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Volumn 289, Issue 12, 2014, Pages 8420-8431

CvfA protein and polynucleotide phosphorylase act in an opposing manner to regulate Staphylococcus aureus virulence

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BLOOD; ENCODING (SYMBOLS); GENE EXPRESSION; GENE EXPRESSION REGULATION; NUCLEOTIDES; PHOSPHORYLATION; PROTEINS;

EID: 84896982104     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.554329     Document Type: Article
Times cited : (20)

References (60)
  • 1
    • 84865165883 scopus 로고    scopus 로고
    • RNA degradation in Bacillus subtilis: An interplay of essential endo- and exoribonucleases
    • Lehnik-Habrink, M., Lewis, R. J., Mader, U., and Stulke, J. (2012) RNA degradation in Bacillus subtilis: an interplay of essential endo- and exoribonucleases. Mol. Microbiol. 84, 1005-1017
    • (2012) Mol. Microbiol. , vol.84 , pp. 1005-1017
    • Lehnik-Habrink, M.1    Lewis, R.J.2    Mader, U.3    Stulke, J.4
  • 2
    • 70450222923 scopus 로고    scopus 로고
    • RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis
    • Shahbabian, K., Jamalli, A., Zig, L., and Putzer, H. (2009) RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis. EMBO J. 28, 3523-3533
    • (2009) EMBO J , vol.28 , pp. 3523-3533
    • Shahbabian, K.1    Jamalli, A.2    Zig, L.3    Putzer, H.4
  • 4
    • 33749645818 scopus 로고    scopus 로고
    • Functional analysis of 11 putative essential genes in Bacillus subtilis
    • DOI 10.1099/mic.0.29152-0
    • Hunt, A., Rawlins, J. P., Thomaides, H. B., and Errington, J. (2006) Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152, 2895-2907 (Pubitemid 44542371)
    • (2006) Microbiology , vol.152 , Issue.10 , pp. 2895-2907
    • Hunt, A.1    Rawlins, J.P.2    Thomaides, H.B.3    Errington, J.4
  • 6
    • 77954358026 scopus 로고    scopus 로고
    • Initiation of decay of Bacillus subtilis rpsO mRNA by endoribonuclease RNase Y
    • Yao, S., and Bechhofer, D. H. (2010) Initiation of decay of Bacillus subtilis rpsO mRNA by endoribonuclease RNase Y. J. Bacteriol. 192, 3279-3286
    • (2010) J. Bacteriol. , vol.192 , pp. 3279-3286
    • Yao, S.1    Bechhofer, D.H.2
  • 7
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y., and Deutscher, M. P. (2001) Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 29, 1017-1026 (Pubitemid 32186186)
    • (2001) Nucleic Acids Research , vol.29 , Issue.5 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 8
    • 77954952126 scopus 로고    scopus 로고
    • Messenger RNA turnover processes in Escherichia coli, Bacillus subtilis, and emerging studies in Staphylococcus aureus
    • Anderson, K. L., and Dunman, P. M. (2009) Messenger RNA turnover processes in Escherichia coli, Bacillus subtilis, and emerging studies in Staphylococcus aureus. Int. J. Microbiol. 2009, 525491
    • (2009) Int. J. Microbiol. , vol.2009 , pp. 525491
    • Anderson, K.L.1    Dunman, P.M.2
  • 9
    • 0030047027 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis
    • Luttinger, A., Hahn, J., and Dubnau, D. (1996) Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis. Mol. Microbiol. 19, 343-356 (Pubitemid 26036114)
    • (1996) Molecular Microbiology , vol.19 , Issue.2 , pp. 343-356
    • Luttinger, A.1    Hahn, J.2    Dubnau, D.3
  • 10
    • 0029787968 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase of Escherichia coli is required for the establishment of bacteriophage P4 immunity
    • Piazza, F., Zappone, M., Sana, M., Briani, F., and Dehò, G. (1996) Polynucleotide phosphorylase of Escherichia coli is required for the establishment of bacteriophage P4 immunity. J. Bacteriol. 178, 5513-5521 (Pubitemid 26304388)
    • (1996) Journal of Bacteriology , vol.178 , Issue.18 , pp. 5513-5521
    • Piazza, F.1    Zappone, M.2    Sana, M.3    Briani, F.4    Deho, G.5
  • 11
    • 0033923957 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional control of polynucleotide phosphorylase during cold acclimation in Escherichia coli
    • DOI 10.1046/j.1365-2958.2000.01971.x
    • Zangrossi, S., Briani, F., Ghisotti, D., Regonesi, M. E., Tortora, P., and Dehò, G. (2000) Transcriptional and post-transcriptional control of polynucleotide phosphorylase during cold acclimation in Escherichia coli. Mol. Microbiol. 36, 1470-1480 (Pubitemid 30449981)
    • (2000) Molecular Microbiology , vol.36 , Issue.6 , pp. 1470-1480
    • Zangrossi, S.1    Briani, F.2    Ghisotti, D.3    Regonesi, M.E.4    Tortora, P.5    Deho, G.6
  • 12
    • 0030002447 scopus 로고    scopus 로고
    • Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain
    • Wang, W., and Bechhofer, D. H. (1996) Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain. J. Bacteriol. 178, 2375-2382 (Pubitemid 26123503)
    • (1996) Journal of Bacteriology , vol.178 , Issue.8 , pp. 2375-2382
    • Wang, W.1    Bechhofer, D.H.2
  • 14
    • 12844250037 scopus 로고    scopus 로고
    • Modulation of Yersinia type three secretion system by the S1 domain of polynucleotide phosphorylase
    • DOI 10.1074/jbc.M405662200
    • Rosenzweig, J. A., Weltman, G., Plano, G. V., and Schesser, K. (2005) Modulation of Yersinia type three secretion system by the S1 domain of polynucleotide phosphorylase. J. Biol. Chem. 280, 156-163 (Pubitemid 40164976)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 156-163
    • Rosenzweig, J.A.1    Weltman, G.2    Plano, G.V.3    Schesser, K.4
  • 15
    • 34247128328 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase independently controls virulence factor expression levels and export in Yersinia spp.
    • DOI 10.1111/j.1574-6968.2007.00689.x
    • Rosenzweig, J. A., Chromy, B., Echeverry, A., Yang, J., Adkins, B., Plano, G. V., McCutchen-Maloney, S., and Schesser, K. (2007) Polynucleotide phosphorylase independently controls virulence factor expression levels and export in Yersinia spp. FEMS Microbiol. Lett. 270, 255-264 (Pubitemid 46597373)
    • (2007) FEMS Microbiology Letters , vol.270 , Issue.2 , pp. 255-264
    • Rosenzweig, J.A.1    Chromy, B.2    Echeverry, A.3    Yang, J.4    Adkins, B.5    Plano, G.V.6    McCutchen-Maloney, S.7    Schesser, K.8
  • 16
    • 0036302006 scopus 로고    scopus 로고
    • Silkworm larvae as an animal model of bacterial infection pathogenic to humans
    • DOI 10.1006/mpat.2002.0494
    • Kaito, C., Akimitsu, N., Watanabe, H., and Sekimizu, K. (2002) Silkworm larvae as an animal model of bacterial infection pathogenic to humans. Microb. Pathog. 32, 183-190 (Pubitemid 34743891)
    • (2002) Microbial Pathogenesis , vol.32 , Issue.4 , pp. 183-190
    • Kaito, C.1    Akimitsu, N.2    Watanabe, H.3    Sekimizu, K.4
  • 17
    • 18444385070 scopus 로고    scopus 로고
    • Silkworm pathogenic bacteria infection model for identification of novel virulence genes
    • DOI 10.1111/j.1365-2958.2005.04596.x
    • Kaito, C., Kurokawa, K., Matsumoto, Y., Terao, Y., Kawabata, S., Hamada, S., and Sekimizu, K. (2005) Silkworm pathogenic bacteria infection model for identification of novel virulence genes. Mol. Microbiol. 56, 934-944 (Pubitemid 40646766)
    • (2005) Molecular Microbiology , vol.56 , Issue.4 , pp. 934-944
    • Kaito, C.1    Kurokawa, K.2    Matsumoto, Y.3    Terao, Y.4    Kawabata, S.5    Hamada, S.6    Sekimizu, K.7
  • 18
    • 80053608322 scopus 로고    scopus 로고
    • Characterization of components of the Staphylococcus aureus mRNA degradosome holoenzyme-like complex
    • Roux, C. M., DeMuth, J. P., and Dunman, P. M. (2011) Characterization of components of the Staphylococcus aureus mRNA degradosome holoenzyme-like complex. J. Bacteriol. 193, 5520-5526
    • (2011) J. Bacteriol. , vol.193 , pp. 5520-5526
    • Roux, C.M.1    DeMuth, J.P.2    Dunman, P.M.3
  • 19
    • 84860769484 scopus 로고    scopus 로고
    • Current knowledge on regulatory RNAs and their machineries in Staphylococcus aureus
    • Romilly, C., Caldelari, I., Parmentier, D., Lioliou, E., Romby, P., and Fechter, P. (2012) Current knowledge on regulatory RNAs and their machineries in Staphylococcus aureus. RNA Biol. 9, 402-413
    • (2012) RNA Biol , vol.9 , pp. 402-413
    • Romilly, C.1    Caldelari, I.2    Parmentier, D.3    Lioliou, E.4    Romby, P.5    Fechter, P.6
  • 20
    • 77952721475 scopus 로고    scopus 로고
    • Virulence gene regulation by CvfA, a putative RNase: The CvfA-enolase complex in Streptococcus pyogenes links nutritional stress, growth-phase control, and virulence gene expression
    • Kang, S. O., Caparon, M. G., and Cho, K. H. (2010) Virulence gene regulation by CvfA, a putative RNase: the CvfA-enolase complex in Streptococcus pyogenes links nutritional stress, growth-phase control, and virulence gene expression. Infect. Immun. 78, 2754-2767
    • (2010) Infect. Immun. , vol.78 , pp. 2754-2767
    • Kang, S.O.1    Caparon, M.G.2    Cho, K.H.3
  • 22
    • 38349167848 scopus 로고    scopus 로고
    • Phosphodiesterase activity of CvfA is required for virulence in Staphylococcus aureus
    • Nagata, M., Kaito, C., and Sekimizu, K. (2008) Phosphodiesterase activity of CvfA is required for virulence in Staphylococcus aureus. J. Biol. Chem. 283, 2176-2184
    • (2008) J. Biol. Chem. , vol.283 , pp. 2176-2184
    • Nagata, M.1    Kaito, C.2    Sekimizu, K.3
  • 24
    • 0026891517 scopus 로고
    • Improved method for electroporation of Staphylococcus aureus
    • Schenk, S., and Laddaga, R. A. (1992) Improved method for electroporation of Staphylococcus aureus. FEMS Microbiol. Lett. 73, 133-138
    • (1992) FEMS Microbiol. Lett. , vol.73 , pp. 133-138
    • Schenk, S.1    Laddaga, R.A.2
  • 25
    • 0030608942 scopus 로고    scopus 로고
    • Site-directed mutagene sis: A two-step method using PCR and DpnI
    • Li, S., and Wilkinson, M. F. (1997) Site-directed mutagenesis: a two-step method using PCR and DpnI. BioTechniques 23, 588-590 (Pubitemid 27450903)
    • (1997) BioTechniques , vol.23 , Issue.4 , pp. 588-590
    • Li, S.1    Wilkinson, M.F.2
  • 26
    • 83855162732 scopus 로고    scopus 로고
    • Evaluation of Staphylococcus aureus virulence factors using a silkworm model
    • Miyazaki, S., Matsumoto, Y., Sekimizu, K., and Kaito, C. (2012) Evaluation of Staphylococcus aureus virulence factors using a silkworm model. FEMS Microbiol. Lett. 326, 116-124
    • (2012) FEMS Microbiol. Lett. , vol.326 , pp. 116-124
    • Miyazaki, S.1    Matsumoto, Y.2    Sekimizu, K.3    Kaito, C.4
  • 28
    • 0030850117 scopus 로고    scopus 로고
    • The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level
    • DOI 10.1007/s002030050469
    • Giraudo, A. T., Cheung, A. L., and Nagel, R. (1997) The sae locus of Staphylococcus aureus controls exoprotein synthesis at the transcriptional level. Arch. Microbiol. 168, 53-58 (Pubitemid 27306037)
    • (1997) Archives of Microbiology , vol.168 , Issue.1 , pp. 53-58
    • Giraudo, A.T.1    Cheung, A.L.2    Nagel, R.3
  • 29
    • 84867444709 scopus 로고    scopus 로고
    • The auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus
    • Jeong, D. W., Cho, H., Jones, M. B., Shatzkes, K., Sun, F., Ji, Q., Liu, Q., Peterson, S. N., He, C., and Bae, T. (2012) The auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus. Mol. Microbiol. 86, 331-348
    • (2012) Mol. Microbiol. , vol.86 , pp. 331-348
    • Jeong, D.W.1    Cho, H.2    Jones, M.B.3    Shatzkes, K.4    Sun, F.5    Ji, Q.6    Liu, Q.7    Peterson, S.N.8    He, C.9    Bae, T.10
  • 30
    • 0036382938 scopus 로고    scopus 로고
    • Mutational analysis of polynucleotide phosphorylase from Escherichia coli
    • Jarrige, A., Bréchemier-Baey, D., Mathy, N., Duché, O., and Portier, C. (2002) Mutational analysis of polynucleotide phosphorylase from Escherichia coli. J. Mol. Biol. 321, 397-409
    • (2002) J. Mol. Biol. , vol.321 , pp. 397-409
    • Jarrige, A.1    Bréchemier-Baey, D.2    Mathy, N.3    Duché, O.4    Portier, C.5
  • 31
    • 55549093442 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation
    • Shi, Z., Yang, W. Z., Lin-Chao, S., Chak, K. F., and Yuan, H. S. (2008) Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. RNA 14, 2361-2371
    • (2008) RNA , vol.14 , pp. 2361-2371
    • Shi, Z.1    Yang, W.Z.2    Lin-Chao, S.3    Chak, K.F.4    Yuan, H.S.5
  • 32
    • 84864242056 scopus 로고    scopus 로고
    • Crystal structure of Caulobacter crescentus polynucleotide phosphorylase reveals a mechanism of RNA substrate channelling and RNA degradosome assembly
    • Hardwick, S. W., Gubbey, T., Hug, I., Jenal, U., and Luisi, B. F. (2012) Crystal structure of Caulobacter crescentus polynucleotide phosphorylase reveals a mechanism of RNA substrate channelling and RNA degradosome assembly. Open Biol. 2, 120028
    • (2012) Open Biol , vol.2 , pp. 120028
    • Hardwick, S.W.1    Gubbey, T.2    Hug, I.3    Jenal, U.4    Luisi, B.F.5
  • 33
    • 84896935548 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 34
    • 0037898952 scopus 로고    scopus 로고
    • Autoinduction and signal transduction in the regulation of staphylococcal virulence
    • Novick, R. P. (2003) Autoinduction and signal transduction in the regulation of staphylococcal virulence. Mol. Microbiol. 48, 1429-1449
    • (2003) Mol. Microbiol. , vol.48 , pp. 1429-1449
    • Novick, R.P.1
  • 35
    • 0035176037 scopus 로고    scopus 로고
    • Cold-temperature induction of Escherichia coli polynucleotide phosphorylase occurs by reversal of its autoregulation
    • DOI 10.1046/j.1365-2958.2001.02216.x
    • Beran, R. K., and Simons, R. W. (2001) Cold-temperature induction of Escherichia coli polynucleotide phosphorylase occurs by reversal of its autoregulation. Mol. Microbiol. 39, 112-125 (Pubitemid 32057681)
    • (2001) Molecular Microbiology , vol.39 , Issue.1 , pp. 112-125
    • Beran, R.K.1    Simons, R.W.2
  • 36
    • 0141532929 scopus 로고    scopus 로고
    • Changes in Escherichia coli transcriptome during acclimatization at low temperature
    • DOI 10.1016/S0923-2508(03)00167-0
    • Polissi, A., De Laurentis, W., Zangrossi, S., Briani, F., Longhi, V., Pesole, G., and Dehò, G. (2003) Changes in Escherichia coli transcriptome during acclimatization at low temperature. Res. Microbiol. 154, 573-580 (Pubitemid 37177001)
    • (2003) Research in Microbiology , vol.154 , Issue.8 , pp. 573-580
    • Polissi, A.1    De Laurentis, W.2    Zangrossi, S.3    Briani, F.4    Longhi, V.5    Pesole, G.6    Deho, G.7
  • 38
    • 33846679926 scopus 로고    scopus 로고
    • Subinhibitory concentrations of β-lactam induce haemolytic activity in Staphylococcus aureus through the SaeRS two-component system
    • DOI 10.1111/j.1574-6968.2006.00568.x
    • Kuroda, H., Kuroda, M., Cui, L., and Hiramatsu, K. (2007) Subinhibitory concentrations of β-lactam induce haemolytic activity in Staphylococcus aureus through the SaeRS two-component system. FEMS Microbiol. Lett. 268, 98-105 (Pubitemid 46192841)
    • (2007) FEMS Microbiology Letters , vol.268 , Issue.1 , pp. 98-105
    • Kuroda, H.1    Kuroda, M.2    Cui, L.3    Hiramatsu, K.4
  • 39
    • 0027169704 scopus 로고
    • The accessory gene regulator (agr) controls Staphylococcus aureus virulence in a murine arthritis model
    • Abdelnour, A., Arvidson, S., Bremell, T., Rydén, C., and Tarkowski, A. (1993) The accessory gene regulator (agr) controls Staphylococcus aureus virulence in a murine arthritis model. Infect. Immun. 61, 3879-3885 (Pubitemid 23260062)
    • (1993) Infection and Immunity , vol.61 , Issue.9 , pp. 3879-3885
    • Abdelnour, A.1    Arvidson, S.2    Bremell, T.3    Ryden, C.4    Tarkowski, A.5
  • 40
    • 77049141059 scopus 로고
    • The structure of ribonucleic acid. I. Cyclic nucleotides produced by ribonuclease and by alkaline hydrolysis
    • Markham, R., and Smith, J. D. (1952) The structure of ribonucleic acid. I. Cyclic nucleotides produced by ribonuclease and by alkaline hydrolysis. Biochem. J. 52, 552-557
    • (1952) Biochem. J. , vol.52 , pp. 552-557
    • Markham, R.1    Smith, J.D.2
  • 41
    • 0030926016 scopus 로고    scopus 로고
    • The human RNA 3'-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea
    • DOI 10.1093/emboj/16.10.2955
    • Genschik, P., Billy, E., Swianiewicz, M., and Filipowicz, W. (1997) The human RNA 3′-terminal phosphate cyclase is a member of a new family of proteins conserved in Eucarya, Bacteria and Archaea. EMBO J. 16, 2955-2967 (Pubitemid 27226231)
    • (1997) EMBO Journal , vol.16 , Issue.10 , pp. 2955-2967
    • Genschik, P.1    Billy, E.2    Swianiewicz, M.3    Filipowicz, W.4
  • 42
    • 0030297538 scopus 로고    scopus 로고
    • tRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • DOI 10.1016/S0092-8674(00)81361-6
    • Sidrauski, C., Cox, J. S., and Walter, P. (1996) tRNA ligase is required for regulated mRNA splicing in the unfolded protein response. Cell 87, 405-413 (Pubitemid 26374315)
    • (1996) Cell , vol.87 , Issue.3 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 43
    • 0028945837 scopus 로고
    • RNA degradation in Escherichia coli regulated by 3′ adenylation and 5′ phosphorylation
    • Xu, F., and Cohen, S. N. (1995) RNA degradation in Escherichia coli regulated by 3′ adenylation and 5′ phosphorylation. Nature 374, 180-183
    • (1995) Nature , vol.374 , pp. 180-183
    • Xu, F.1    Cohen, S.N.2
  • 44
    • 0033548140 scopus 로고    scopus 로고
    • Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro
    • Blum, E., Carpousis, A. J., and Higgins, C. F. (1999) Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro. J. Biol. Chem. 274, 4009-4016
    • (1999) J. Biol. Chem. , vol.274 , pp. 4009-4016
    • Blum, E.1    Carpousis, A.J.2    Higgins, C.F.3
  • 45
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • DOI 10.1038/381169a0
    • Py, B., Higgins, C. F., Krisch, H. M., and Carpousis, A. J. (1996) A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381, 169-172 (Pubitemid 26137967)
    • (1996) Nature , vol.381 , Issue.6578 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 46
    • 48849090895 scopus 로고    scopus 로고
    • The expression of α-haemolysin is required for Staphylococcus aureus phagosomal escape after internalization in CFT-1 cells
    • Jarry, T. M., Memmi, G., and Cheung, A. L. (2008) The expression of α-haemolysin is required for Staphylococcus aureus phagosomal escape after internalization in CFT-1 cells. Cell. Microbiol. 10, 1801-1814
    • (2008) Cell. Microbiol. , vol.10 , pp. 1801-1814
    • Jarry, T.M.1    Memmi, G.2    Cheung, A.L.3
  • 47
    • 0038304134 scopus 로고    scopus 로고
    • Alpha-toxin is required for biofilm formation by Staphylococcus aureus
    • DOI 10.1128/JB.185.10.3214-3217.2003
    • Caiazza, N. C., and O'Toole, G. A. (2003) Alpha-toxin is required for biofilm formation by Staphylococcus aureus. J. Bacteriol. 185, 3214-3217 (Pubitemid 36539119)
    • (2003) Journal of Bacteriology , vol.185 , Issue.10 , pp. 3214-3217
    • Caiazza, N.C.1    O'Toole, G.A.2
  • 48
    • 33846814907 scopus 로고    scopus 로고
    • Surface proteins and exotoxins are required for the pathogenesis of Staphylococcus aureus pneumonia
    • DOI 10.1128/IAI.01313-06
    • Bubeck Wardenburg, J., Patel, R. J., and Schneewind, O. (2007) Surface proteins and exotoxins are required for the pathogenesis of Staphylococcus aureus pneumonia. Infect. Immun. 75, 1040-1044 (Pubitemid 46203470)
    • (2007) Infection and Immunity , vol.75 , Issue.2 , pp. 1040-1044
    • Wardenburg, J.B.1    Patel, R.J.2    Schneewind, O.3
  • 49
    • 36849064891 scopus 로고    scopus 로고
    • Poring over pores: α-hemolysin and Panton-Valentine leukocidin in Staphylococcus aureus pneumonia
    • DOI 10.1038/nm1207-1405, PII NM12071405
    • Bubeck Wardenburg, J., Bae, T., Otto, M., Deleo, F. R., and Schneewind, O. (2007) Poring over pores: α-hemolysin and Panton-Valentine leukocidin in Staphylococcus aureus pneumonia. Nat. Med. 13, 1405-1406 (Pubitemid 350224232)
    • (2007) Nature Medicine , vol.13 , Issue.12 , pp. 1405-1406
    • Wardenburg, J.B.1    Bae, T.2    Otto, M.3    DeLeo, F.R.4    Schneewind, O.5
  • 50
    • 0023807526 scopus 로고
    • Cloning, characterization, and sequencing of an accessory gene regulator (agr) in Staphylococcus aureus
    • Peng, H. L., Novick, R. P., Kreiswirth, B., Kornblum, J., and Schlievert, P. (1988) Cloning, characterization, and sequencing of an accessory gene regulator (agr) in Staphylococcus aureus. J. Bacteriol. 170, 4365-4372
    • (1988) J. Bacteriol. , vol.170 , pp. 4365-4372
    • Peng, H.L.1    Novick, R.P.2    Kreiswirth, B.3    Kornblum, J.4    Schlievert, P.5
  • 54
    • 0031820416 scopus 로고    scopus 로고
    • A Bacillus subtilis gene-encoding protein homologous to eukaryotic SMC motor protein is necessary for chromosome partition
    • DOI 10.1046/j.1365-2958.1998.00919.x
    • Moriya, S., Tsujikawa, E., Hassan, A. K., Asai, K., Kodama, T., and Ogasawara, N. (1998) A Bacillus subtilis gene-encoding protein homologous to eukaryotic SMC motor protein is necessary for chromosome partition. Mol. Microbiol. 29, 179-187 (Pubitemid 28318572)
    • (1998) Molecular Microbiology , vol.29 , Issue.1 , pp. 179-187
    • Moriya, S.1    Tsujikawa, E.2    Hassan, A.K.M.3    Asai, K.4    Kodama, T.5    Ogasawara, N.6
  • 55
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., Dervyn, E., and Ehrlich, S. D. (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144, 3097-3104 (Pubitemid 28515588)
    • (1998) Microbiology , vol.144 , Issue.11 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 57
    • 34147150605 scopus 로고    scopus 로고
    • Regulation of exoprotein gene expression by the Staphylococcus aureus cvfB gene
    • DOI 10.1128/IAI.01552-06
    • Matsumoto, Y., Kaito, C., Morishita, D., Kurokawa, K., and Sekimizu, K. (2007) Regulation of exoprotein gene expression by the Staphylococcus aureus cvfB gene. Infect. Immun. 75, 1964-1972 (Pubitemid 46559466)
    • (2007) Infection and Immunity , vol.75 , Issue.4 , pp. 1964-1972
    • Matsumoto, Y.1    Kaito, C.2    Morishita, D.3    Kurokawa, K.4    Sekimizu, K.5
  • 59
    • 0027327486 scopus 로고
    • The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein
    • DOI 10.1016/0092-8674(93)90420-U
    • Siomi, H., Siomi, M. C., Nussbaum, R. L., and Dreyfuss, G. (1993) The protein product of the fragile X gene, FMR1, has characteristics of an RNA-binding protein. Cell 74, 291-298 (Pubitemid 23221705)
    • (1993) Cell , vol.74 , Issue.2 , pp. 291-298
    • Siomi, H.1    Siomi, M.C.2    Nussbaum, R.L.3    Dreyfuss, G.4


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