메뉴 건너뛰기




Volumn 289, Issue 39, 2014, Pages 27046-27054

The T4 phage DNA mimic protein arn inhibits the DNA binding activity of the bacterial histone-like protein H-NS

Author keywords

[No Author keywords available]

Indexed keywords

DNA;

EID: 84907457043     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.590851     Document Type: Article
Times cited : (31)

References (47)
  • 2
    • 27844526220 scopus 로고    scopus 로고
    • Protein mimicry of DNA and pathway regulation
    • Putnam, C. D., and Tainer, J. A. (2005) Protein mimicry of DNA and pathway regulation. DNA Repair 4, 1410-1420
    • (2005) DNA Repair , vol.4 , pp. 1410-1420
    • Putnam, C.D.1    Tainer, J.A.2
  • 3
    • 84900559770 scopus 로고    scopus 로고
    • DNA mimic proteins: Functions, structures, and bioinformatic analysis
    • Wang, H. C., Ho, C. H., Hsu, K. C., Yang, J. M., and Wang, A. H. (2014) DNA mimic proteins: functions, structures, and bioinformatic analysis. Biochemistry 53, 2865-2874
    • (2014) Biochemistry , vol.53 , pp. 2865-2874
    • Wang, H.C.1    Ho, C.H.2    Hsu, K.C.3    Yang, J.M.4    Wang, A.H.5
  • 4
    • 84893236435 scopus 로고    scopus 로고
    • Staphylococcus aureus protein SAUGI acts as a uracil-DNA glycosylase inhibitor
    • Wang, H. C., Hsu, K. C., Yang, J. M., Wu, M. L., Ko, T. P., Lin, S. R., and Wang, A. H. (2014) Staphylococcus aureus protein SAUGI acts as a uracil-DNA glycosylase inhibitor. Nucleic Acids Res. 42, 1354-1364
    • (2014) Nucleic Acids Res. , vol.42 , pp. 1354-1364
    • Wang, H.C.1    Hsu, K.C.2    Yang, J.M.3    Wu, M.L.4    Ko, T.P.5    Lin, S.R.6    Wang, A.H.7
  • 5
    • 84877304449 scopus 로고    scopus 로고
    • Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein
    • Wang, H. C., Wu, M. L., Ko, T. P., and Wang, A. H. (2013) Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein. Nucleic Acids Res. 41, 5127-5138
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5127-5138
    • Wang, H.C.1    Wu, M.L.2    Ko, T.P.3    Wang, A.H.4
  • 6
    • 84863222948 scopus 로고    scopus 로고
    • Neisseria conserved protein DMP19 is a DNA mimic protein that prevents DNA binding to a hypothetical nitrogen-response transcription factor
    • Wang, H. C., Ko, T. P., Wu, M. L., Ku, S. C., Wu, H. J., and Wang, A. H. (2012) Neisseria conserved protein DMP19 is a DNA mimic protein that prevents DNA binding to a hypothetical nitrogen-response transcription factor. Nucleic Acids Res. 40, 5718-5730
    • (2012) Nucleic Acids Res. , vol.40 , pp. 5718-5730
    • Wang, H.C.1    Ko, T.P.2    Wu, M.L.3    Ku, S.C.4    Wu, H.J.5    Wang, A.H.6
  • 8
    • 0020061789 scopus 로고
    • Physical mapping and cloning of bacteriophage T4 anti-restriction endonuclease gene
    • Dharmalingam, K., Revel, H. R., and Goldberg, E. B. (1982) Physical mapping and cloning of bacteriophage T4 anti-restriction endonuclease gene. J. Bacteriol. 149, 694-699
    • (1982) J. Bacteriol. , vol.149 , pp. 694-699
    • Dharmalingam, K.1    Revel, H.R.2    Goldberg, E.B.3
  • 9
    • 0031592828 scopus 로고    scopus 로고
    • Nucleotide sequence and revised map location of the arn gene from bacteriophage T4
    • Kim, B. C., Kim, K., Park, E. H., and Lim, C. J. (1997) Nucleotide sequence and revised map location of the arn gene from bacteriophage T4. Mol. Cells 7, 694-696
    • (1997) Mol. Cells , vol.7 , pp. 694-696
    • Kim, B.C.1    Kim, K.2    Park, E.H.3    Lim, C.J.4
  • 10
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and 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, Z.1    Minor, W.2
  • 11
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G. M. (2008) A short history of SHELX. Acta Crystallogr. A 64, 112-122
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 12
    • 0002473587 scopus 로고    scopus 로고
    • Phase combination and cross validation in iterated density-modification calculations
    • Cowtan, K. D., and Main, P. (1996) Phase combination and cross validation in iterated density-modification calculations. Acta Crystallogr. D Biol. Crystallogr. 52, 43-48
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 43-48
    • Cowtan, K.D.1    Main, P.2
  • 13
    • 33748337934 scopus 로고    scopus 로고
    • The buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 16
  • 19
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 20
    • 0026666265 scopus 로고
    • Electron microscopic visualization of DNA and DNA-protein complexes as adjunct to biochemical studies
    • Thresher, R., and Griffith, J. (1992) Electron microscopic visualization of DNA and DNA-protein complexes as adjunct to biochemical studies. Methods Enzymol. 211, 481-490
    • (1992) Methods Enzymol. , vol.211 , pp. 481-490
    • Thresher, R.1    Griffith, J.2
  • 23
    • 33746008173 scopus 로고    scopus 로고
    • Selective silencing of foreign DNA with low GC content by the H-NS protein in salmonella
    • Navarre, W. W., Porwollik, S., Wang, Y., McClelland, M., Rosen, H., Libby, S. J., and Fang, F.C. (2006) Selective silencing of foreign DNA with low GC content by the H-NS protein in Salmonella. Science 313, 236-238
    • (2006) Science , vol.313 , pp. 236-238
    • Navarre, W.W.1    Porwollik, S.2    Wang, Y.3    McClelland, M.4    Rosen, H.5    Libby, S.J.6    Fang, F.C.7
  • 24
    • 34250724903 scopus 로고    scopus 로고
    • Silencing of xenogeneic DNA by H-NS-facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA
    • Navarre, W.W., McClelland, M., Libby, S. J., and Fang, F. C. (2007) Silencing of xenogeneic DNA by H-NS-facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA. Genes Dev. 21, 1456-1471
    • (2007) Genes Dev. , vol.21 , pp. 1456-1471
    • Navarre, W.W.1    McClelland, M.2    Libby, S.J.3    Fang, F.C.4
  • 25
    • 34247628510 scopus 로고    scopus 로고
    • H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing
    • Bouffartigues, E., Buckle, M., Badaut, C., Travers, A., and Rimsky, S. (2007) H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing. Nat. Struct. Mol. Biol. 14, 441-448
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 441-448
    • Bouffartigues, E.1    Buckle, M.2    Badaut, C.3    Travers, A.4    Rimsky, S.5
  • 27
    • 0033760257 scopus 로고    scopus 로고
    • T4 early promoter strength probed in vivo with unribosylated and ADP-ribosylated escherichia coli RNA polymerase: A mutation analysis
    • Sommer, N., Salniene, V., Gineikiene, E., Nivinskas, R., and Rüger, W. (2000) T4 early promoter strength probed in vivo with unribosylated and ADP-ribosylated Escherichia coli RNA polymerase: a mutation analysis. Microbiology 146, 2643-2653
    • (2000) Microbiology , vol.146 , pp. 2643-2653
    • Sommer, N.1    Salniene, V.2    Gineikiene, E.3    Nivinskas, R.4    Rüger, W.5
  • 28
    • 3242877815 scopus 로고    scopus 로고
    • Clus-pro: A fully automated algorithm for protein-protein docking
    • Comeau, S. R., Gatchell, D. W., Vajda, S., and Camacho, C. J. (2004) Clus-Pro: a fully automated algorithm for protein-protein docking. Nucleic Acids Res. 32, W96-W99
    • (2004) Nucleic Acids Res. , vol.32 , pp. W96-W99
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 29
    • 0345832301 scopus 로고    scopus 로고
    • Clus-pro: An automated docking and discrimination method for the prediction of protein complexes
    • Comeau, S. R., Gatchell, D. W., Vajda, S., and Camacho, C. J. (2004) Clus-Pro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20, 45-50
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 30
    • 33749020839 scopus 로고    scopus 로고
    • PIPER: An FFT-based protein docking program with pairwise potentials
    • Kozakov, D., Brenke, R., Comeau, S. R., and Vajda, S. (2006) PIPER: an FFT-based protein docking program with pairwise potentials. Proteins 65, 392-406
    • (2006) Proteins , vol.65 , pp. 392-406
    • Kozakov, D.1    Brenke, R.2    Comeau, S.R.3    Vajda, S.4
  • 31
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: Cluspro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov, D., Hall, D. R., Beglov, D., Brenke, R., Comeau, S. R., Shen, Y., Li, K., Zheng, J., Vakili, P., Paschalidis, I. Ch., and Vajda, S. (2010) Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78, 3124-3130
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5    Shen, Y.6    Li, K.7    Zheng, J.8    Vakili, P.9    Paschalidis I.Ch.10    Vajda, S.11
  • 32
    • 0034666271 scopus 로고    scopus 로고
    • H-NS mediated compaction of DNA visualised by atomic force microscopy
    • Dame, R. T., Wyman, C., and Goosen, N. (2000) H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res. 28, 3504-3510
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3504-3510
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 33
    • 0033605817 scopus 로고    scopus 로고
    • Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with escherichia coli uracil-DNA glycosylase
    • Putnam, C. D., Shroyer, M. J., Lundquist, A. J., Mol, C. D., Arvai, A. S., Mosbaugh, D. W., and Tainer, J. A. (1999) Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase. J. Mol. Biol. 287, 331-346
    • (1999) J. Mol. Biol. , vol.287 , pp. 331-346
    • Putnam, C.D.1    Shroyer, M.J.2    Lundquist, A.J.3    Mol, C.D.4    Arvai, A.S.5    Mosbaugh, D.W.6    Tainer, J.A.7
  • 36
    • 84867319588 scopus 로고    scopus 로고
    • The recognition domain of the methyl-specific endonuclease McrBC flips out 5-methylcytosine
    • Sukackaite, R., Grazulis, S., Tamulaitis, G., and Siksnys, V. (2012) The recognition domain of the methyl-specific endonuclease McrBC flips out 5-methylcytosine. Nucleic Acids Res. 40, 7552-7562
    • (2012) Nucleic Acids Res. , vol.40 , pp. 7552-7562
    • Sukackaite, R.1    Grazulis, S.2    Tamulaitis, G.3    Siksnys, V.4
  • 37
    • 0024004997 scopus 로고
    • Proteins from the prokaryotic nucleoid: Primary and quaternary structure of the 15-kDa escherichia coli DNA binding protein H-NS
    • Falconi, M., Gualtieri, M. T., La Teana, A., Losso, M. A., and Pon, C. L. (1988) Proteins from the prokaryotic nucleoid: primary and quaternary structure of the 15-kDa Escherichia coli DNA binding protein H-NS. Mol. Microbiol. 2, 323-329
    • (1988) Mol. Microbiol. , vol.2 , pp. 323-329
    • Falconi, M.1    Gualtieri, M.T.2    La Teana, A.3    Losso, M.A.4    Pon, C.L.5
  • 38
    • 78649640318 scopus 로고    scopus 로고
    • Effects of nucleoid-associated proteins on bacterial chromosome structure and gene expression
    • Browning, D.F., Grainger, D.C., and Busby, S. J.(2010) Effects of nucleoid-associated proteins on bacterial chromosome structure and gene expression. Curr. Opin. Microbiol. 13, 773-780
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 773-780
    • Browning, D.F.1    Grainger, D.C.2    Busby, S.J.3
  • 40
    • 0035083490 scopus 로고    scopus 로고
    • Structural basis for preferential binding of H-NS to curved DNA
    • Dame, R. T., Wyman, C., and Goosen, N. (2001) Structural basis for preferential binding of H-NS to curved DNA. Biochimie 83, 231-234
    • (2001) Biochimie , vol.83 , pp. 231-234
    • Dame, R.T.1    Wyman, C.2    Goosen, N.3
  • 42
    • 27444441689 scopus 로고    scopus 로고
    • H-NS is a part of a thermally controlled mechanism for bacterial gene regulation
    • Ono, S., Goldberg, M. D., Olsson, T., Esposito, D., Hinton, J. C., and Ladbury, J. E. (2005) H-NS is a part of a thermally controlled mechanism for bacterial gene regulation. Biochem. J. 391, 203-213
    • (2005) Biochem. J. , vol.391 , pp. 203-213
    • Ono, S.1    Goldberg, M.D.2    Olsson, T.3    Esposito, D.4    Hinton, J.C.5    Ladbury, J.E.6
  • 43
    • 17644393469 scopus 로고    scopus 로고
    • SspA is required for acid resistance in stationary phase by down-regulation of H-NS in escherichia coli
    • Hansen, A. M., Qiu, Y., Yeh, N., Blattner, F. R., Durfee, T., and Jin, D. J. (2005) SspA is required for acid resistance in stationary phase by down-regulation of H-NS in Escherichia coli. Mol. Microbiol. 56, 719-734
    • (2005) Mol. Microbiol. , vol.56 , pp. 719-734
    • Hansen, A.M.1    Qiu, Y.2    Yeh, N.3    Blattner, F.R.4    Durfee, T.5    Jin, D.J.6
  • 44
    • 33745753388 scopus 로고    scopus 로고
    • Concert of regulators to switch on LEE expression in enterohemorrhagic escherichia coli O157:H7: Interplay between ler, GrlA, HNS, and RpoS
    • Laaberki, M. H., Janabi, N., Oswald, E., and Repoila, F. (2006) Concert of regulators to switch on LEE expression in enterohemorrhagic Escherichia coli O157:H7: interplay between Ler, GrlA, HNS, and RpoS. Int. J. Med. Microbiol. 296, 197-210
    • (2006) Int. J. Med. Microbiol. , vol.296 , pp. 197-210
    • Laaberki, M.H.1    Janabi, N.2    Oswald, E.3    Repoila, F.4
  • 45
    • 28844491363 scopus 로고    scopus 로고
    • Environmental control of the in vivo oligomerization of nucleoid protein H-NS
    • Stella, S., Falconi, M., Lammi, M., Gualerzi, C. O., and Pon, C. L. (2006) Environmental control of the in vivo oligomerization of nucleoid protein H-NS. J. Mol. Biol. 355, 169-174
    • (2006) J. Mol. Biol. , vol.355 , pp. 169-174
    • Stella, S.1    Falconi, M.2    Lammi, M.3    Gualerzi, C.O.4    Pon, C.L.5
  • 46
    • 80052549313 scopus 로고    scopus 로고
    • The 5.5 protein of phage T7 inhibits H-NS through interactions with the Central oligomerization domain
    • Ali, S. S., Beckett, E., Bae, S. J., and Navarre, W. W. (2011) The 5.5 protein of phage T7 inhibits H-NS through interactions with the central oligomerization domain. J. Bacteriol. 193, 4881-4892
    • (2011) J. Bacteriol. , vol.193 , pp. 4881-4892
    • Ali, S.S.1    Beckett, E.2    Bae, S.J.3    Navarre, W.W.4
  • 47
    • 36549031282 scopus 로고    scopus 로고
    • Genome analysis of phage JS98 defines a fourth major subgroup of T4-like phages in escherichia coli
    • Zuber, S., Ngom-Bru, C., Barretto, C., Bruttin, A., Brüssow, H., and Denou, E. (2007) Genome analysis of phage JS98 defines a fourth major subgroup of T4-like phages in Escherichia coli. J. Bacteriol. 189, 8206-8214
    • (2007) J. Bacteriol. , vol.189 , pp. 8206-8214
    • Zuber, S.1    Ngom-Bru, C.2    Barretto, C.3    Bruttin, A.4    Brüssow, H.5    Denou, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.