메뉴 건너뛰기
mBio
Volumn 6, Issue 1, 2014, Pages
LocZ is a new cell division protein involved in proper septum placement in Streptococcus pneumoniae
Author keywords

[No Author keywords available]
Indexed keywords

BACTERIAL PROTEIN; LOCZ PROTEIN; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN;
EID: 84924178704     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01700-14     Document Type: Article
Times cited : (76)
References (64)
  • 1
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi EF, Lutkenhaus J. 1991. FtsZ ring structure associated with division in Escherichia coli. Nature 354: 161-164. http://dx. doi. org/10. 1038/354161a0.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 2
    • 0020054652 scopus 로고
    • On the precision and accuracy achieved by Escherichia coli cells at fission about their middle
    • Trueba FJ. 1982. On the precision and accuracy achieved by Escherichia coli cells at fission about their middle. Arch Microbiol 131: 55-59. http://dx. doi. org/10. 1007/BF00451499.
    • (1982) Arch Microbiol , vol.131 , pp. 55-59
    • Trueba, F.J.1
  • 3
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • de Boer PA. 2010. Advances in understanding E. coli cell fission. Curr Opin Microbiol 13: 730-737. http://dx. doi. org/10. 1016/j. mib. 2010. 09. 015.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 730-737
    • de Boer, P.A.1
  • 4
    • 84872856522 scopus 로고    scopus 로고
    • The physiology of bacterial cell division
    • Egan AJ, Vollmer W. 2013. The physiology of bacterial cell division. Ann N Y Acad Sci 1277: 8-28. http://dx. doi. org/10. 1111/j. 1749-6632. 2012. 06818. x.
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 8-28
    • Egan, A.J.1    Vollmer, W.2
  • 5
    • 84867995401 scopus 로고    scopus 로고
    • Bacterial cytokinesis: From Z ring to divisome
    • Lutkenhaus J, Pichoff S, Du S. 2012. Bacterial cytokinesis: from Z ring to divisome. Cytoskeleton (Hoboken) 69: 778-790. http://dx. doi. org/10. 1002/cm. 21054.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 6
    • 84880563030 scopus 로고    scopus 로고
    • In the beginning, Escherichia coli assembled the proto-ring: An initial phase of division
    • Rico AI, Krupka M, Vicente M. 2013. In the beginning, Escherichia coli assembled the proto-ring: an initial phase of division. J Biol Chem 288: 20830-20836. http://dx. doi. org/10. 1074/jbc. R113. 479519.
    • (2013) J Biol Chem , vol.288 , pp. 20830-20836
    • Rico, A.I.1    Krupka, M.2    Vicente, M.3
  • 7
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin W. 2005. FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 6: 862-871. http://dx. doi. org/10. 1038/nrm1745.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 862-871
    • Margolin, W.1
  • 8
    • 84897651217 scopus 로고    scopus 로고
    • Division site positioning in bacteria: One size does not fit all
    • Monahan LG, Liew AT, Bottomley AL, Harry EJ. 2014. Division site positioning in bacteria: one size does not fit all. Front Microbiol 5: 19. http://dx. doi. org/10. 3389/fmicb. 2014. 00019.
    • (2014) Front Microbiol , vol.5
    • Monahan, L.G.1    Liew, A.T.2    Bottomley, A.L.3    Harry, E.J.4
  • 9
    • 34047118117 scopus 로고    scopus 로고
    • Division site recognition in Escherichia coli and Bacillus subtilis
    • Barák I, Wilkinson AJ. 2007. Division site recognition in Escherichia coli and Bacillus subtilis. FEMS Microbiol Rev 31: 311-326. http://dx. doi. org/10. 1111/j. 1574-6976. 2007. 00067. x.
    • (2007) FEMS Microbiol Rev , vol.31 , pp. 311-326
    • Barák, I.1    Wilkinson, A.J.2
  • 10
    • 0035010154 scopus 로고    scopus 로고
    • Bacterial cell division: Regulating Z-ring formation
    • Harry EJ. 2001. Bacterial cell division: regulating Z-ring formation. Mol Microbiol 40: 795-803. http://dx. doi. org/10. 1046/j. 1365-2958. 2001. 02370. x.
    • (2001) Mol Microbiol , vol.40 , pp. 795-803
    • Harry, E.J.1
  • 11
    • 0035196036 scopus 로고    scopus 로고
    • Spatial regulation of cytokinesis in bacteria
    • Margolin W. 2001. Spatial regulation of cytokinesis in bacteria. Curr Opin Microbiol 4: 647-652. http://dx. doi. org/10. 1016/S1369-5274(01)00264-8.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 647-652
    • Margolin, W.1
  • 12
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli
    • Bernhardt TG, de Boer PA. 2005. SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli. Mol Cell 18: 555-564. http://dx. doi. org/10. 1016/j. molcel. 2005. 04. 012.
    • (2005) Mol Cell , vol.18 , pp. 555-564
    • Bernhardt, T.G.1    de Boer, P.A.2
  • 13
    • 79952741894 scopus 로고    scopus 로고
    • Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho H, McManus HR, Dove SL, Bernhardt TG. 2011. Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc Natl Acad Sci U S A 108: 3773-3778. http://dx. doi. org/10. 1073/pnas. 1018674108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3    Bernhardt, T.G.4
  • 15
    • 84879531614 scopus 로고    scopus 로고
    • SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid
    • Tonthat NK, Milam SL, Chinnam N, Whitfill T, Margolin W, Schumacher MA. 2013. SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid. Proc Natl Acad Sci U S A 110: 10586-10591. http://dx. doi. org/10. 1073/pnas. 1221036110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 10586-10591
    • Tonthat, N.K.1    Milam, S.L.2    Chinnam, N.3    Whitfill, T.4    Margolin, W.5    Schumacher, M.A.6
  • 16
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis
    • Wu LJ, Errington J. 2004. Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis. Cell 117: 915-925. http://dx. doi. org/10. 1016/j. cell. 2004. 06. 002.
    • (2004) Cell , vol.117 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 17
    • 67650435786 scopus 로고    scopus 로고
    • Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation
    • Wu LJ, Ishikawa S, Kawai Y, Oshima T, Ogasawara N, Errington J. 2009. Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation. EMBO J 28: 1940-1952. http://dx. doi. org/10. 1038/emboj. 2009. 144.
    • (2009) EMBO J , vol.28 , pp. 1940-1952
    • Wu, L.J.1    Ishikawa, S.2    Kawai, Y.3    Oshima, T.4    Ogasawara, N.5    Errington, J.6
  • 18
    • 83855160828 scopus 로고    scopus 로고
    • Nucleoid occlusion and bacterial cell division
    • Wu LJ, Errington J. 2012. Nucleoid occlusion and bacterial cell division. Nat Rev Microbiol 10: 8-12. http://dx. doi. org/10. 1038/nrmicro2671.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 8-12
    • Wu, L.J.1    Errington, J.2
  • 19
    • 0023876706 scopus 로고
    • Isolation and properties of minB, a complex genetic locus involved in correct placement of the division site in Escherichia coli
    • de Boer PA, Crossley RE, Rothfield LI. 1988. Isolation and properties of minB, a complex genetic locus involved in correct placement of the division site in Escherichia coli. J Bacteriol 170: 2106-2112.
    • (1988) J Bacteriol , vol.170 , pp. 2106-2112
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 20
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
    • de Boer PA, Crossley RE, Rothfield LI. 1989. A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 56: 641-649. http://dx. doi. org/10. 1016/0092-8674(89)90586-2.
    • (1989) Cell , vol.56 , pp. 641-649
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 21
    • 0026585155 scopus 로고
    • Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli
    • de Boer PA, Crossley RE, Rothfield LI. 1992. Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli. J Bacteriol 174: 63-70.
    • (1992) J Bacteriol , vol.174 , pp. 63-70
    • de Boer, P.A.1    Crossley, R.E.2    Rothfield, L.I.3
  • 22
    • 0027478595 scopus 로고
    • The minCD locus of Bacillus subtilis lacks the minE determinant that provides topological specificity to cell division
    • Lee S, Price CW. 1993. The minCD locus of Bacillus subtilis lacks the minE determinant that provides topological specificity to cell division. Mol Microbiol 7: 601-610. h t t p://d x. d o i. o r g/1 0. 1 1 1 1/j. 1 3 6 5-2958. 1993. tb01151. x.
    • (1993) Mol Microbiol , vol.7 , pp. 601-610
    • Lee, S.1    Price, C.W.2
  • 23
    • 0033592949 scopus 로고    scopus 로고
    • The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
    • Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J. 1999. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Proc Natl Acad Sci U S A 96: 14819-14824. http://dx. doi. org/10. 1073/pnas. 96. 26. 14819.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 14819-14824
    • Hu, Z.1    Mukherjee, A.2    Pichoff, S.3    Lutkenhaus, J.4
  • 24
    • 0034750707 scopus 로고    scopus 로고
    • Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation
    • Pichoff S, Lutkenhaus J. 2001. Escherichia coli division inhibitor MinCD blocks septation by preventing Z-ring formation. J Bacteriol 183: 6630-6635. http://dx. doi. org/10. 1128/JB. 183. 22. 6630-6635. 2001.
    • (2001) J Bacteriol , vol.183 , pp. 6630-6635
    • Pichoff, S.1    Lutkenhaus, J.2
  • 27
    • 33846246039 scopus 로고    scopus 로고
    • Bacterial cell division: The mechanism and its precision
    • Harry E, Monahan L, Thompson L. 2006. Bacterial cell division: the mechanism and its precision. Int Rev Cytol 253: 27-94. http://dx. doi. org/10. 1016/S0074-7696(06)53002-5.
    • (2006) Int Rev Cytol , vol.253 , pp. 27-94
    • Harry, E.1    Monahan, L.2    Thompson, L.3
  • 28
    • 33745699284 scopus 로고    scopus 로고
    • MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter
    • Thanbichler M, Shapiro L. 2006. MipZ, a spatial regulator coordinating chromosome segregation with cell division in Caulobacter. Cell 126: 147-162. http://dx. doi. org/10. 1016/j. cell. 2006. 05. 038.
    • (2006) Cell , vol.126 , pp. 147-162
    • Thanbichler, M.1    Shapiro, L.2
  • 30
    • 0014733740 scopus 로고
    • Model for cell wall growth of Streptococcus faecalis
    • Higgins ML, Shockman GD. 1970. Model for cell wall growth of Streptococcus faecalis. J Bacteriol 101: 643-648.
    • (1970) J Bacteriol , vol.101 , pp. 643-648
    • Higgins, M.L.1    Shockman, G.D.2
  • 31
    • 0017141619 scopus 로고
    • Study of cycle of cell wall assembly in Streptococcus faecalis by three-dimensional reconstructions of thin sections of cells
    • Higgins ML, Shockman GD. 1976. Study of cycle of cell wall assembly in Streptococcus faecalis by three-dimensional reconstructions of thin sections of cells. J Bacteriol 127: 1346-1358.
    • (1976) J Bacteriol , vol.127 , pp. 1346-1358
    • Higgins, M.L.1    Shockman, G.D.2
  • 32
    • 0003302183 scopus 로고    scopus 로고
    • Streptococcus pneumoniae: Functional anatomy
    • Tomasz A (ed), Mary Ann Liebert Publishing, New York, NY
    • Tomasz A. 2000. Streptococcus pneumoniae: functional anatomy, p 9-21. In Tomasz A (ed), Streptococcus pneumoniae: molecular biology and mechanisms of disease. Mary Ann Liebert Publishing, New York, NY.
    • (2000) Streptococcus pneumoniae: Molecular biology and mechanisms of disease , pp. 9-21
    • Tomasz, A.1
  • 33
    • 84888857354 scopus 로고    scopus 로고
    • From models to pathogens: How much have we learned about Streptococcus pneumoniae cell division?
    • Massidda O, Nováková L, Vollmer W. 2013. From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division? Environ Microbiol 15: 3133-3157. http://dx. doi. org/10. 1111/1462-2920. 12189.
    • (2013) Environ Microbiol , vol.15 , pp. 3133-3157
    • Massidda, O.1    Nováková, L.2    Vollmer, W.3
  • 34
    • 84882662775 scopus 로고    scopus 로고
    • How to get (a)round: Mechanisms controlling growth and division of coccoid bacteria
    • Pinho MG, Kjos M, Veening JW. 2013. How to get (a)round: mechanisms controlling growth and division of coccoid bacteria. Nat Rev Microbiol 11: 601-614. http://dx. doi. org/10. 1038/nrmicro3088.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 601-614
    • Pinho, M.G.1    Kjos, M.2    Veening, J.W.3
  • 35
    • 82155168230 scopus 로고    scopus 로고
    • Superresolution microscopy reveals cell wall dynamics and peptidoglycan architecture in ovococcal bacteria
    • Wheeler R, Mesnage S, Boneca IG, Hobbs JK, Foster SJ. 2011. Superresolution microscopy reveals cell wall dynamics and peptidoglycan architecture in ovococcal bacteria. Mol Microbiol 82: 1096-1109. http://dx. doi. org/10. 1111/j. 1365-2958. 2011. 07871. x.
    • (2011) Mol Microbiol , vol.82 , pp. 1096-1109
    • Wheeler, R.1    Mesnage, S.2    Boneca, I.G.3    Hobbs, J.K.4    Foster, S.J.5
  • 37
    • 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. http://dx. doi. org/10. 1046/j. 1365-2958. 2003. 03767. x.
    • (2003) Mol Microbiol , vol.50 , pp. 845-855
    • Morlot, C.1    Zapun, A.2    Dideberg, O.3    Vernet, T.4
  • 38
    • 84859576482 scopus 로고    scopus 로고
    • Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP
    • Beilharz K, Nováková L, Fadda D, Branny P, Massidda O, Veening JW. 2012. Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP. Proc Natl Acad Sci U S A 109: E905-E913. http://dx. doi. org/10. 1073/pnas. 1119172109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. E905-E913
    • Beilharz, K.1    Nováková, L.2    Fadda, D.3    Branny, P.4    Massidda, O.5    Veening, J.W.6
  • 39
    • 1642442760 scopus 로고    scopus 로고
    • The D, D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae
    • Morlot C, Noirclerc-Savoye M, Zapun A, Dideberg O, Vernet T. 2004. The D, D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae. Mol Microbiol 51: 1641-1648. http://dx. doi. org/10. 1046/j. 1365-2958. 2003. 03953. x.
    • (2004) Mol Microbiol , vol.51 , pp. 1641-1648
    • Morlot, C.1    Noirclerc-Savoye, M.2    Zapun, A.3    Dideberg, O.4    Vernet, T.5
  • 40
    • 13144257721 scopus 로고    scopus 로고
    • In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae
    • Noirclerc-Savoye M, Le Gouëllec A, Morlot C, Dideberg O, Vernet T, Zapun A. 2005. In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae. Mol Microbiol 55: 413-424. http://dx. doi. org/10. 1111/j. 1365-2958. 2004. 04408. x.
    • (2005) Mol Microbiol , vol.55 , pp. 413-424
    • Noirclerc-Savoye, M.1    Le Gouëllec, A.2    Morlot, C.3    Dideberg, O.4    Vernet, T.5    Zapun, A.6
  • 41
    • 33846922483 scopus 로고    scopus 로고
    • Streptococcus pneumoniae DivIVA: Localization and interactions in a MinCD-free context
    • Fadda D, Santona A, D'Ulisse V, Ghelardini P, Ennas MG, Whalen MB, Massidda O. 2007. Streptococcus pneumoniae DivIVA: localization and interactions in a MinCD-free context. J Bacteriol 189: 1288-1298. http://dx. doi. org/10. 1128/JB. 01168-06.
    • (2007) J Bacteriol , vol.189 , pp. 1288-1298
    • Fadda, D.1    Santona, A.2    D'Ulisse, V.3    Ghelardini, P.4    Ennas, M.G.5    Whalen, M.B.6    Massidda, O.7
  • 42
    • 77954414035 scopus 로고    scopus 로고
    • Identification of multiple substrates of the StkP Ser/Thr protein kinase in Streptococcus pneumoniae
    • Nováková L, Bezousková S, Pompach P, Spidlová P, Sasková L, Weiser J, Branny P. 2010. Identification of multiple substrates of the StkP Ser/Thr protein kinase in Streptococcus pneumoniae. J Bacteriol 192: 3629-3638. http://dx. doi. org/10. 1128/JB. 01564-09.
    • (2010) J Bacteriol , vol.192 , pp. 3629-3638
    • Nováková, L.1    Bezousková, S.2    Pompach, P.3    Spidlová, P.4    Sasková, L.5    Weiser, J.6    Branny, P.7
  • 43
    • 70449535630 scopus 로고    scopus 로고
    • A self-deleting Cre-lox-ermAM cassette, Cheshire, for marker-less gene deletion in Streptococcus pneumoniae
    • Weng L, Biswas I, Morrison DA. 2009. A self-deleting Cre-lox-ermAM cassette, Cheshire, for marker-less gene deletion in Streptococcus pneumoniae. J Microbiol Methods 79: 353-357. http://dx. doi. org/10. 1016/j. mimet. 2009. 10. 007.
    • (2009) J Microbiol Methods , vol.79 , pp. 353-357
    • Weng, L.1    Biswas, I.2    Morrison, D.A.3
  • 44
    • 34249801777 scopus 로고    scopus 로고
    • Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae
    • Sasková L, Nováková L, Basler M, Branny P. 2007. Eukaryotic-type serine/threonine protein kinase StkP is a global regulator of gene expression in Streptococcus pneumoniae. J Bacteriol 189: 4168-4179. http://dx. doi. org/10. 1128/JB. 01616-06.
    • (2007) J Bacteriol , vol.189 , pp. 4168-4179
    • Sasková, L.1    Nováková, L.2    Basler, M.3    Branny, P.4
  • 45
    • 79955024764 scopus 로고    scopus 로고
    • Highthroughput, subpixel precision analysis of bacterial morphogenesis and intracellular spatio-temporal dynamics
    • Sliusarenko O, Heinritz J, Emonet T, Jacobs-Wagner C. 2011. Highthroughput, subpixel precision analysis of bacterial morphogenesis and intracellular spatio-temporal dynamics. Mol Microbiol 80: 612-627. http://dx. doi. org/10. 1111/j. 1365-2958. 2011. 07579. x.
    • (2011) Mol Microbiol , vol.80 , pp. 612-627
    • Sliusarenko, O.1    Heinritz, J.2    Emonet, T.3    Jacobs-Wagner, C.4
  • 46
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • Daniel RA, Errington J. 2003. Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113: 767-776. http://dx. doi. org/10. 1016/S0092-8674(03)00421-5.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 47
    • 70349920678 scopus 로고    scopus 로고
    • Cellular localization of choline-utilization proteins in Streptococcus pneumoniae using novel fluorescent reporter systems
    • Eberhardt A, Wu LJ, Errington J, Vollmer W, Veening JW. 2009. Cellular localization of choline-utilization proteins in Streptococcus pneumoniae using novel fluorescent reporter systems. Mol Microbiol 74: 395-408. http://dx. doi. org/10. 1111/j. 1365-2958. 2009. 06872. x.
    • (2009) Mol Microbiol , vol.74 , pp. 395-408
    • Eberhardt, A.1    Wu, L.J.2    Errington, J.3    Vollmer, W.4    Veening, J.W.5
  • 48
    • 84872819538 scopus 로고    scopus 로고
    • Construction of improved tools for protein localization studies in Streptococcus pneumoniae
    • Henriques MX, Catalão MJ, Figueiredo J, Gomes JP, Filipe SR. 2013. Construction of improved tools for protein localization studies in Streptococcus pneumoniae. PLoS One 8: e55049. http://dx. doi. org/10. 1371/journal. pone. 0055049.
    • (2013) PLoS One , vol.8
    • Henriques, M.X.1    Catalão, M.J.2    Figueiredo, J.3    Gomes, J.P.4    Filipe, S.R.5
  • 49
    • 78049378075 scopus 로고    scopus 로고
    • An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates
    • Molle V, Leiba J, Zanella-Cléon I, Becchi M, Kremer L. 2010. An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates. Proteomics 10: 3910-3915. http://dx. doi. org/10. 1002/pmic. 201000316.
    • (2010) Proteomics , vol.10 , pp. 3910-3915
    • Molle, V.1    Leiba, J.2    Zanella-Cléon, I.3    Becchi, M.4    Kremer, L.5
  • 50
    • 73649133664 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae
    • Sun X, Ge F, Xiao CL, Yin XF, Ge R, Zhang LH, He QY. 2010. Phosphoproteomic analysis reveals the multiple roles of phosphorylation in pathogenic bacterium Streptococcus pneumoniae. J Proteome Res 9: 275-282. http://dx. doi. org/10. 1021/pr900612v.
    • (2010) J Proteome Res , vol.9 , pp. 275-282
    • Sun, X.1    Ge, F.2    Xiao, C.L.3    Yin, X.F.4    Ge, R.5    Zhang, L.H.6    He, Q.Y.7
  • 51
    • 79960708973 scopus 로고    scopus 로고
    • SMC is recruited to oriC by ParB and promotes chromosome segregation in Strep-tococcus pneumoniae
    • Minnen A, Attaiech L, Thon M, Gruber S, Veening JW. 2011. SMC is recruited to oriC by ParB and promotes chromosome segregation in Strep-tococcus pneumoniae. Mol Microbiol 81: 676-688. http://dx. doi. org/10. 1111/j. 1365-2958. 2011. 07722. x.
    • (2011) Mol Microbiol , vol.81 , pp. 676-688
    • Minnen, A.1    Attaiech, L.2    Thon, M.3    Gruber, S.4    Veening, J.W.5
  • 52
    • 0025052434 scopus 로고
    • Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D, Dcarboxypeptidase penicillin-binding protein 3
    • Schuster C, Dobrinski B, Hakenbeck R. 1990. Unusual septum formation in Streptococcus pneumoniae mutants with an alteration in the D, Dcarboxypeptidase penicillin-binding protein 3. J Bacteriol 172: 6499-6505.
    • (1990) J Bacteriol , vol.172 , pp. 6499-6505
    • Schuster, C.1    Dobrinski, B.2    Hakenbeck, R.3
  • 53
    • 79955543481 scopus 로고    scopus 로고
    • Characterization of mutants deficient in the L, D-carboxypeptidase (DacB) and WalRK (VicRK) regulon, 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) regulon, involved in peptidoglycan maturation of Streptococcus pneumoniae serotype 2 strain D39. J Bacteriol 193: 2290-2300. http://dx. doi. org/10. 1128/JB. 01555-10.
    • (2011) J Bacteriol , vol.193 , pp. 2290-2300
    • Barendt, S.M.1    Sham, L.T.2    Winkler, M.E.3
  • 55
    • 78650917468 scopus 로고    scopus 로고
    • Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces
    • Willemse J, Borst JW, de Wall WE, Bisseling T, van Wezel GP. 2011. Positive control of cell division: FtsZ is recruited by SsgB during sporulation of Streptomyces. Genes Dev 25: 89-99. http://dx. doi. org/10. 1101/gad. 600211.
    • (2011) Genes Dev , vol.25 , pp. 89-99
    • Willemse, J.1    Borst, J.W.2    de Wall, W.E.3    Bisseling, T.4    van Wezel, G.P.5
  • 56
    • 39249085850 scopus 로고    scopus 로고
    • MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ
    • Dajkovic A, Lan G, Sun SX, Wirtz D, Lutkenhaus J. 2008. MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ. Curr Biol 18: 235-244. http://dx. doi. org/10. 1016/j. cub. 2008. 01. 042.
    • (2008) Curr Biol , vol.18 , pp. 235-244
    • Dajkovic, A.1    Lan, G.2    Sun, S.X.3    Wirtz, D.4    Lutkenhaus, J.5
  • 57
    • 0032213104 scopus 로고    scopus 로고
    • Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
    • Marston AL, Thomaides HB, Edwards DH, Sharpe ME, Errington J. 1998. Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. Genes Dev 12: 3419-3430. http://dx. doi. org/10. 1101/gad. 12. 21. 3419.
    • (1998) Genes Dev , vol.12 , pp. 3419-3430
    • Marston, A.L.1    Thomaides, H.B.2    Edwards, D.H.3    Sharpe, M.E.4    Errington, J.5
  • 59
    • 84856585868 scopus 로고    scopus 로고
    • Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae
    • Fleurie A, Cluzel C, Guiral S, Freton C, Galisson F, Zanella-Cleon I, Di Guilmi AM, Grangeasse C. 2012. Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae. Mol Microbiol 83: 746-758. http://dx. doi. org/10. 1111/j. 1365-2958. 2011. 07962. x.
    • (2012) Mol Microbiol , vol.83 , pp. 746-758
    • Fleurie, A.1    Cluzel, C.2    Guiral, S.3    Freton, C.4    Galisson, F.5    Zanella-Cleon, I.6    Di Guilmi, A.M.7    Grangeasse, C.8
  • 60
    • 39149098134 scopus 로고    scopus 로고
    • The different shapes of cocci
    • Zapun A, Vernet T, Pinho MG. 2008. The different shapes of cocci. FEMS Microbiol Rev 32: 345-360. http://dx. doi. org/10. 1111/j. 1574-6976. 2007. 00098. x.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 345-360
    • Zapun, A.1    Vernet, T.2    Pinho, M.G.3
  • 61
    • 0000331730 scopus 로고
    • A study of the genetic material determining an enzyme in Pneumococcus
    • Lacks S, Hotchkiss RD. 1960. A study of the genetic material determining an enzyme in Pneumococcus. Biochim Biophys Acta 39: 508-518. http://dx. doi. org/10. 1016/0006-3002(60)90205-5.
    • (1960) Biochim Biophys Acta , vol.39 , pp. 508-518
    • Lacks, S.1    Hotchkiss, R.D.2
  • 62
    • 16544367143 scopus 로고    scopus 로고
    • Extracellular-peptide control of competence for genetic transformation in Streptococcus pneumoniae
    • Claverys JP, Havarstein LS. 2002. Extracellular-peptide control of competence for genetic transformation in Streptococcus pneumoniae. Front Biosci 7: d1798-d1814. http://dx. doi. org/10. 2741/claverys.
    • (2002) Front Biosci , vol.7 , pp. d1798-d1814
    • Claverys, J.P.1    Havarstein, L.S.2
  • 63
    • 0013666301 scopus 로고
    • Electron microscopical studies of phage multiplication. IV. The establishment of the DNA pool of vegetative phage and the maturation of phage particles
    • Kellenberger E, Sechaud J, Ryter A. 1959. Electron microscopical studies of phage multiplication. IV. The establishment of the DNA pool of vegetative phage and the maturation of phage particles. Virology 8: 478-498. http://dx. doi. org/10. 1016/0042-6822(59)90050-9.
    • (1959) Virology , vol.8 , pp. 478-498
    • Kellenberger, E.1    Sechaud, J.2    Ryter, A.3
  • 64
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electronopaque stain in electron microscopy
    • Reynolds ES. 1963. The use of lead citrate at high pH as an electronopaque stain in electron microscopy. J Cell Biol 17: 208-212. http://dx. doi. org/10. 1083/jcb. 17. 1. 208.
    • (1963) J Cell Biol , vol.17 , pp. 208-212
    • Reynolds, E.S.1

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.