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Volumn 2, Issue 5, 2011, Pages

Dynamic distribution of the secA and secY translocase subunits and septal localization of the HtrA surface chaperone/protease during Streptococcus pneumoniae D39 cell division

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; CARRIER PROTEIN; FLOTILLIN 1; FLOTILLIN 2; PEPTIDOGLYCAN; SECA TRANSLOCASE; SECY TRANSLOCASE; SERINE PROTEINASE OMI; UNCLASSIFIED DRUG;

EID: 80455158425     PISSN: None     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00202-11     Document Type: Article
Times cited : (58)

References (50)
  • 2
    • 77952850206 scopus 로고    scopus 로고
    • SecA: A tale of two protomers
    • Sardis MF, Economou A. 2010. SecA: a tale of two protomers. Mol. Microbiol. 76:1070-1081.
    • (2010) Mol. Microbiol , vol.76 , pp. 1070-1081
    • Sardis, M.F.1    Economou, A.2
  • 3
    • 77953453090 scopus 로고    scopus 로고
    • The action of cardiolipin onthe bacterial translocon
    • Gold VA, et al. 2010. The action of cardiolipin onthe bacterial translocon. Proc. Natl. Acad. Sci. U. S. A. 107:10044-10049.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 10044-10049
    • Gold, V.A.1
  • 4
    • 4644287815 scopus 로고    scopus 로고
    • Subcellular sites for bacterial protein export
    • Campo N, et al. 2004. Subcellular sites for bacterial protein export. Mol. Microbiol. 53:1583-1599.
    • (2004) Mol. Microbiol , vol.53 , pp. 1583-1599
    • Campo, N.1
  • 5
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch J, Caparon M. 2004. A microdomain for protein secretion in Gram-positive bacteria. Science 304:1513-1515.
    • (2004) Science , vol.304 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 6
    • 27944484031 scopus 로고    scopus 로고
    • The ExPortal: An organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes
    • Rosch JW, Caparon MG. 2005. The ExPortal: an organelle dedicated to the biogenesis of secreted proteins in Streptococcus pyogenes. Mol. Micro-biol. 58:959-968.
    • (2005) Mol. Micro-biol , vol.58 , pp. 959-968
    • Rosch, J.W.1    Caparon, M.G.2
  • 7
    • 65549129105 scopus 로고    scopus 로고
    • Mechanism for sortase localization and the role of sortase localization in efficient pilus assembly in Enterococcus faecalis
    • Kline KA, et al. 2009. Mechanism for sortase localization and the role of sortase localization in efficient pilus assembly in Enterococcus faecalis. J. Bacteriol. 191:3237-3247.
    • (2009) J. Bacteriol , vol.191 , pp. 3237-3247
    • Kline, K.A.1
  • 8
    • 37349125189 scopus 로고    scopus 로고
    • Sec translocase and sortase A are colocalised in a locus in the cytoplasmic membrane of Streptococcus mutans
    • Hu P, Bian Z, Fan M, Huang M, Zhang P. 2008. Sec translocase and sortase A are colocalised in a locus in the cytoplasmic membrane of Streptococcus mutans. Arch. Oral Biol. 53:150-154.
    • (2008) Arch. Oral Biol , vol.53 , pp. 150-154
    • Hu, P.1    Bian, Z.2    Fan, M.3    Huang, M.4    Zhang, P.5
  • 9
    • 57449114045 scopus 로고    scopus 로고
    • Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane
    • Raz A, Fischetti VA. 2008. Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane. Proc. Natl. Acad. Sci. U. S. A. 105: 18549-18554.
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 18549-18554
    • Raz, A.1    Fischetti, V.A.2
  • 10
    • 33747870454 scopus 로고    scopus 로고
    • Signal sequence directs localized secretion of bacterial surface proteins
    • Carlsson F, et al. 2006. Signal sequence directs localized secretion of bacterial surface proteins. Nature 442:943-946.
    • (2006) Nature , vol.442 , pp. 943-946
    • Carlsson, F.1
  • 11
    • 54349128596 scopus 로고    scopus 로고
    • Signal peptides direct surface proteins totwo distinct envelope locations ofStaphylococcus aureus
    • DeDent A, Bae T, Missiakas DM, Schneewind O. 2008. Signal peptides direct surface proteins totwo distinct envelope locations ofStaphylococcus aureus. EMBO J. 27:2656-2668.
    • (2008) EMBO J , vol.27 , pp. 2656-2668
    • Dedent, A.1    Bae, T.2    Missiakas, D.M.3    Schneewind, O.4
  • 12
    • 77952558570 scopus 로고    scopus 로고
    • Commensal pathogens, with a focus on Streptococcus pneumoniae, and interactions with the human host
    • Henriques-Normark B, Normark S. 2010. Commensal pathogens, with a focus on Streptococcus pneumoniae, and interactions with the human host. Exp. Cell Res. 316:1408-1414.
    • (2010) Exp. Cell Res , vol.316 , pp. 1408-1414
    • Henriques-Normark, B.1    Normark, S.2
  • 13
    • 70350498834 scopus 로고    scopus 로고
    • Pathogenesis, treatment, and prevention of pneumococcal pneumonia
    • van der Poll T, Opal SM. 2009. Pathogenesis, treatment, and prevention of pneumococcal pneumonia. Lancet 374:1543-1556.
    • (2009) Lancet , vol.374 , pp. 1543-1556
    • van der Poll, T.1    Opal, S.M.2
  • 15
    • 2442715491 scopus 로고    scopus 로고
    • Virulence properties of Streptococcus mutans
    • Banas JA. 2004. Virulence properties of Streptococcus mutans. Front. Bio-sci. 9:1267-1277.
    • (2004) Front. Bio-sci , vol.9 , pp. 1267-1277
    • Banas, J.A.1
  • 16
    • 40949162838 scopus 로고    scopus 로고
    • The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease
    • Kadioglu A, Weiser JN, Paton JC, Andrew PW. 2008. The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease. Nat. Rev. Microbiol. 6:288-301.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 288-301
    • Kadioglu, A.1    Weiser, J.N.2    Paton, J.C.3    Andrew, P.W.4
  • 17
    • 70349223864 scopus 로고    scopus 로고
    • A decade of molecular pathog-enomic analysis of group A Streptococcus
    • Musser JM, Shelburne SA, III. 2009. A decade of molecular pathog-enomic analysis of group A Streptococcus. J. Clin. Invest. 119:2455-2463.
    • (2009) J. Clin. Invest , vol.119 , pp. 2455-2463
    • Musser, J.M.1    Shelburne, S.A.2
  • 18
    • 42549137778 scopus 로고    scopus 로고
    • LocateP: Genome-scale subcellular-location predictor for bacterial proteins
    • Zhou M, Boekhorst J, Francke C, Siezen RJ. 2008. LocateP: genome-scale subcellular-location predictor for bacterial proteins. BMC Bioin-form. 9:173.
    • (2008) BMC Bioin-form , vol.9 , pp. 173
    • Zhou, M.1    Boekhorst, J.2    Francke, C.3    Siezen, R.J.4
  • 19
    • 65549117531 scopus 로고    scopus 로고
    • Influences of capsule on cell shape and chain formation of wild-type andpcsB mutants of serotype 2Streptococcus pneu-moniae
    • Barendt SM, et al. 2009. Influences of capsule on cell shape and chain formation of wild-type andpcsB mutants of serotype 2Streptococcus pneu-moniae. J. Bacteriol. 191:3024-3040.
    • (2009) J. Bacteriol , vol.191 , pp. 3024-3040
    • Barendt, S.M.1
  • 20
    • 33845957666 scopus 로고    scopus 로고
    • Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of un-encapsulated laboratory strain R6
    • Lanie JA, et al. 2007. Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of un-encapsulated laboratory strain R6. J. Bacteriol. 189:38-51.
    • (2007) J. Bacteriol , vol.189 , pp. 38-51
    • Lanie, J.A.1
  • 21
    • 79961133524 scopus 로고    scopus 로고
    • The requirement for pneumococcal MreC and MreD is relieved by inactivation of the gene encoding PBP1a
    • Land AD, Winkler ME. 2011. The requirement for pneumococcal MreC and MreD is relieved by inactivation of the gene encoding PBP1a. J. Bac-teriol. 193:4166-4179.
    • (2011) J. Bac-teriol , vol.193 , pp. 4166-4179
    • Land, A.D.1    Winkler, M.E.2
  • 22
    • 0242437870 scopus 로고    scopus 로고
    • Growth and division of Streptococcus pneumoniae: Localization of the high molecular weight penicillin-binding proteins during the cell cycle
    • Morlot C, Zapun A, Dideberg O, Vernet T. 2003. Growth and division of Streptococcus pneumoniae: localization of the high molecular weight penicillin-binding proteins during the cell cycle. Mol. Microbiol. 50: 845-855.
    • (2003) Mol. Microbiol , vol.50 , pp. 845-855
    • Morlot, C.1    Zapun, A.2    Dideberg, O.3    Vernet, T.4
  • 23
    • 78751699495 scopus 로고    scopus 로고
    • A new morphogenesis pathway in bacteria: Unbalanced activity of cell wall synthesis machineries leads to coccus-to-rod transition and filamentation in ovococci
    • Pérez-Núñez D, et al. 2011. A new morphogenesis pathway in bacteria: unbalanced activity of cell wall synthesis machineries leads to coccus-to-rod transition and filamentation in ovococci. Mol. Microbiol. 79: 759-771.
    • (2011) Mol. Microbiol , vol.79 , pp. 759-771
    • Pérez-Núñez, D.1
  • 25
    • 2542617706 scopus 로고    scopus 로고
    • Role of HtrA in the virulence and competence of Streptococcus pneumoniae
    • Ibrahim YM, Kerr AR, McCluskey J, Mitchell TJ. 2004. Role of HtrA in the virulence and competence of Streptococcus pneumoniae. Infect. Im-mun. 72:3584-3591.
    • (2004) Infect. Im-mun , vol.72 , pp. 3584-3591
    • Ibrahim, Y.M.1    Kerr, A.R.2    McCluskey, J.3    Mitchell, T.J.4
  • 26
    • 0023878031 scopus 로고
    • Phosphatidylglycerol is involved in protein translocation across Esche-richia coli inner membranes
    • de Vrije T, de Swart RL, Dowhan W, Tommassen J, de Kruijff B. 1988. Phosphatidylglycerol is involved in protein translocation across Esche-richia coli inner membranes. Nature 334:173-175.
    • (1988) Nature , vol.334 , pp. 173-175
    • de Vrije, T.1    de Swart, R.L.2    Dowhan, W.3    Tommassen, J.4    de Kruijff, B.5
  • 27
    • 33846603187 scopus 로고    scopus 로고
    • Anionic lipids enriched at the ExPortal of Streptococcus pyogenes
    • Rosch JW, Hsu FF, Caparon MG. 2007. Anionic lipids enriched at the ExPortal of Streptococcus pyogenes. J. Bacteriol. 189:801- 806.
    • (2007) J. Bacteriol , vol.189 , pp. 801-806
    • Rosch, J.W.1    Hsu, F.F.2    Caparon, M.G.3
  • 28
    • 32244446796 scopus 로고    scopus 로고
    • Construction and evaluation of a chromosomal expression platform (CEP) for ectopic, maltose-driven gene expression in Streptococcus pneumoniae
    • Guiral S, et al. 2006. Construction and evaluation of a chromosomal expression platform (CEP) for ectopic, maltose-driven gene expression in Streptococcus pneumoniae. Microbiology 152:343-349.
    • (2006) Microbiology , vol.152 , pp. 343-349
    • Guiral, S.1
  • 29
    • 73849125970 scopus 로고    scopus 로고
    • Identification and characterization of noncoding small RNAs in Streptococcus pneumoniae serotype 2 strain D39
    • Tsui HC, et al. 2010. Identification and characterization of noncoding small RNAs in Streptococcus pneumoniae serotype 2 strain D39. J. Bacte-riol. 192:264-279.
    • (2010) J. Bacte-riol , vol.192 , pp. 264-279
    • Tsui, H.C.1
  • 30
    • 0037336363 scopus 로고    scopus 로고
    • fcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae
    • Chan PF, et al. 2003. Characterization of a novel fucose-regulated promoter (PfcsK) suitable for gene essentiality and antibacterial mode-of-action studies in Streptococcus pneumoniae. J. Bacteriol. 185:2051-2058.
    • (2003) J. Bacteriol , vol.185 , pp. 2051-2058
    • Chan, P.F.1
  • 31
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • López D, Kolter R. 2010. Functional microdomains in bacterial membranes. Genes Dev. 24:1893-1902.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • López, D.1    Kolter, R.2
  • 33
    • 79955543481 scopus 로고    scopus 로고
    • Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regu-lon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39
    • Barendt SM, Sham LT, Winkler ME. 2011. Characterization of mutants deficient in the L,D-carboxypeptidase (DacB) and WalRK (VicRK) regu-lon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39. J. Bacteriol. 193:2290-2300.
    • (2011) J. Bacteriol , vol.193 , pp. 2290-2300
    • Barendt, S.M.1    Sham, L.T.2    Winkler, M.E.3
  • 34
    • 77953182143 scopus 로고    scopus 로고
    • The pneumococcal eukaryotic-type serine/threonine protein kinase StkP co-localizes with the cell division apparatus and interacts with FtsZ in vitro
    • Giefing C, Jelencsics KE, Gelbmann D, Senn BM, Nagy E. 2010. The pneumococcal eukaryotic-type serine/threonine protein kinase StkP co-localizes with the cell division apparatus and interacts with FtsZ in vitro. Microbiology 156:1697-1707.
    • (2010) Microbiology , vol.156 , pp. 1697-1707
    • Giefing, C.1    Jelencsics, K.E.2    Gelbmann, D.3    Senn, B.M.4    Nagy, E.5
  • 35
    • 77956540008 scopus 로고    scopus 로고
    • Localization and cellular amounts of the WalRKJ (VicRKX) two-component regulatory system proteins inserotype 2 Streptococcus pneumoniae
    • Wayne KJ, et al. 2010. Localization and cellular amounts of the WalRKJ (VicRKX) two-component regulatory system proteins inserotype 2 Streptococcus pneumoniae. J. Bacteriol. 192:4388-4394.
    • (2010) J. Bacteriol , vol.192 , pp. 4388-4394
    • Wayne, K.J.1
  • 36
    • 42549145631 scopus 로고    scopus 로고
    • Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis
    • Claessen D, et al. 2008. Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis. Mol. Microbiol. 68: 1029-1046.
    • (2008) Mol. Microbiol , vol.68 , pp. 1029-1046
    • Claessen, D.1
  • 37
    • 47249140823 scopus 로고    scopus 로고
    • A new twist on an old pathway-accessory Sec systems
    • Rigel NW, Braunstein M. 2008. A new twist on an old pathway-accessory Sec systems. Mol. Microbiol. 69:291-302.
    • (2008) Mol. Microbiol , vol.69 , pp. 291-302
    • Rigel, N.W.1    Braunstein, M.2
  • 38
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma H, Bolhuis A, Jongbloed JD, Bron S, van Dijl JM. 2000. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64:515-547.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    van Dijl, J.M.5
  • 39
  • 40
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer T, et al. 2008. Structural basis for the regulated protease and chaperone function of DegP. Nature 453:885-890.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1
  • 41
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess C, Beil A, Ehrmann M. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 42
    • 0036074050 scopus 로고    scopus 로고
    • Microarray-based identification of htrA, a Streptococcus pneumoniae gene that is regulated by the CiaRH two-component system and contributes to nasopha-ryngeal colonization
    • Sebert ME, Palmer LM, Rosenberg M, Weiser JN. 2002. Microarray-based identification of htrA, a Streptococcus pneumoniae gene that is regulated by the CiaRH two-component system and contributes to nasopha-ryngeal colonization. Infect. Immun. 70:4059-4067.
    • (2002) Infect. Immun , vol.70 , pp. 4059-4067
    • Sebert, M.E.1    Palmer, L.M.2    Rosenberg, M.3    Weiser, J.N.4
  • 43
    • 62649122954 scopus 로고    scopus 로고
    • Bacteriocin activity of Streptococcus pneumoniae is controlled by the serine protease HtrA via posttran-scriptional regulation
    • Dawid S, Sebert ME, Weiser JN. 2009. Bacteriocin activity of Streptococcus pneumoniae is controlled by the serine protease HtrA via posttran-scriptional regulation. J. Bacteriol. 191:1509-1518.
    • (2009) J. Bacteriol , vol.191 , pp. 1509-1518
    • Dawid, S.1    Sebert, M.E.2    Weiser, J.N.3
  • 44
    • 34548700626 scopus 로고    scopus 로고
    • Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: Five out of 15 promoters drive expression of small non-coding RNAs
    • Halfmann A, Kovács M, Hakenbeck R, Brückner R. 2007. Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: five out of 15 promoters drive expression of small non-coding RNAs. Mol. Microbiol. 66:110-126.
    • (2007) Mol. Microbiol , vol.66 , pp. 110-126
    • Halfmann, A.1    Kovács, M.2    Hakenbeck, R.3    Brückner, R.4
  • 45
    • 33644785222 scopus 로고    scopus 로고
    • The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and by mutations in pbp2x involved in beta-lactam resistance
    • Mascher T, Heintz M, Zähner D, Merai M, Hakenbeck R. 2006. The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and by mutations in pbp2x involved in beta-lactam resistance. J. Bacteriol. 188:1959-1968.
    • (2006) J. Bacteriol , vol.188 , pp. 1959-1968
    • Mascher, T.1    Heintz, M.2    Zähner, D.3    Merai, M.4    Hakenbeck, R.5
  • 46
    • 0026777830 scopus 로고
    • Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding
    • Ulbrandt ND, London E, Oliver DB. 1992. Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding. J. Biol. Chem. 267: 15184-15192.
    • (1992) J. Biol. Chem , vol.267 , pp. 15184-15192
    • Ulbrandt, N.D.1    London, E.2    Oliver, D.B.3
  • 47
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill R, Dowhan W, Wickner W. 1990. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell 60:271-280.
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 48
    • 33645099878 scopus 로고    scopus 로고
    • Role of anionic phospholipids in the adaptation of Bacillus subtilis to high salinity
    • López CS, Alice AF, Heras H, Rivas EA, Sánchez-Rivas C. 2006. Role of anionic phospholipids in the adaptation of Bacillus subtilis to high salinity. Microbiology 152:605-616.
    • (2006) Microbiology , vol.152 , pp. 605-616
    • López, C.S.1    Alice, A.F.2    Heras, H.3    Rivas, E.A.4    Sánchez-Rivas, C.5
  • 49
    • 78651399469 scopus 로고    scopus 로고
    • Staphylococcus aureus requires cardiolipin for survival under conditions of high salinity
    • Tsai M, et al. 2011. Staphylococcus aureus requires cardiolipin for survival under conditions of high salinity. BMC Microbiol. 11:13.
    • (2011) BMC Microbiol , vol.11 , pp. 13
    • Tsai, M.1
  • 50
    • 0035512266 scopus 로고    scopus 로고
    • An rpsL cassette, Janus, for gene replacement through negative selection in Streptococcus pneu-moniae
    • Sung CK, Li H, Claverys JP, Morrison DA. 2001. An rpsL cassette, Janus, for gene replacement through negative selection in Streptococcus pneu-moniae. Appl. Environ. Microbiol. 67:5190-5196.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 5190-5196
    • Sung, C.K.1    Li, H.2    Claverys, J.P.3    Morrison, D.A.4


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