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Volumn 84, Issue 1, 2015, Pages 67-76

RNA helicase important for Listeria monocytogenes hemolytic activity and virulence factor expression

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; ACTIN DEPOLYMERIZING FACTOR A; BACTERIAL PROTEIN; LISTERIOLYSIN O; PRFA PROTEIN; RNA HELICASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR; ACTA PROTEIN, LISTERIA MONOCYTOGENES; BACTERIAL TOXIN; HEAT SHOCK PROTEIN; HEMOLYSIN; HLYA PROTEIN, LISTERIA MONOCYTOGENES; MEMBRANE PROTEIN; PRFA PROTEIN, LISTERIA MONOCYTOGENES; TRANSLATION TERMINATION FACTOR; GLUTATHIONE;

EID: 84957630146     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/iai.00849-15     Document Type: Article
Times cited : (16)

References (65)
  • 1
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py B, Higgins CF, Krisch HM, Carpousis AJ. 1996. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381:169-172. http://dx.doi.org/10.1038/381169a0.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 2
    • 0033214259 scopus 로고    scopus 로고
    • Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3'3' exonuclease and a DEAD-box RNA helicase
    • Coburn GA, Miao X, Briant DJ, Mackie GA. 1999. Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3' exonuclease and a DEAD-box RNA helicase. Genes Dev 13: 2594-2603. http://dx.doi.org/10.1101/gad.13.19.2594.
    • (1999) Genes Dev , vol.13 , pp. 2594-2603
    • Coburn, G.A.1    Miao, X.2    Briant, D.J.3    Mackie, G.A.4
  • 3
    • 84875155719 scopus 로고    scopus 로고
    • Lifelong companions: RNA helicases and their roles in RNA metabolism
    • Klostermeier D. 2013. Lifelong companions: RNA helicases and their roles in RNA metabolism. RNA Biol 10:2-3. http://dx.doi.org/10.4161/rna.23500.
    • (2013) RNA Biol , vol.10 , pp. 2-3
    • Klostermeier, D.1
  • 4
    • 84877921782 scopus 로고    scopus 로고
    • Bacterial helicases in posttranscriptional control
    • Kaberdin VR, Blasi U. 2013. Bacterial helicases in posttranscriptional control. Biochim Biophys Acta 1829:878-883. http://dx.doi.org/10.1016/j.bbagrm.2012.12.005.
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 878-883
    • Kaberdin, V.R.1    Blasi, U.2
  • 5
    • 0016438636 scopus 로고
    • Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure
    • Portier C. 1975. Quaternary structure of Escherichia coli polynucleotide phosphorylase: new evidence for a trimeric structure. FEBS Lett 50:79-81. http://dx.doi.org/10.1016/0014-5793(75)81045-3.
    • (1975) FEBS Lett , vol.50 , pp. 79-81
    • Portier, C.1
  • 6
    • 84866321527 scopus 로고    scopus 로고
    • A Listeria monocytogenes RNA helicase essential for growth and ribosomal maturation at low temperatures uses its C terminus for appropriate interaction with the ribosome
    • Netterling S, Vaitkevicius K, Nord S, Johansson J. 2012. A Listeria monocytogenes RNA helicase essential for growth and ribosomal maturation at low temperatures uses its C terminus for appropriate interaction with the ribosome. J Bacteriol 194:4377-4385. http://dx.doi.org/10.1128/JB.00348-12.
    • (2012) J Bacteriol , vol.194 , pp. 4377-4385
    • Netterling, S.1    Vaitkevicius, K.2    Nord, S.3    Johansson, J.4
  • 7
  • 8
    • 84878106232 scopus 로고    scopus 로고
    • Looking back on the birth of DEAD-box RNAhelicases
    • Linder P, Fuller-Pace FV. 2013. Looking back on the birth of DEAD-box RNAhelicases. Biochim Biophys Acta 1829:750-755. http://dx.doi.org/10.1016/j.bbagrm.2013.03.007.
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 750-755
    • Linder, P.1    Fuller-Pace, F.V.2
  • 9
    • 84877923285 scopus 로고    scopus 로고
    • Functions of DEAD-box proteins in bacteria: current knowledge and pending questions
    • Iost I, Bizebard T, Dreyfus M. 2013. Functions of DEAD-box proteins in bacteria: current knowledge and pending questions. Biochim Biophys Acta 1829:866-877. http://dx.doi.org/10.1016/j.bbagrm.2013.01.012.
    • (2013) Biochim Biophys Acta , vol.1829 , pp. 866-877
    • Iost, I.1    Bizebard, T.2    Dreyfus, M.3
  • 10
    • 79956071179 scopus 로고    scopus 로고
    • DEAD-box proteins as RNA helicases and chaperones
    • Jarmoskaite I, Russell R. 2011. DEAD-box proteins as RNA helicases and chaperones. Wires RNA 2:135-152. http://dx.doi.org/10.1002/wrna.50.
    • (2011) Wires RNA , vol.2 , pp. 135-152
    • Jarmoskaite, I.1    Russell, R.2
  • 11
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: from generic motors to specific dissociation functions
    • Tanner NK, Linder P. 2001. DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol Cell 8:251-262. http://dx.doi.org/10.1016/S1097-2765(01)00329-X.
    • (2001) Mol Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 12
    • 33745219157 scopus 로고    scopus 로고
    • The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1
    • Nagahama M, Yamazoe T, Hara Y, Tani K, Tsuji A, Tagaya M. 2006. The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1. Biochem Biophys Res Commun 346:1075-1082. http://dx.doi.org/10.1016/j.bbrc.2006.06.017.
    • (2006) Biochem Biophys Res Commun , vol.346 , pp. 1075-1082
    • Nagahama, M.1    Yamazoe, T.2    Hara, Y.3    Tani, K.4    Tsuji, A.5    Tagaya, M.6
  • 13
    • 84901634173 scopus 로고    scopus 로고
    • Global effects of the DEAD-box RNA helicase DeaD (CsdA) on gene expression over a broad range of temperatures
    • Vakulskas CA, Pannuri A, Cortes-Selva D, Zere TR, Ahmer BM, Babitzke P, Romeo T. 2014. Global effects of the DEAD-box RNA helicase DeaD (CsdA) on gene expression over a broad range of temperatures. Mol Microbiol 92:945-958. http://dx.doi.org/10.1111/mmi.12606.
    • (2014) Mol Microbiol , vol.92 , pp. 945-958
    • Vakulskas, C.A.1    Pannuri, A.2    Cortes-Selva, D.3    Zere, T.R.4    Ahmer, B.M.5    Babitzke, P.6    Romeo, T.7
  • 15
    • 84923546539 scopus 로고    scopus 로고
    • DExDbox RNA-helicases in Listeria monocytogenes are important for growth, ribosomal maturation, rRNA processing, and virulence factor expression
    • Bareclev C, Vaitkevicius K, Netterling S, Johansson J. 2014. DExDbox RNA-helicases in Listeria monocytogenes are important for growth, ribosomal maturation, rRNA processing, and virulence factor expression. RNA Biol 11:1457-1466. http://dx.doi.org/10.1080/15476286.2014.996099.
    • (2014) RNA Biol , vol.11 , pp. 1457-1466
    • Bareclev, C.1    Vaitkevicius, K.2    Netterling, S.3    Johansson, J.4
  • 16
    • 84862999441 scopus 로고    scopus 로고
    • DEAD-box RNA helicases in gram-positive RNA decay
    • Redder P, Linder P. 2012. DEAD-box RNA helicases in gram-positive RNA decay. Methods Enzymol 511:369-383. http://dx.doi.org/10.1016/B978-0-12-396546-2.00017-6.
    • (2012) Methods Enzymol , vol.511 , pp. 369-383
    • Redder, P.1    Linder, P.2
  • 17
    • 84885070661 scopus 로고    scopus 로고
    • The assembly and distribution in vivo of the Escherichia coli RNA degradosome
    • Dominguez-Malfavon L, Islas LD, Luisi BF, Garcia-Villegas R, Garcia-Mena J. 2013. The assembly and distribution in vivo of the Escherichia coli RNA degradosome. Biochimie 95:2034-2041. http://dx.doi.org/10.1016/j.biochi.2013.07.022.
    • (2013) Biochimie , vol.95 , pp. 2034-2041
    • Dominguez-Malfavon, L.1    Islas, L.D.2    Luisi, B.F.3    Garcia-Villegas, R.4    Garcia-Mena, J.5
  • 19
    • 80053608322 scopus 로고    scopus 로고
    • Characterization of components of the Staphylococcus aureusmRNA degradosome holoenzymelike complex
    • Roux CM, De Muth JP, Dunman PM. 2011. Characterization of components of the Staphylococcus aureusmRNA degradosome holoenzymelike complex. J Bacteriol 193:5520-5526. http://dx.doi.org/10.1128/JB.05485-11.
    • (2011) J Bacteriol , vol.193 , pp. 5520-5526
    • Roux, C.M.1    De Muth, J.P.2    Dunman, P.M.3
  • 20
    • 77955351104 scopus 로고    scopus 로고
    • The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex
    • Lehnik-Habrink M, Pfortner H, Rempeters L, Pietack N, Herzberg C, Stulke J. 2010. The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex. Mol Microbiol 77:958-971. http://dx.doi.org/10.1111/j.1365-2958.2010.07264.x.
    • (2010) Mol Microbiol , vol.77 , pp. 958-971
    • Lehnik-Habrink, M.1    Pfortner, H.2    Rempeters, L.3    Pietack, N.4    Herzberg, C.5    Stulke, J.6
  • 21
    • 84944677098 scopus 로고    scopus 로고
    • The C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogen Staphylococcus aureus
    • Giraud C, Hausmann S, Lemeille S, Prados J, Redder P, Linder P. 2015. The C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogen Staphylococcus aureus. RNA Biol 12:658-674. http://dx.doi.org/10.1080/15476286.2015.1035505.
    • (2015) RNA Biol , vol.12 , pp. 658-674
    • Giraud, C.1    Hausmann, S.2    Lemeille, S.3    Prados, J.4    Redder, P.5    Linder, P.6
  • 22
    • 58249087041 scopus 로고    scopus 로고
    • Assaying DEAD-box RNA helicases and their role inmRNAdegradation in Escherichia coli
    • Carpousis AJ, Khemici V, Poljak L. 2008. Assaying DEAD-box RNA helicases and their role inmRNAdegradation in Escherichia coli. Methods Enzymol 447:183-197. http://dx.doi.org/10.1016/S0076-6879(08)02210-6.
    • (2008) Methods Enzymol , vol.447 , pp. 183-197
    • Carpousis, A.J.1    Khemici, V.2    Poljak, L.3
  • 23
    • 0037174922 scopus 로고    scopus 로고
    • DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • Liou GG, Chang HY, Lin CS, Lin-Chao S. 2002. DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E. J Biol Chem 277:41157-41162. http://dx.doi.org/10.1074/jbc.M206618200.
    • (2002) J Biol Chem , vol.277 , pp. 41157-41162
    • Liou, G.G.1    Chang, H.Y.2    Lin, C.S.3    Lin-Chao, S.4
  • 24
    • 77955931727 scopus 로고    scopus 로고
    • Inactivation of a cold-induced putative RNA helicase gene of Listeria monocytogenes is accompanied by failure to grow at low temperatures but does not affect freeze-thaw tolerance
    • Azizoglu RO, Kathariou S. 2010. Inactivation of a cold-induced putative RNA helicase gene of Listeria monocytogenes is accompanied by failure to grow at low temperatures but does not affect freeze-thaw tolerance. J Food Prot 73:1474-1479.
    • (2010) J Food Prot , vol.73 , pp. 1474-1479
    • Azizoglu, R.O.1    Kathariou, S.2
  • 25
    • 35448958030 scopus 로고    scopus 로고
    • Microarraybased characterization of the Listeria monocytogenes cold regulon in logand stationary-phase cells
    • Chan YC, Raengpradub S, Boor KJ, Wiedmann M. 2007. Microarraybased characterization of the Listeria monocytogenes cold regulon in logand stationary-phase cells. Appl Environ Microbiol 73:6484-6498. http://dx.doi.org/10.1128/AEM.00897-07.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6484-6498
    • Chan, Y.C.1    Raengpradub, S.2    Boor, K.J.3    Wiedmann, M.4
  • 26
    • 84868325448 scopus 로고    scopus 로고
    • Roles of four putative DEAD-box RNA helicase genes in growth of Listeria monocytogenes EGD-e under heat, pH, osmotic, ethanol, and oxidative stress conditions
    • Markkula A, Lindstrom M, Johansson P, Bjorkroth J, Korkeala H. 2012. Roles of four putative DEAD-box RNA helicase genes in growth of Listeria monocytogenes EGD-e under heat, pH, osmotic, ethanol, and oxidative stress conditions. Appl Environ Microbiol 78:6875-6882. http://dx.doi.org/10.1128/AEM.01526-12.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 6875-6882
    • Markkula, A.1    Lindstrom, M.2    Johansson, P.3    Bjorkroth, J.4    Korkeala, H.5
  • 27
    • 84864392067 scopus 로고    scopus 로고
    • Genes encoding putative DEAD-box RNA helicases in Listeria monocytogenes EGD-e are needed for growth and motility at 3°C
    • Markkula A, Mattila M, Lindstrom M, Korkeala H. 2012. Genes encoding putative DEAD-box RNA helicases in Listeria monocytogenes EGD-e are needed for growth and motility at 3°C. Environ Microbiol 14:2223-2232 http://dx.doi.org/10.1111/j.1462-2920.2012.02761.x.
    • (2012) Environ Microbiol , vol.14 , pp. 2223-2232
    • Markkula, A.1    Mattila, M.2    Lindstrom, M.3    Korkeala, H.4
  • 30
    • 84856927549 scopus 로고    scopus 로고
    • Incidence of listeriosis and related mortality among groups at risk of acquiring listeriosis
    • Goulet V, Hebert M, Hedberg C, Laurent E, Vaillant V, De Valk H, Desenclos JC. 2012. Incidence of listeriosis and related mortality among groups at risk of acquiring listeriosis. Clin Infect Dis 54:652-660. http://dx.doi.org/10.1093/cid/cir902.
    • (2012) Clin Infect Dis , vol.54 , pp. 652-660
    • Goulet, V.1    Hebert, M.2    Hedberg, C.3    Laurent, E.4    Vaillant, V.5    De Valk, H.6    Desenclos, J.C.7
  • 31
    • 79960170605 scopus 로고    scopus 로고
    • Transcriptome analysis of Listeria monocytogenes grown on a ready-to-eat meat matrix
    • Bae D, Crowley MR, Wang C. 2011. Transcriptome analysis of Listeria monocytogenes grown on a ready-to-eat meat matrix. J Food Prot 74: 1104-1111. http://dx.doi.org/10.1016/j.jprot.2011.04.004.
    • (2011) J Food Prot , vol.74 , pp. 1104-1111
    • Bae, D.1    Crowley, M.R.2    Wang, C.3
  • 32
    • 33750725730 scopus 로고    scopus 로고
    • Listeria monocytogenes: food-borne pathogen and hygiene indicator
    • Jemmi T, Stephan R. 2006. Listeria monocytogenes: food-borne pathogen and hygiene indicator. Rev Sci Technol 25:571-580.
    • (2006) Rev Sci Technol , vol.25 , pp. 571-580
    • Jemmi, T.1    Stephan, R.2
  • 33
    • 3042691769 scopus 로고    scopus 로고
    • HrpA, a DEAH-box RNA helicase, is involved in mRNA processing of a fimbrial operon in Escherichia coli
    • Koo JT, Choe J, Moseley SL. 2004. HrpA, a DEAH-box RNA helicase, is involved in mRNA processing of a fimbrial operon in Escherichia coli. Mol Microbiol 52:1813-1826. http://dx.doi.org/10.1111/j.1365-2958.2004.04099.x.
    • (2004) Mol Microbiol , vol.52 , pp. 1813-1826
    • Koo, J.T.1    Choe, J.2    Moseley, S.L.3
  • 34
    • 84892878516 scopus 로고    scopus 로고
    • HrpA, an RNA helicase involved in RNA processing, is required for mouse infectivity and tick transmission of the Lyme disease spirochete
    • Salman-Dilgimen A, Hardy PO, Radolf JD, Caimano MJ, Chaconas G. 2013. HrpA, an RNA helicase involved in RNA processing, is required for mouse infectivity and tick transmission of the Lyme disease spirochete. PLoS Pathog 9:e1003841. http://dx.doi.org/10.1371/journal.ppat.1003841.
    • (2013) PLoS Pathog , vol.9
    • Salman-Dilgimen, A.1    Hardy, P.O.2    Radolf, J.D.3    Caimano, M.J.4    Chaconas, G.5
  • 35
    • 84937936475 scopus 로고    scopus 로고
    • The RNA helicase DeaD stimulates ExsA translation to promote expression of the Pseudomonas aeruginosa type III secretion system
    • Intile PJ, Balzer GJ, Wolfgang MC, Yahr TL. 2015. The RNA helicase DeaD stimulates ExsA translation to promote expression of the Pseudomonas aeruginosa type III secretion system. J Bacteriol 197:2664-2674. http://dx.doi.org/10.1128/JB.00231-15.
    • (2015) J Bacteriol , vol.197 , pp. 2664-2674
    • Intile, P.J.1    Balzer, G.J.2    Wolfgang, M.C.3    Yahr, T.L.4
  • 36
    • 84857870455 scopus 로고    scopus 로고
    • An unstructured 5'-coding region of the prfA mRNA is required for efficient translation
    • Loh E, Memarpour F, Vaitkevicius K, Kallipolitis BH, Johansson J, Sonden B. 2012. An unstructured 5'-coding region of the prfA mRNA is required for efficient translation. Nucleic Acids Res 40:1818-1827. http://dx.doi.org/10.1093/nar/gkr850.
    • (2012) Nucleic Acids Res , vol.40 , pp. 1818-1827
    • Loh, E.1    Memarpour, F.2    Vaitkevicius, K.3    Kallipolitis, B.H.4    Johansson, J.5    Sonden, B.6
  • 37
    • 0037031594 scopus 로고    scopus 로고
    • An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes
    • Johansson J, Mandin P, Renzoni A, Chiaruttini C, Springer M, Cossart P. 2002. An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes. Cell 110:551-561. http://dx.doi.org/10.1016/S0092-8674(02)00905-4.
    • (2002) Cell , vol.110 , pp. 551-561
    • Johansson, J.1    Mandin, P.2    Renzoni, A.3    Chiaruttini, C.4    Springer, M.5    Cossart, P.6
  • 39
    • 84864359154 scopus 로고    scopus 로고
    • Optimizing the balance between host and environmental survival skills: lessons learned from Listeria monocytogenes
    • Xayarath B, Freitag NE. 2012. Optimizing the balance between host and environmental survival skills: lessons learned from Listeria monocytogenes. Future Microbiol 7:839-852. http://dx.doi.org/10.2217/fmb.12.57.
    • (2012) Future Microbiol , vol.7 , pp. 839-852
    • Xayarath, B.1    Freitag, N.E.2
  • 41
    • 0025856654 scopus 로고
    • Pleiotropic control of Listeria monocytogenes virulence factors by a gene that is autoregulated
    • Mengaud J, Dramsi S, Gouin E, Vazquez-Boland JA, Milon G, Cossart P. 1991. Pleiotropic control of Listeria monocytogenes virulence factors by a gene that is autoregulated. Mol Microbiol 5:2273-2283. http://dx.doi.org/10.1111/j.1365-2958.1991.tb02158.x.
    • (1991) Mol Microbiol , vol.5 , pp. 2273-2283
    • Mengaud, J.1    Dramsi, S.2    Gouin, E.3    Vazquez-Boland, J.A.4    Milon, G.5    Cossart, P.6
  • 42
    • 17144398027 scopus 로고    scopus 로고
    • The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif
    • Eiting M, Hageluken G, Schubert WD, Heinz DW. 2005. The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif. Mol Microbiol 56:433-446. http://dx.doi.org/10.1111/j.1365-2958.2005.04561.x.
    • (2005) Mol Microbiol , vol.56 , pp. 433-446
    • Eiting, M.1    Hageluken, G.2    Schubert, W.D.3    Heinz, D.W.4
  • 43
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria
    • Arnaud M, Chastanet A, Debarbouille M. 2004. New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, gram-positive bacteria. Appl Environ Microbiol 70:6887-6891. http://dx.doi.org/10.1128/AEM.70.11.6887-6891.2004.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Debarbouille, M.3
  • 44
    • 0008456114 scopus 로고
    • Biochemical and immunological effects of Listeria monocytogenes hemolysin
    • Kingdon GC, Sword CP. 1970. Biochemical and immunological effects of Listeria monocytogenes hemolysin. Infect Immun 1:363-372.
    • (1970) Infect Immun , vol.1 , pp. 363-372
    • Kingdon, G.C.1    Sword, C.P.2
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. http://dx.doi.org/10.1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 0028872473 scopus 로고
    • An efficient method for preparation of extracts from Gram-positive bacteria for comparison of cellular protein patterns
    • Kampfer P. 1995. An efficient method for preparation of extracts from Gram-positive bacteria for comparison of cellular protein patterns. J Microbiol Methods 21:55-60. http://dx.doi.org/10.1016/0167-7012(94)00033-4.
    • (1995) J Microbiol Methods , vol.21 , pp. 55-60
    • Kampfer, P.1
  • 47
    • 25844458478 scopus 로고    scopus 로고
    • Hfq-dependent regulation ofOmpAsynthesis is mediated by an antisense RNA
    • Udekwu KI, Darfeuille F, Vogel J, Reimegard J, Holmqvist E, Wagner EG. 2005. Hfq-dependent regulation ofOmpAsynthesis is mediated by an antisense RNA. Genes Dev 19:2355-2366. http://dx.doi.org/10.1101/gad.354405.
    • (2005) Genes Dev , vol.19 , pp. 2355-2366
    • Udekwu, K.I.1    Darfeuille, F.2    Vogel, J.3    Reimegard, J.4    Holmqvist, E.5    Wagner, E.G.6
  • 49
    • 0037128931 scopus 로고    scopus 로고
    • Listeriolysin O: a genuine cytolysin optimized for an intracellular parasite
    • Dramsi S, Cossart P. 2002. Listeriolysin O: a genuine cytolysin optimized for an intracellular parasite. J Cell Biol 156:943-946. http://dx.doi.org/10.1083/jcb.200202121.
    • (2002) J Cell Biol , vol.156 , pp. 943-946
    • Dramsi, S.1    Cossart, P.2
  • 50
    • 33744948764 scopus 로고    scopus 로고
    • Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions
    • Kayal S, Charbit A. 2006. Listeriolysin O: a key protein of Listeria monocytogenes with multiple functions. FEMS Microbiol Rev 30:514-529. http://dx.doi.org/10.1111/j.1574-6976.2006.00021.x.
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 514-529
    • Kayal, S.1    Charbit, A.2
  • 51
    • 34548490518 scopus 로고    scopus 로고
    • Listeriolysin O: a phagosome-specific lysin
    • Schnupf P, Portnoy DA. 2007. Listeriolysin O: a phagosome-specific lysin. Microbes Infect 9:1176-1187. http://dx.doi.org/10.1016/j.micinf.2007.05.005.
    • (2007) Microbes Infect , vol.9 , pp. 1176-1187
    • Schnupf, P.1    Portnoy, D.A.2
  • 52
    • 0037128936 scopus 로고    scopus 로고
    • The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells
    • Glomski IJ, Gedde MM, Tsang AW, Swanson JA, Portnoy DA. 2002. The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells. J Cell Biol 156:1029-1038. http://dx.doi.org/10.1083/jcb.200201081.
    • (2002) J Cell Biol , vol.156 , pp. 1029-1038
    • Glomski, I.J.1    Gedde, M.M.2    Tsang, A.W.3    Swanson, J.A.4    Portnoy, D.A.5
  • 53
  • 55
    • 69249090504 scopus 로고    scopus 로고
    • Listeria monocytogenes: from saprophyte to intracellular pathogen
    • Freitag NE, Port GC, Miner MD. 2009. Listeria monocytogenes: from saprophyte to intracellular pathogen. Nat Rev Microbiol 7:623-628. http://dx.doi.org/10.1038/nrmicro2171.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 623-628
    • Freitag, N.E.1    Port, G.C.2    Miner, M.D.3
  • 56
    • 84873428099 scopus 로고    scopus 로고
    • Cycles of light and dark co-ordinate reversible colony differentiation in Listeria monocytogenes
    • Tiensuu T, Andersson C, Ryden P, Johansson J. 2013. Cycles of light and dark co-ordinate reversible colony differentiation in Listeria monocytogenes. Mol Microbiol 87:909-924. http://dx.doi.org/10.1111/mmi.12140.
    • (2013) Mol Microbiol , vol.87 , pp. 909-924
    • Tiensuu, T.1    Andersson, C.2    Ryden, P.3    Johansson, J.4
  • 58
    • 80051636253 scopus 로고    scopus 로고
    • Probing the role of protein surface charge in the activation of PrfA, the central regulator of Listeria monocytogenes pathogenesis
    • Xayarath B, Volz KW, Smart JI, Freitag NE. 2011. Probing the role of protein surface charge in the activation of PrfA, the central regulator of Listeria monocytogenes pathogenesis. PLoS One 6:e23502. http://dx.doi.org/10.1371/journal.pone.0023502.
    • (2011) PLoS One , vol.6
    • Xayarath, B.1    Volz, K.W.2    Smart, J.I.3    Freitag, N.E.4
  • 60
    • 0023617861 scopus 로고
    • In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2
    • Gaillard JL, Berche P, Mounier J, Richard S, Sansonetti P. 1987. In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2. Infect Immun 55:2822-2829.
    • (1987) Infect Immun , vol.55 , pp. 2822-2829
    • Gaillard, J.L.1    Berche, P.2    Mounier, J.3    Richard, S.4    Sansonetti, P.5
  • 62
    • 0031024403 scopus 로고    scopus 로고
    • Carbonsource regulation of virulence gene expression in Listeria monocytogenes
    • Milenbachs AA, Brown DP, Moors M, Youngman P. 1997. Carbonsource regulation of virulence gene expression in Listeria monocytogenes. Mol Microbiol 23:1075-1085. http://dx.doi.org/10.1046/j.1365-2958.1997.2711634.x.
    • (1997) Mol Microbiol , vol.23 , pp. 1075-1085
    • Milenbachs, A.A.1    Brown, D.P.2    Moors, M.3    Youngman, P.4
  • 63
    • 0029830548 scopus 로고    scopus 로고
    • Specific binding of the Listeria monocytogenes transcriptional regulator PrfA to target sequences requires additional factor(s) and is influenced by iron
    • Bockmann R, Dickneite C, Middendorf B, Goebel W, Sokolovic Z. 1996 Specific binding of the Listeria monocytogenes transcriptional regulator PrfA to target sequences requires additional factor(s) and is influenced by iron. Mol Microbiol 22:643-653. http://dx.doi.org/10.1046/j.1365-2958.1996.d01-1722.x.
    • (1996) Mol Microbiol , vol.22 , pp. 643-653
    • Bockmann, R.1    Dickneite, C.2    Middendorf, B.3    Goebel, W.4    Sokolovic, Z.5
  • 64
    • 0003191832 scopus 로고
    • BRL pUC host: Escherichia coli DH5α competent cells
    • Bethesda Research Laboratories. 1986. BRL pUC host: Escherichia coli DH5α competent cells. Focus 8:9.
    • (1986) Focus , vol.8 , pp. 9


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