lawrence, J.G.2    Groisman, E.A.3
  • 3
    • 28544449319 scopus 로고    scopus 로고
    • The ins and outs of DNA transfer in bacteria
    • Chen I., Christie P.J., and Dubnau D. The ins and outs of DNA transfer in bacteria. Science 310 (2005) 1456-1460
    • (2005) Science , vol.310 , pp. 1456-1460
    • Chen, I.1    Christie, P.J.2    Dubnau, D.3
  • 4
    • 0025934745 scopus 로고
    • Conjugational junctions: morphology of specific contacts in conjugating Escherichia coli bacteria
    • Dürrenberger M.B., Villiger W., and Bachi T. Conjugational junctions: morphology of specific contacts in conjugating Escherichia coli bacteria. J Struct Biol 107 (1991) 146-156
    • (1991) J Struct Biol , vol.107 , pp. 146-156
    • Dürrenberger, M.B.1    Villiger, W.2    Bachi, T.3
  • 5
    • 0034646538 scopus 로고    scopus 로고
    • Infectious history
    • Lederberg J. Infectious history. Science 288 (2000) 287-293
    • (2000) Science , vol.288 , pp. 287-293
    • Lederberg, J.1
  • 6
    • 0029007928 scopus 로고
    • DNA processing reactions in bacterial conjugation
    • Lanka E., and Wilkins B.M. DNA processing reactions in bacterial conjugation. Annu Rev Biochem 64 (1995) 141-169
    • (1995) Annu Rev Biochem , vol.64 , pp. 141-169
    • Lanka, E.1    Wilkins, B.M.2
  • 7
    • 51149212256 scopus 로고
    • Gene recombination in Escherichia coli
    • Tatum E.L., and Lederberg J. Gene recombination in Escherichia coli. Nature 158 (1946) 558-658
    • (1946) Nature , vol.158 , pp. 558-658
    • Tatum, E.L.1    Lederberg, J.2
  • 9
    • 0015402376 scopus 로고
    • Trimethoprim resistance conferred by W plasmids in Enterobacteriaceae
    • Datta N., and Hedges R.W. Trimethoprim resistance conferred by W plasmids in Enterobacteriaceae. J Gen Microbiol 72 (1972) 349-355
    • (1972) J Gen Microbiol , vol.72 , pp. 349-355
    • Datta, N.1    Hedges, R.W.2
  • 11
    • 0345689425 scopus 로고    scopus 로고
    • Assembly of pili on the surface of Corynebacterium diphtheriae
    • Ton-That H., and Schneewind O. Assembly of pili on the surface of Corynebacterium diphtheriae. Mol Microbiol 50 (2003) 1429-1438
    • (2003) Mol Microbiol , vol.50 , pp. 1429-1438
    • Ton-That, H.1    Schneewind, O.2
  • 12
    • 0037905748 scopus 로고    scopus 로고
    • Conjugative plasmid transfer in Gram-positive bacteria
    • Grohmann E., Muth G., and Espinosa M. Conjugative plasmid transfer in Gram-positive bacteria. Microbiol Mol Biol Rev 67 (2003) 277-301
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 277-301
    • Grohmann, E.1    Muth, G.2    Espinosa, M.3
  • 13
    • 8844259469 scopus 로고    scopus 로고
    • Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems
    • Christie P.J. Type IV secretion: the Agrobacterium VirB/D4 and related conjugation systems. Biochim Biophys Acta 1694 (2004) 219-234
    • (2004) Biochim Biophys Acta , vol.1694 , pp. 219-234
    • Christie, P.J.1
  • 14
    • 0031033180 scopus 로고    scopus 로고
    • Towards a structural biology of bacterial conjugation
    • Silverman P.M. Towards a structural biology of bacterial conjugation. Mol Microbiol 23 (1997) 423-429
    • (1997) Mol Microbiol , vol.23 , pp. 423-429
    • Silverman, P.M.1
  • 16
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • A very recent review of T4SS.
    • Backert S., and Meyer T.F. Type IV secretion systems and their effectors in bacterial pathogenesis. Curr Opin Microbiol 9 (2006) 207-217. A very recent review of T4SS.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 17
    • 0024368954 scopus 로고
    • TraJ protein of plasmid RP4 binds to a 19-base pair invert sequence repetition within the transfer origin
    • Ziegelin G., Furste J.P., and Lanka E. TraJ protein of plasmid RP4 binds to a 19-base pair invert sequence repetition within the transfer origin. J Biol Chem 264 (1989) 11989-11994
    • (1989) J Biol Chem , vol.264 , pp. 11989-11994
    • Ziegelin, G.1    Furste, J.P.2    Lanka, E.3
  • 18
    • 0034255091 scopus 로고    scopus 로고
    • Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells
    • Christie P.J., and Vogel J.P. Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells. Trends Microbiol 8 (2000) 354-360
    • (2000) Trends Microbiol , vol.8 , pp. 354-360
    • Christie, P.J.1    Vogel, J.P.2
  • 19
    • 0035035578 scopus 로고    scopus 로고
    • Type IV secretion: intercellular transfer of macromolecules by systems ancestrally related to conjugation machines
    • Christie P.J. Type IV secretion: intercellular transfer of macromolecules by systems ancestrally related to conjugation machines. Mol Microbiol 40 (2001) 294-305
    • (2001) Mol Microbiol , vol.40 , pp. 294-305
    • Christie, P.J.1
  • 21
    • 0242384036 scopus 로고    scopus 로고
    • The outs and ins of bacterial type IV secretion substrates
    • Ding Z., Atmakuri K., and Christie P.J. The outs and ins of bacterial type IV secretion substrates. Trends Microbiol 11 (2003) 527-535
    • (2003) Trends Microbiol , vol.11 , pp. 527-535
    • Ding, Z.1    Atmakuri, K.2    Christie, P.J.3
  • 22
    • 2342445023 scopus 로고    scopus 로고
    • Coupling factors in macromolecular type-IV secretion machineries
    • Gomis-Rüth F.X., Solà M., de la Cruz F., and Coll M. Coupling factors in macromolecular type-IV secretion machineries. Curr Pharm Des 10 (2004) 1551-1565
    • (2004) Curr Pharm Des , vol.10 , pp. 1551-1565
    • Gomis-Rüth, F.X.1    Solà, M.2    de la Cruz, F.3    Coll, M.4
  • 23
    • 0033917122 scopus 로고    scopus 로고
    • Mobilization of chimeric oriT plasmids by F and R100-1: role of relaxosome formation in defining plasmid specificity
    • Fekete R.A., and Frost L.S. Mobilization of chimeric oriT plasmids by F and R100-1: role of relaxosome formation in defining plasmid specificity. J Bacteriol 182 (2000) 4022-4028
    • (2000) J Bacteriol , vol.182 , pp. 4022-4028
    • Fekete, R.A.1    Frost, L.S.2
  • 24
    • 0002412420 scopus 로고
    • DNA processing and replication during plasmid transfer between gram-negative bacteria
    • Clewell D.B. (Ed), Plenum Press
    • Wilkins B., and Lanka E. DNA processing and replication during plasmid transfer between gram-negative bacteria. In: Clewell D.B. (Ed). Bacterial Conjugation (1993), Plenum Press 105-135
    • (1993) Bacterial Conjugation , pp. 105-135
    • Wilkins, B.1    Lanka, E.2
  • 25
    • 0036047412 scopus 로고    scopus 로고
    • Bacterial conjugation: a two-step mechanism for DNA transport
    • Llosa M., Gomis-Rüth F.X., Coll M., and de la Cruz F. Bacterial conjugation: a two-step mechanism for DNA transport. Mol Microbiol 45 (2002) 1-8
    • (2002) Mol Microbiol , vol.45 , pp. 1-8
    • Llosa, M.1    Gomis-Rüth, F.X.2    Coll, M.3    de la Cruz, F.4
  • 26
    • 0017840933 scopus 로고
    • The requirements for conjugal DNA synthesis in the donor strain during flac transfer
    • Kingsman A., and Willetts N. The requirements for conjugal DNA synthesis in the donor strain during flac transfer. J Mol Biol 122 (1978) 287-300
    • (1978) J Mol Biol , vol.122 , pp. 287-300
    • Kingsman, A.1    Willetts, N.2
  • 27
    • 0030766851 scopus 로고    scopus 로고
    • Plasmid rolling circle replication: identification of the RNA polymerase-directed primer RNA and requirement for DNA polymerase I for lagging strand synthesis
    • Kramer M.G., Khan S.A., and Espinosa M. Plasmid rolling circle replication: identification of the RNA polymerase-directed primer RNA and requirement for DNA polymerase I for lagging strand synthesis. EMBO J 16 (1997) 5784-5795
    • (1997) EMBO J , vol.16 , pp. 5784-5795
    • Kramer, M.G.1    Khan, S.A.2    Espinosa, M.3
  • 28
    • 0034072571 scopus 로고    scopus 로고
    • Initiation and termination of DNA transfer during conjugation of IncI1 plasmid R64: roles of two sets of inverted repeat sequences within oriT in termination of R64 transfer
    • Furuya N., and Komano T. Initiation and termination of DNA transfer during conjugation of IncI1 plasmid R64: roles of two sets of inverted repeat sequences within oriT in termination of R64 transfer. J Bacteriol 182 (2000) 3191-3196
    • (2000) J Bacteriol , vol.182 , pp. 3191-3196
    • Furuya, N.1    Komano, T.2
  • 29
    • 0026586047 scopus 로고
    • The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: implications for nuclear uptake of DNA in plant cells
    • Howard E.A., Zupan J.R., Citovsky V., and Zambryski P.C. The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: implications for nuclear uptake of DNA in plant cells. Cell 68 (1992) 109-118
    • (1992) Cell , vol.68 , pp. 109-118
    • Howard, E.A.1    Zupan, J.R.2    Citovsky, V.3    Zambryski, P.C.4
  • 31
    • 28044438533 scopus 로고    scopus 로고
    • Site-specific recombinase and integrase activities of a conjugative relaxase in recipient cells
    • Draper O., Cesar C.E., Machón C., de la Cruz F., and Llosa M. Site-specific recombinase and integrase activities of a conjugative relaxase in recipient cells. Proc Natl Acad Sci USA 102 (2005) 16385-16390
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16385-16390
    • Draper, O.1    Cesar, C.E.2    Machón, C.3    de la Cruz, F.4    Llosa, M.5
  • 32
    • 0242542025 scopus 로고    scopus 로고
    • Structural insights into single-stranded DNA binding and cleavage by F factor Tral
    • The first description of the structure of the relaxase domain of plasmid F protein TraI.
    • Datta S., Larkin C., and Schildbach J.F. Structural insights into single-stranded DNA binding and cleavage by F factor Tral. Structure 11 (2003) 1369-1379. The first description of the structure of the relaxase domain of plasmid F protein TraI.
    • (2003) Structure , vol.11 , pp. 1369-1379
    • Datta, S.1    Larkin, C.2    Schildbach, J.F.3
  • 33
    • 0344628800 scopus 로고    scopus 로고
    • Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC
    • The first description of the structure of the relaxase domain of plasmid R388 protein TrwC bound to DNA. The authors managed to co-crystallise the relaxase with a 25-base DNA oligonucleotide encompassing the recognition sequence upstream of the cleavage site. The DNA folds into a hairpin structure like one of the arms of the extruded cruciform at plasmid origin of transfer.
    • Guasch A., Lucas M., Cabezas M., Pérez-Luque R., Gomis-Rüth F.X., de la Cruz F., and Coll M. Recognition and processing of the origin of transfer DNA by conjugative relaxase TrwC. Nat Struct Biol 10 (2003) 1002-1010. The first description of the structure of the relaxase domain of plasmid R388 protein TrwC bound to DNA. The authors managed to co-crystallise the relaxase with a 25-base DNA oligonucleotide encompassing the recognition sequence upstream of the cleavage site. The DNA folds into a hairpin structure like one of the arms of the extruded cruciform at plasmid origin of transfer.
    • (2003) Nat Struct Biol , vol.10 , pp. 1002-1010
    • Guasch, A.1    Lucas, M.2    Cabezas, M.3    Pérez-Luque, R.4    Gomis-Rüth, F.X.5    de la Cruz, F.6    Coll, M.7
  • 34
    • 26444521223 scopus 로고    scopus 로고
    • Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase
    • Larkin C., Datta S., Harley M.J., Anderson B.J., Ebie A., Hargreaves V., and Schildbach J.F. Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase. Structure 13 (2005) 1533-1544
    • (2005) Structure , vol.13 , pp. 1533-1544
    • Larkin, C.1    Datta, S.2    Harley, M.J.3    Anderson, B.J.4    Ebie, A.5    Hargreaves, V.6    Schildbach, J.F.7
  • 35
    • 33646850212 scopus 로고    scopus 로고
    • Unveiling the molecular mechanism of a conjugative relaxase: the structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site
    • Boer R., Russi S., Guasch A., Lucas M., Blanco A.G., Pérez-Luque R., Coll M., and de la Cruz F. Unveiling the molecular mechanism of a conjugative relaxase: the structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site. J Mol Biol 358 (2006) 857-869
    • (2006) J Mol Biol , vol.358 , pp. 857-869
    • Boer, R.1    Russi, S.2    Guasch, A.3    Lucas, M.4    Blanco, A.G.5    Pérez-Luque, R.6    Coll, M.7    de la Cruz, F.8
  • 36
    • 0036671409 scopus 로고    scopus 로고
    • Structural unity among viral origin binding proteins: crystal structure of the nuclease domain of adeno-associated virus Rep
    • Hickman A.B., Ronning D.R., Kotin R.M., and Dyda F. Structural unity among viral origin binding proteins: crystal structure of the nuclease domain of adeno-associated virus Rep. Mol Cell 10 (2002) 327-337
    • (2002) Mol Cell , vol.10 , pp. 327-337
    • Hickman, A.B.1    Ronning, D.R.2    Kotin, R.M.3    Dyda, F.4
  • 38
    • 0037086545 scopus 로고    scopus 로고
    • Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex
    • Enemark E.J., Stenlund A., and Joshua-Tor L. Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex. EMBO J 21 (2002) 1487-1496
    • (2002) EMBO J , vol.21 , pp. 1487-1496
    • Enemark, E.J.1    Stenlund, A.2    Joshua-Tor, L.3
  • 39
    • 33646193384 scopus 로고    scopus 로고
    • Crystal structure of the simian virus 40 large T-antigen origin-binding domain
    • Meinke G., Bullock P.A., and Bohm A. Crystal structure of the simian virus 40 large T-antigen origin-binding domain. J Virol 80 (2006) 4304-4312
    • (2006) J Virol , vol.80 , pp. 4304-4312
    • Meinke, G.1    Bullock, P.A.2    Bohm, A.3
  • 40
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247 (1995) 536-540
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 41
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis D.L., Brick P., Hamlin R., Xuong N.G., and Steitz T.A. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature 313 (1985) 762-766
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 42
    • 4344610198 scopus 로고    scopus 로고
    • DNA binding properties of protein TrwA, a possible structural variant of the Arc repressor superfamily
    • Moncalián G., and de la Cruz F. DNA binding properties of protein TrwA, a possible structural variant of the Arc repressor superfamily. Biochim Biophys Acta 1701 (2004) 15-23
    • (2004) Biochim Biophys Acta , vol.1701 , pp. 15-23
    • Moncalián, G.1    de la Cruz, F.2
  • 43
    • 0036965763 scopus 로고    scopus 로고
    • TraY DNA recognition of its two F factor binding sites
    • Lum P.L., Rodgers M.E., and Schildbach J.F. TraY DNA recognition of its two F factor binding sites. J Mol Biol 321 (2002) 563-578
    • (2002) J Mol Biol , vol.321 , pp. 563-578
    • Lum, P.L.1    Rodgers, M.E.2    Schildbach, J.F.3
  • 44
    • 0028986676 scopus 로고
    • DNA recognition by a β-sheet
    • Suzuki M. DNA recognition by a β-sheet. Protein Eng 8 (1995) 1-4
    • (1995) Protein Eng , vol.8 , pp. 1-4
    • Suzuki, M.1
  • 46
    • 0036723823 scopus 로고    scopus 로고
    • A genetically economical family of plasmid-encoded transcriptional repressors involved in control of plasmid copy number
    • del Solar G., Hernández-Arriaga A.M., Gomis-Rüth F.X., Coll M., and Espinosa M. A genetically economical family of plasmid-encoded transcriptional repressors involved in control of plasmid copy number. J Bacteriol 184 (2002) 4943-4951
    • (2002) J Bacteriol , vol.184 , pp. 4943-4951
    • del Solar, G.1    Hernández-Arriaga, A.M.2    Gomis-Rüth, F.X.3    Coll, M.4    Espinosa, M.5
  • 47
    • 0030451819 scopus 로고    scopus 로고
    • Crystal structure of an IHF-DNA complex: a protein induced DNA U-turn
    • Rice P.A., Yang S.-W., Mizuuchi K., and Nash H.A. Crystal structure of an IHF-DNA complex: a protein induced DNA U-turn. Cell 87 (1996) 1295-1306
    • (1996) Cell , vol.87 , pp. 1295-1306
    • Rice, P.A.1    Yang, S.-W.2    Mizuuchi, K.3    Nash, H.A.4
  • 48
    • 0028867005 scopus 로고
    • Stepwise assembly of a relaxosome at the F plasmid origin of transfer
    • Howard M.T., Nelson W.C., and Matson S.W. Stepwise assembly of a relaxosome at the F plasmid origin of transfer. J Biol Chem 270 (1995) 28381-28386
    • (1995) J Biol Chem , vol.270 , pp. 28381-28386
    • Howard, M.T.1    Nelson, W.C.2    Matson, S.W.3
  • 49
    • 20444431234 scopus 로고    scopus 로고
    • TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase
    • This report demonstrates the DNA-dependent ATPase activity of TrwB. T4CPs were presumed to be ATPases, but no enzymatic assay had proved it before. TrwB displays positive cooperativity for ATP hydrolysis, with at least three catalytic sites involved, and requires DNA longer than 40 bp to be active.
    • Tato I., Zunzunegui S., de la Cruz F., and Cabezón E. TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNA-dependent ATPase. Proc Natl Acad Sci USA 102 (2005) 8156-8161. This report demonstrates the DNA-dependent ATPase activity of TrwB. T4CPs were presumed to be ATPases, but no enzymatic assay had proved it before. TrwB displays positive cooperativity for ATP hydrolysis, with at least three catalytic sites involved, and requires DNA longer than 40 bp to be active.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8156-8161
    • Tato, I.1    Zunzunegui, S.2    de la Cruz, F.3    Cabezón, E.4
  • 50
    • 0033579554 scopus 로고    scopus 로고
    • Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation
    • Moncalián G., Cabezón E., Alkorta I., Valle M., Moro F., Valpuesta J.M., Goñi F.M., and de la Cruz F. Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation. J Biol Chem 274 (1999) 36117-36124
    • (1999) J Biol Chem , vol.274 , pp. 36117-36124
    • Moncalián, G.1    Cabezón, E.2    Alkorta, I.3    Valle, M.4    Moro, F.5    Valpuesta, J.M.6    Goñi, F.M.7    de la Cruz, F.8
  • 51
    • 0031859043 scopus 로고    scopus 로고
    • Both the fipA gene of pKM101 and the pifC gene of F inhibit conjugal transfer of RP1 by an effect on traG
    • Santini J.M., and Stanisch V.A. Both the fipA gene of pKM101 and the pifC gene of F inhibit conjugal transfer of RP1 by an effect on traG. J Bacteriol 180 (1998) 4093-4101
    • (1998) J Bacteriol , vol.180 , pp. 4093-4101
    • Santini, J.M.1    Stanisch, V.A.2
  • 52
    • 2442483942 scopus 로고    scopus 로고
    • Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation
    • Cabezón E., Sastre J.I., and de la Cruz F. Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation. Mol Gen Genet 254 (1997) 400-406
    • (1997) Mol Gen Genet , vol.254 , pp. 400-406
    • Cabezón, E.1    Sastre, J.I.2    de la Cruz, F.3
  • 53
    • 0000862044 scopus 로고    scopus 로고
    • Structure and function of the F factor and mechanism of conjugation
    • Neidhart F.C., Curtiss III R., Ingraham J.L., Lin E.C.C., Low K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., and Umbarger H.C. (Eds), American Society for Microbiology
    • Firth N., Ippen-Ihler K., and Skurray R.A. Structure and function of the F factor and mechanism of conjugation. In: Neidhart F.C., Curtiss III R., Ingraham J.L., Lin E.C.C., Low K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., and Umbarger H.C. (Eds). Escherichia Coli and Salmonella: Cellular and Molecular Biology. edn 2 (1996), American Society for Microbiology 2377-2401
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology. edn 2 , pp. 2377-2401
    • Firth, N.1    Ippen-Ihler, K.2    Skurray, R.A.3
  • 54
    • 0036217298 scopus 로고    scopus 로고
    • Structure and role of coupling proteins in conjugal DNA transfer
    • Gomis-Rüth F.X., de la Cruz F., and Coll M. Structure and role of coupling proteins in conjugal DNA transfer. Res Microbiol 153 (2002) 199-204
    • (2002) Res Microbiol , vol.153 , pp. 199-204
    • Gomis-Rüth, F.X.1    de la Cruz, F.2    Coll, M.3
  • 56
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G.W., Lutter R., and Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 57
    • 33746987484 scopus 로고    scopus 로고
    • Double-stranded DNA translocation: structure and mechanism of hexameric FtsK
    • This first description of the bacterial FtsK DNA translocase structure shows it to be closely related to T4CPs. In addition, EM experiments prove that dsDNA threads through the central channel of the hexameric ring.
    • Massey T.H., Mercogliano C.P., Yates J., Sherratt D.J., and Löwe J. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol Cell 23 (2006) 457-469. This first description of the bacterial FtsK DNA translocase structure shows it to be closely related to T4CPs. In addition, EM experiments prove that dsDNA threads through the central channel of the hexameric ring.
    • (2006) Mol Cell , vol.23 , pp. 457-469
    • Massey, T.H.1    Mercogliano, C.P.2    Yates, J.3    Sherratt, D.J.4    Löwe, J.5
  • 58
    • 0036510408 scopus 로고    scopus 로고
    • Conjugative plasmid protein TrwB, an integral membrane type IV secretion system coupling protein: detailed structural features and mapping of the active-site cleft
    • Gomis-Rüth F.X., Moncalián G., de la Cruz F., and Coll M. Conjugative plasmid protein TrwB, an integral membrane type IV secretion system coupling protein: detailed structural features and mapping of the active-site cleft. J Biol Chem 277 (2002) 7556-7566
    • (2002) J Biol Chem , vol.277 , pp. 7556-7566
    • Gomis-Rüth, F.X.1    Moncalián, G.2    de la Cruz, F.3    Coll, M.4
  • 59
    • 0028047404 scopus 로고
    • Genetic organization of the conjugal DNA processing region of the IncW plasmid R388
    • Llosa M., Bolland S., and de la Cruz F. Genetic organization of the conjugal DNA processing region of the IncW plasmid R388. J Mol Biol 235 (1994) 448-464
    • (1994) J Mol Biol , vol.235 , pp. 448-464
    • Llosa, M.1    Bolland, S.2    de la Cruz, F.3
  • 60
    • 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., and Koraimann G. 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 (2004) 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
  • 61
    • 0039702020 scopus 로고    scopus 로고
    • The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro
    • Disque-Kochem C., and Dreiseikelmann B. The cytoplasmic DNA-binding protein TraM binds to the inner membrane protein TraD in vitro. J Bacteriol 179 (1997) 6133-6137
    • (1997) J Bacteriol , vol.179 , pp. 6133-6137
    • Disque-Kochem, C.1    Dreiseikelmann, B.2
  • 62
    • 0032498267 scopus 로고    scopus 로고
    • Transfer protein TraM stimulates TraI-catalyzed cleavage of the transfer origin of plasmid R1 in vivo
    • Kupelwieser G., Schwab M., Hogenauer G., Koraimann G., and Zechner E.L. Transfer protein TraM stimulates TraI-catalyzed cleavage of the transfer origin of plasmid R1 in vivo. J Mol Biol 275 (1998) 81-94
    • (1998) J Mol Biol , vol.275 , pp. 81-94
    • Kupelwieser, G.1    Schwab, M.2    Hogenauer, G.3    Koraimann, G.4    Zechner, E.L.5
  • 64
    • 33745518716 scopus 로고    scopus 로고
    • Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM
    • The first structure of the C-terminal domain of the conjugative ancillary protein TraM is presented. Four protonated glutamic acid residues stabilise the helical bundle tetrameric quaternary structure, leading the authors to propose that deprotonation of TraM is a mechanism for the downregulation of conjugation.
    • Lu J., Edwards R.A., Wong J.J., Manchak J., Scott P.G., Frost L.S., and Glover J.N. Protonation-mediated structural flexibility in the F conjugation regulatory protein, TraM. EMBO J 25 (2006) 2930-2939. The first structure of the C-terminal domain of the conjugative ancillary protein TraM is presented. Four protonated glutamic acid residues stabilise the helical bundle tetrameric quaternary structure, leading the authors to propose that deprotonation of TraM is a mechanism for the downregulation of conjugation.
    • (2006) EMBO J , vol.25 , pp. 2930-2939
    • Lu, J.1    Edwards, R.A.2    Wong, J.J.3    Manchak, J.4    Scott, P.G.5    Frost, L.S.6    Glover, J.N.7
  • 65
    • 1842861589 scopus 로고    scopus 로고
    • Structural biology of bacterial pathogenesis
    • A comprehensive structural review of T4SS.
    • Remaut H., and Waksman G. Structural biology of bacterial pathogenesis. Curr Opin Struct Biol 14 (2004) 161-170. A comprehensive structural review of T4SS.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 161-170
    • Remaut, H.1    Waksman, G.2
  • 67
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • The first structure of a ring helicase, showing a ssDNA segment in the central channel. The ssDNA adopts a helical conformation with most of the bases stacked.
    • Enemark E.J., and Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 442 (2006) 270-2755. The first structure of a ring helicase, showing a ssDNA segment in the central channel. The ssDNA adopts a helical conformation with most of the bases stacked.
    • (2006) Nature , vol.442 , pp. 270-2755
    • Enemark, E.J.1    Joshua-Tor, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.