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Volumn 92, Issue 4, 2014, Pages 733-755

Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PENICILLIN BINDING PROTEIN 2X; ZINC; PBP 2X PROTEIN, STREPTOCOCCUS; PENICILLIN BINDING PROTEIN; SIGNAL PEPTIDE;

EID: 84899896995     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12588     Document Type: Article
Times cited : (48)

References (83)
  • 1
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: assembly, maintenance and disassembly of the Z ring
    • Adams, D.W., and Errington, J. (2009) Bacterial cell division: assembly, maintenance and disassembly of the Z ring. Nat Rev Microbiol 7: 642-653.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 2
    • 0029787421 scopus 로고    scopus 로고
    • Competence pheromone, oligopeptide permease, and induction of competence in Streptococcus pneumoniae
    • Alloing, G., Granadel, C., Morrison, D.A., and Claverys, J.-P. (1996) Competence pheromone, oligopeptide permease, and induction of competence in Streptococcus pneumoniae. Mol Microbiol 21: 471-478.
    • (1996) Mol Microbiol , vol.21 , pp. 471-478
    • Alloing, G.1    Granadel, C.2    Morrison, D.A.3    Claverys, J.-P.4
  • 3
    • 84983711696 scopus 로고
    • Studies on the chemical nature of the substance inducing transformation of pneumococcal types. Induction of transformation by a desoxyribonucleic acid fraction isolated from pneumococcus type III
    • Avery, O.T., MacLeod, C.M., and McCarty, M. (1944) Studies on the chemical nature of the substance inducing transformation of pneumococcal types. Induction of transformation by a desoxyribonucleic acid fraction isolated from pneumococcus type III. J Exp Med 79: 137-158.
    • (1944) J Exp Med , vol.79 , pp. 137-158
    • Avery, O.T.1    MacLeod, C.M.2    McCarty, M.3
  • 4
    • 65549117531 scopus 로고    scopus 로고
    • Influences of capsule on cell shape and chain formation of wild-type and pcsB mutants of serotype 2 Streptococcus pneumoniae
    • Barendt, S.M., Land, A.D., Sham, L.T., Ng, W.L., Tsui, H.C., Arnold, R.J., and Winkler, M.E. (2009) Influences of capsule on cell shape and chain formation of wild-type and pcsB mutants of serotype 2 Streptococcus pneumoniae. J Bacteriol 191: 3024-3040.
    • (2009) J Bacteriol , vol.191 , pp. 3024-3040
    • Barendt, S.M.1    Land, A.D.2    Sham, L.T.3    Ng, W.L.4    Tsui, H.C.5    Arnold, R.J.6    Winkler, M.E.7
  • 5
    • 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, S.M., Sham, L.T., and Winkler, M.E. (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.
    • (2011) J Bacteriol , vol.193 , pp. 2290-2300
    • Barendt, S.M.1    Sham, L.T.2    Winkler, M.E.3
  • 6
    • 84859576482 scopus 로고    scopus 로고
    • Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP
    • Beilharz, K., Novakova, L., Fadda, D., Branny, P., Massidda, O., and Veening, J.W. (2012) Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP. Proc Natl Acad Sci USA 109: E905-E913.
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Beilharz, K.1    Novakova, L.2    Fadda, D.3    Branny, P.4    Massidda, O.5    Veening, J.W.6
  • 7
    • 84884580019 scopus 로고    scopus 로고
    • The effect of low Pbp2b levels on cell morphology and peptidoglycan composition in Streptococcus pneumoniae R6
    • Berg, K.H., Stamsas, G.A., Straume, D., and Havarstein, L.S. (2013) The effect of low Pbp2b levels on cell morphology and peptidoglycan composition in Streptococcus pneumoniae R6. J Bacteriol 195: 4342-4354.
    • (2013) J Bacteriol , vol.195 , pp. 4342-4354
    • Berg, K.H.1    Stamsas, G.A.2    Straume, D.3    Havarstein, L.S.4
  • 8
    • 84869073827 scopus 로고    scopus 로고
    • The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide
    • Cassone, M., Gagne, A.L., Spruce, L.A., Seeholzer, S.H., and Sebert, M.E. (2012) The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide. J Biol Chem 287: 38449-38459.
    • (2012) J Biol Chem , vol.287 , pp. 38449-38459
    • Cassone, M.1    Gagne, A.L.2    Spruce, L.A.3    Seeholzer, S.H.4    Sebert, M.E.5
  • 9
    • 79951967246 scopus 로고    scopus 로고
    • HTRA proteases: regulated proteolysis in protein quality control
    • Clausen, T., Kaiser, M., Huber, R., and Ehrmann, M. (2011) HTRA proteases: regulated proteolysis in protein quality control. Nat Rev Mol Cell Biol 12: 152-162.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 152-162
    • Clausen, T.1    Kaiser, M.2    Huber, R.3    Ehrmann, M.4
  • 10
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell
    • Daniel, R.A., and Errington, J. (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 13: 767-776.
    • (2003) Cell , vol.13 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 11
    • 0037244586 scopus 로고    scopus 로고
    • Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole
    • Den Blaauwen, T., Aarsman, M.E., Vischer, N.O., and Nanninga, N. (2003) Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially in the lateral wall and at mid-cell in comparison with the old cell pole. Mol Microbiol 47: 539-547.
    • (2003) Mol Microbiol , vol.47 , pp. 539-547
    • Den Blaauwen, T.1    Aarsman, M.E.2    Vischer, N.O.3    Nanninga, N.4
  • 13
    • 70349920678 scopus 로고    scopus 로고
    • Cellular localization of choline-utilization proteins in Streptococcus pneumoniae using novel fluorescent reporter systems
    • Eberhardt, A., Wu, L.J., Errington, J., Vollmer, W., and Veening, J.W. (2009) Cellular localization of choline-utilization proteins in Streptococcus pneumoniae using novel fluorescent reporter systems. Mol Microbiol 74: 395-408.
    • (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
  • 14
    • 84872856522 scopus 로고    scopus 로고
    • The physiology of bacterial cell division
    • Egan, A.J., and Vollmer, W. (2013) The physiology of bacterial cell division. Ann N Y Acad Sci 1277: 8-28.
    • (2013) Ann N Y Acad Sci , vol.1277 , pp. 8-28
    • Egan, A.J.1    Vollmer, W.2
  • 15
    • 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., etal. (2012) Mutational dissection of the S/T-kinase StkP reveals crucial roles in cell division of Streptococcus pneumoniae. Mol Microbiol 83: 746-758.
    • (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
  • 16
    • 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, K.E., Gelbmann, D., Senn, B.M., and 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
  • 17
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs
    • 1079-1071
    • Goffin, C., and Ghuysen, J.-M. (1998) Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol Mol Biol Rev 62: 1079-1.
    • (1998) Microbiol Mol Biol Rev , vol.62
    • Goffin, C.1    Ghuysen, J.-M.2
  • 18
    • 0034595512 scopus 로고    scopus 로고
    • The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance
    • Gordon, E., Mouz, N., Duee, E., and Dideberg, O. (2000) The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. J Mol Biol 299: 477-485.
    • (2000) J Mol Biol , vol.299 , pp. 477-485
    • Gordon, E.1    Mouz, N.2    Duee, E.3    Dideberg, O.4
  • 19
    • 0023093968 scopus 로고
    • Interaction of non-lytic β-lactams with penicillin-binding proteins in Streptococcus pneumoniae
    • Hakenbeck, R., Tornette, S., and Adkinson, N.F. (1987) Interaction of non-lytic β-lactams with penicillin-binding proteins in Streptococcus pneumoniae. J Gen Microbiol 133: 755-760.
    • (1987) J Gen Microbiol , vol.133 , pp. 755-760
    • Hakenbeck, R.1    Tornette, S.2    Adkinson, N.F.3
  • 20
    • 0025766776 scopus 로고
    • Variability of penicillin-binding proteins from penicillin-sensitive Streptococcus pneumoniae
    • Hakenbeck, R., Briese, T., Chalkley, L., Ellerbrok, H., Kalliokoski, R., Latorre, C., etal. (1991) Variability of penicillin-binding proteins from penicillin-sensitive Streptococcus pneumoniae. J Infect Dis 164: 307-312.
    • (1991) J Infect Dis , vol.164 , pp. 307-312
    • Hakenbeck, R.1    Briese, T.2    Chalkley, L.3    Ellerbrok, H.4    Kalliokoski, R.5    Latorre, C.6
  • 22
    • 84858024596 scopus 로고    scopus 로고
    • Molecular mechanism of beta-lactam resistance in Streptococcus pneumoniae
    • Hakenbeck, R., Brückner, R., Denapaite, D., and Maurer, P. (2012) Molecular mechanism of beta-lactam resistance in Streptococcus pneumoniae. Future Microbiol 7: 395-410.
    • (2012) Future Microbiol , vol.7 , pp. 395-410
    • Hakenbeck, R.1    Brückner, R.2    Denapaite, D.3    Maurer, P.4
  • 23
    • 33846966329 scopus 로고    scopus 로고
    • A new integrative reporter plasmid for Streptococcus pneumoniae
    • Halfmann, A., Hakenbeck, R., and Brückner, R. (2007a) A new integrative reporter plasmid for Streptococcus pneumoniae. FEMS Microbiol Lett 268: 217-224.
    • (2007) FEMS Microbiol Lett , vol.268 , pp. 217-224
    • Halfmann, A.1    Hakenbeck, R.2    Brückner, R.3
  • 24
    • 34548700626 scopus 로고    scopus 로고
    • Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: five out of fifteen promoters drive expression of small noncoding RNAs
    • Halfmann, A., Kovács, M., Hakenbeck, R., and Brückner, R. (2007b) Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: five out of fifteen promoters drive expression of small noncoding 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
  • 26
    • 33748766086 scopus 로고    scopus 로고
    • An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II
    • Hasper, H.E., Kramer, N.E., Smith, J.L., Hillman, J.D., Zachariah, C., Kuipers, O.P., etal. (2006) An alternative bactericidal mechanism of action for lantibiotic peptides that target lipid II. Science 313: 1636-1637.
    • (2006) Science , vol.313 , pp. 1636-1637
    • Hasper, H.E.1    Kramer, N.E.2    Smith, J.L.3    Hillman, J.D.4    Zachariah, C.5    Kuipers, O.P.6
  • 27
    • 0014733740 scopus 로고
    • Model for cell wall growth of Streptococcus faecalis
    • Higgins, M.L., and Shockman, G.D. (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
  • 28
    • 0032716126 scopus 로고    scopus 로고
    • Gene disruption studies of penicillin-binding proteins 1a, 1b and 2a in Streptococcus pneumoniae
    • Hoskins, J., Matsushima, P., Mullen, D.L., Tang, J., Zhao, G., Meier, T., I, etal. (1999) Gene disruption studies of penicillin-binding proteins 1a, 1b and 2a in Streptococcus pneumoniae. J Bacteriol 181: 6552-6555.
    • (1999) J Bacteriol , vol.181 , pp. 6552-6555
    • Hoskins, J.1    Matsushima, P.2    Mullen, D.L.3    Tang, J.4    Zhao, G.5    Meier, I.T.6
  • 29
    • 0035788801 scopus 로고    scopus 로고
    • A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress
    • Hyyrylainen, H.L., Bolhuis, A., Darmon, E., Muukkonen, L., Koski, P., Vitikainen, M., etal. (2001) A novel two-component regulatory system in Bacillus subtilis for the survival of severe secretion stress. Mol Microbiol 41: 1159-1172.
    • (2001) Mol Microbiol , vol.41 , pp. 1159-1172
    • Hyyrylainen, H.L.1    Bolhuis, A.2    Darmon, E.3    Muukkonen, L.4    Koski, P.5    Vitikainen, M.6
  • 30
    • 80355131554 scopus 로고    scopus 로고
    • Live Cell imaging of Bacillus subtilis and Streptococcus pneumoniae using automated time-lapse microscopy
    • de Jong, I.G., Beilharz, K., Kuipers, O.P., and Veening, J.W. (2011) Live Cell imaging of Bacillus subtilis and Streptococcus pneumoniae using automated time-lapse microscopy. J Vis Exp 53: e3145.
    • (2011) J Vis Exp , vol.53
    • de Jong, I.G.1    Beilharz, K.2    Kuipers, O.P.3    Veening, J.W.4
  • 31
    • 0027446117 scopus 로고
    • Deletion analysis of the essentiality of penicillin-binding proteins 1A, 2B and 2X of Streptococcus pneumoniae
    • Kell, C.M., Sharma, U.K., Dowson, C.G., Town, C., Balganesh, T.S., and Spratt, B.G. (1993) Deletion analysis of the essentiality of penicillin-binding proteins 1A, 2B and 2X of Streptococcus pneumoniae. FEMS Microbiol Lett 106: 171-175.
    • (1993) FEMS Microbiol Lett , vol.106 , pp. 171-175
    • Kell, C.M.1    Sharma, U.K.2    Dowson, C.G.3    Town, C.4    Balganesh, T.S.5    Spratt, B.G.6
  • 32
    • 84875521516 scopus 로고    scopus 로고
    • The HtrA protease of Streptococcus pneumoniae controls density-dependent stimulation of the bacteriocin blp locus via disruption of pheromone secretion
    • Kochan, T.J., and Dawid, S. (2013) The HtrA protease of Streptococcus pneumoniae controls density-dependent stimulation of the bacteriocin blp locus via disruption of pheromone secretion. J Bacteriol 195: 1561-1572.
    • (2013) J Bacteriol , vol.195 , pp. 1561-1572
    • Kochan, T.J.1    Dawid, S.2
  • 33
    • 0000331730 scopus 로고
    • A study of the genetic material determining an enzyme activity in pneumococcus
    • Lacks, S., and Hotchkiss, R.D. (1960) A study of the genetic material determining an enzyme activity in pneumococcus. Biochim Biophys Acta 39: 508-517.
    • (1960) Biochim Biophys Acta , vol.39 , pp. 508-517
    • Lacks, S.1    Hotchkiss, R.D.2
  • 34
    • 84888881225 scopus 로고    scopus 로고
    • The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability
    • Lages, M.C.A., Beilharz, K., Angeles, D.M., Veening, J.-W., and Scheffers, D.-J. (2013) The localization of key Bacillus subtilis penicillin binding proteins during cell growth is determined by substrate availability. Environ Microbiol 15: 3272-3281.
    • (2013) Environ Microbiol , vol.15 , pp. 3272-3281
    • Lages, M.C.A.1    Beilharz, K.2    Angeles, D.M.3    Veening, J.-W.4    Scheffers, D.-J.5
  • 35
    • 0023444805 scopus 로고
    • Penicillin-binding proteins in β-lactam-resistant laboratory mutants of Streptococcus pneumoniae
    • Laible, G., and Hakenbeck, R. (1987) Penicillin-binding proteins in β-lactam-resistant laboratory mutants of Streptococcus pneumoniae. Mol Microbiol 1: 355-363.
    • (1987) Mol Microbiol , vol.1 , pp. 355-363
    • Laible, G.1    Hakenbeck, R.2
  • 36
    • 0024374096 scopus 로고
    • Nucleotide sequences of the pbpX genes encoding the penicillin-binding protein 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506
    • Laible, G., Hakenbeck, R., Sicard, M.A., Joris, B., and Ghuysen, J.-M. (1989) Nucleotide sequences of the pbpX genes encoding the penicillin-binding protein 2x from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Mol Microbiol 3: 1337-1348.
    • (1989) Mol Microbiol , vol.3 , pp. 1337-1348
    • Laible, G.1    Hakenbeck, R.2    Sicard, M.A.3    Joris, B.4    Ghuysen, J.-M.5
  • 37
    • 79961133524 scopus 로고    scopus 로고
    • The requirement for pneumococcal MreC and MreD is relieved by inactivation of the gene encoding PBP1a
    • Land, A.D., and Winkler, M.E. (2011) The requirement for pneumococcal MreC and MreD is relieved by inactivation of the gene encoding PBP1a. J Bacteriol 193: 4166-4179.
    • (2011) J Bacteriol , vol.193 , pp. 4166-4179
    • Land, A.D.1    Winkler, M.E.2
  • 38
    • 84888315230 scopus 로고    scopus 로고
    • Requirement of essential Pbp2x and GpsB for septal ring closure in Streptococcus pneumoniae D39
    • Land, A.D., Tsui, H.C., Kocaoglu, O., Vella, S.A., Shaw, S.L., Keen, S.K., etal. (2013) Requirement of essential Pbp2x and GpsB for septal ring closure in Streptococcus pneumoniae D39. Mol Microbiol 90: 939-955.
    • (2013) Mol Microbiol , vol.90 , pp. 939-955
    • Land, A.D.1    Tsui, H.C.2    Kocaoglu, O.3    Vella, S.A.4    Shaw, S.L.5    Keen, S.K.6
  • 39
    • 64349091158 scopus 로고    scopus 로고
    • Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6
    • Lanie, J.A., Ng, W.L., Kazmierczak, K.M., Andrzejewski, T.M., Davidsen, T.M., Wayne, K.J., etal. (2007) Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus pneumoniae and comparison with that of unencapsulated laboratory strain R6. J Bacteriol 297: 503-512.
    • (2007) J Bacteriol , vol.297 , pp. 503-512
    • Lanie, J.A.1    Ng, W.L.2    Kazmierczak, K.M.3    Andrzejewski, T.M.4    Davidsen, T.M.5    Wayne, K.J.6
  • 40
    • 0025886123 scopus 로고
    • Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis
    • LeBlanc, D.J., Lee, L.N., and Inamine, J.M. (1991) Cloning and nucleotide base sequence analysis of a spectinomycin adenyltransferase AAD(9) determinant from Enterococcus faecalis. Antimicrob Agents Chemother 35: 1804-1810.
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 1804-1810
    • LeBlanc, D.J.1    Lee, L.N.2    Inamine, J.M.3
  • 41
    • 0025299083 scopus 로고
    • Bacterial cell shape regulation: testing of additional predictions unique to the two-competing-sites model for peptidoglycan assembly and isolation of conditional rod-shaped mutants from some wild-type cocci
    • Lleo, M.M., Canepari, P., and Satta, G. (1990) Bacterial cell shape regulation: testing of additional predictions unique to the two-competing-sites model for peptidoglycan assembly and isolation of conditional rod-shaped mutants from some wild-type cocci. J Bacteriol 172: 3758-3771.
    • (1990) J Bacteriol , vol.172 , pp. 3758-3771
    • Lleo, M.M.1    Canepari, P.2    Satta, G.3
  • 42
    • 84861892432 scopus 로고    scopus 로고
    • Structural perspective of peptidoglycan biosynthesis and assembly
    • Lovering, A.L., Safadi, S.S., and Strynadka, N.C. (2012) Structural perspective of peptidoglycan biosynthesis and assembly. Annu Rev Biochem 81: 451-478.
    • (2012) Annu Rev Biochem , vol.81 , pp. 451-478
    • Lovering, A.L.1    Safadi, S.S.2    Strynadka, N.C.3
  • 43
    • 84867995401 scopus 로고    scopus 로고
    • Bacterial cytokinesis: from Z ring to divisome
    • Lutkenhaus, J., Pichoff, S., and Du, S. (2012) Bacterial cytokinesis: from Z ring to divisome. Cytoskeleton 69: 778-790.
    • (2012) Cytoskeleton , vol.69 , pp. 778-790
    • Lutkenhaus, J.1    Pichoff, S.2    Du, S.3
  • 44
    • 78651376345 scopus 로고    scopus 로고
    • Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae
    • Maestro, B., Novaková, L., Hesek, D., Lee, M., Leyva, E., Mobashery, S., etal. (2011) Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae. FEBS Lett 585: 357-363.
    • (2011) FEBS Lett , vol.585 , pp. 357-363
    • Maestro, B.1    Novaková, L.2    Hesek, D.3    Lee, M.4    Leyva, E.5    Mobashery, S.6
  • 45
    • 33644785222 scopus 로고    scopus 로고
    • The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and mutations in pbp2x involved in beta-lactam resistance
    • Mascher, T., Heintz, M., Zähner, D., Merai, M., and Hakenbeck, R. (2006) The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and 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
    • 0037214390 scopus 로고    scopus 로고
    • The Streptococcus pneumoniae cia regulon: CiaR target sites and transcription profile analysis
    • Mascher, T., Zähner, D., Merai, M., Balmelle, N., de Saizieu, A.B., and Hakenbeck, R. (2003) The Streptococcus pneumoniae cia regulon: CiaR target sites and transcription profile analysis. J Bacteriol 185: 60-70.
    • (2003) J Bacteriol , vol.185 , pp. 60-70
    • Mascher, T.1    Zähner, D.2    Merai, M.3    Balmelle, N.4    de Saizieu, A.B.5    Hakenbeck, R.6
  • 47
    • 84888857354 scopus 로고    scopus 로고
    • From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division?
    • Massidda, O., Novakova, L., and Vollmer, W. (2013) From models to pathogens: how much have we learned about Streptococcus pneumoniae cell division? Environ Microbiol 15: 3133-3157.
    • (2013) Environ Microbiol , vol.15 , pp. 3133-3157
    • Massidda, O.1    Novakova, L.2    Vollmer, W.3
  • 48
    • 39149111919 scopus 로고    scopus 로고
    • Penicillin-binding protein 2x of Streptococcus pneumoniae: three new mutational pathways for remodelling an essential enzyme into a resistance determinant
    • Maurer, P., Koch, B., Zerfaß, I., Krauß, J., van der Linden, M., Frère, J.-M., etal. (2008) Penicillin-binding protein 2x of Streptococcus pneumoniae: three new mutational pathways for remodelling an essential enzyme into a resistance determinant. J Mol Biol 376: 1403-1416.
    • (2008) J Mol Biol , vol.376 , pp. 1403-1416
    • Maurer, P.1    Koch, B.2    Zerfaß, I.3    Krauß, J.4    van der Linden, M.5    Frère, J.-M.6
  • 49
    • 84862002474 scopus 로고    scopus 로고
    • The C-terminal PASTA-domains of Streptococcus pneumoniae PBP2x are important for beta-lactam binding
    • Maurer, P., Todorova, K., Sauerbier, J., and Hakenbeck, R. (2012) The C-terminal PASTA-domains of Streptococcus pneumoniae PBP2x are important for beta-lactam binding. Microb Drug Resist 18: 314-321.
    • (2012) Microb Drug Resist , vol.18 , pp. 314-321
    • Maurer, P.1    Todorova, K.2    Sauerbier, J.3    Hakenbeck, R.4
  • 50
    • 79960964670 scopus 로고    scopus 로고
    • The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization
    • Mir, M., Asong, J., Li, X., Cardot, J., Boons, G.J., and Husson, R.N. (2011) The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization. PLoS Pathog 7: e1002182.
    • (2011) PLoS Pathog , vol.7
    • Mir, M.1    Asong, J.2    Li, X.3    Cardot, J.4    Boons, G.J.5    Husson, R.N.6
  • 51
    • 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., and 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
  • 52
    • 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., and Vernet, T. (2004) The D, D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae. Mol Microbiol 51: 1641-1648.
    • (2004) Mol Microbiol , vol.51 , pp. 1641-1648
    • Morlot, C.1    Noirclerc-Savoye, M.2    Zapun, A.3    Dideberg, O.4    Vernet, T.5
  • 53
    • 84884703178 scopus 로고    scopus 로고
    • Interaction of penicillin-binding protein 2x and Ser/Thr protein kinase StkP, two key players in Streptococcus pneumoniae R6 morphogenesis
    • Morlot, C., Bayle, L., Jacq, M., Fleurie, A., Tourcier, G., Galisson, F., etal. (2013) Interaction of penicillin-binding protein 2x and Ser/Thr protein kinase StkP, two key players in Streptococcus pneumoniae R6 morphogenesis. Mol Microbiol 90: 88-102.
    • (2013) Mol Microbiol , vol.90 , pp. 88-102
    • Morlot, C.1    Bayle, L.2    Jacq, M.3    Fleurie, A.4    Tourcier, G.5    Galisson, F.6
  • 54
    • 84860324496 scopus 로고    scopus 로고
    • Signal perception by the secretion stress-responsive CssRS two-component system in Bacillus subtilis
    • Noone, D., Botella, E., Butler, C., Hansen, A., Jende, I., and Devine, K.M. (2012) Signal perception by the secretion stress-responsive CssRS two-component system in Bacillus subtilis. J Bacteriol 194: 1800-1814.
    • (2012) J Bacteriol , vol.194 , pp. 1800-1814
    • Noone, D.1    Botella, E.2    Butler, C.3    Hansen, A.4    Jende, I.5    Devine, K.M.6
  • 55
    • 0000612766 scopus 로고
    • Release of genetic transforming agent from pneumococcal cultures during growth and disintegration
    • Ottolenghi, E., and Hotchkiss, R.D. (1962) Release of genetic transforming agent from pneumococcal cultures during growth and disintegration. J Exp Med 116: 491-519.
    • (1962) J Exp Med , vol.116 , pp. 491-519
    • Ottolenghi, E.1    Hotchkiss, R.D.2
  • 56
    • 0033014014 scopus 로고    scopus 로고
    • Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins
    • Paik, J., Kern, I., Lurz, R., and Hakenbeck, R. (1999) Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins. J Bacteriol 181: 3852-3856.
    • (1999) J Bacteriol , vol.181 , pp. 3852-3856
    • Paik, J.1    Kern, I.2    Lurz, R.3    Hakenbeck, R.4
  • 57
    • 78649529310 scopus 로고    scopus 로고
    • The extended conformation of the 2.9-A crystal structure of the three-PASTA domain of a Ser/Thr kinase from the human pathogen Staphylococcus aureus
    • Paracuellos, P., Ballandras, A., Robert, X., Kahn, R., Herve, M., Mengin-Lecreulx, D., etal. (2010) The extended conformation of the 2.9-A crystal structure of the three-PASTA domain of a Ser/Thr kinase from the human pathogen Staphylococcus aureus. J Mol Biol 404: 847-858.
    • (2010) J Mol Biol , vol.404 , pp. 847-858
    • Paracuellos, P.1    Ballandras, A.2    Robert, X.3    Kahn, R.4    Herve, M.5    Mengin-Lecreulx, D.6
  • 58
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • Pares, S., Mouz, N., Pétillot, Y., Hakenbeck, R., and Dideberg, O. (1996) X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat Struct Biol 3: 284-289.
    • (1996) Nat Struct Biol , vol.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Pétillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 59
    • 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
    • Perez-Nunez, D., Briandet, R., David, B., Gautier, C., Renault, P., Hallet, B., etal. (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
    • Perez-Nunez, D.1    Briandet, R.2    David, B.3    Gautier, C.4    Renault, P.5    Hallet, B.6
  • 60
    • 0026481149 scopus 로고
    • The high level streptomycin resistance gene from Streptococcus pneumoniae is a homologue of the ribosomal protein S12 gene from Escherichia coli
    • Salles, C., Creancier, L., Claverys, J.P., and Méjean, V. (1992) The high level streptomycin resistance gene from Streptococcus pneumoniae is a homologue of the ribosomal protein S12 gene from Escherichia coli. Nucleic Acids Res 20: 6103.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6103
    • Salles, C.1    Creancier, L.2    Claverys, J.P.3    Méjean, V.4
  • 62
    • 84880134951 scopus 로고    scopus 로고
    • Target evaluation of the non-coding csRNAs reveals a link of the two-component regulatory system CiaRH to competence control in Streptococcus pneumoniae R6
    • Schnorpfeil, A., Kranz, M., Kovacs, M., Kirsch, C., Gartmann, J., Brunner, I., etal. (2013) Target evaluation of the non-coding csRNAs reveals a link of the two-component regulatory system CiaRH to competence control in Streptococcus pneumoniae R6. Mol Microbiol 89: 334-349.
    • (2013) Mol Microbiol , vol.89 , pp. 334-349
    • Schnorpfeil, A.1    Kranz, M.2    Kovacs, M.3    Kirsch, C.4    Gartmann, J.5    Brunner, I.6
  • 63
    • 0011734167 scopus 로고    scopus 로고
    • Quantitative analysis of gene expression with an improved green fluorescent protein
    • Scholz, O., Thiel, A., Hillen, W., and Niederweis, M. (2000) Quantitative analysis of gene expression with an improved green fluorescent protein. Eur J Biochem 267: 1565-1570.
    • (2000) Eur J Biochem , vol.267 , pp. 1565-1570
    • Scholz, O.1    Thiel, A.2    Hillen, W.3    Niederweis, M.4
  • 64
    • 0026651908 scopus 로고
    • Altered murein composition in a DD-carboxypeptidase mutant of Streptococcus pneumoniae
    • Severin, A., Schuster, C., Hakenbeck, R., and Tomasz, A. (1992) Altered murein composition in a DD-carboxypeptidase mutant of Streptococcus pneumoniae. J Bacteriol 174: 5125-5155.
    • (1992) J Bacteriol , vol.174 , pp. 5125-5155
    • Severin, A.1    Schuster, C.2    Hakenbeck, R.3    Tomasz, A.4
  • 65
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah, I.M., Laaberki, M.H., Popham, D.L., and Dworkin, J. (2008) A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135: 486-496.
    • (2008) Cell , vol.135 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 66
    • 84861805227 scopus 로고    scopus 로고
    • Recent advances in pneumococcal peptidoglycan biosynthesis suggest new vaccine and antimicrobial targets
    • Sham, L.T., Tsui, H.C., Land, A.D., Barendt, S.M., and Winkler, M.E. (2012) Recent advances in pneumococcal peptidoglycan biosynthesis suggest new vaccine and antimicrobial targets. Curr Opin Microbiol 15: 194-203.
    • (2012) Curr Opin Microbiol , vol.15 , pp. 194-203
    • Sham, L.T.1    Tsui, H.C.2    Land, A.D.3    Barendt, S.M.4    Winkler, M.E.5
  • 67
    • 0018408260 scopus 로고
    • A plasmid in Streptococcus pneumoniae
    • Smith, M.D., and Guild, W.R. (1979) A plasmid in Streptococcus pneumoniae. J Bacteriol 137: 735-739.
    • (1979) J Bacteriol , vol.137 , pp. 735-739
    • Smith, M.D.1    Guild, W.R.2
  • 68
    • 84555178075 scopus 로고    scopus 로고
    • Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy
    • Squeglia, F., Marchetti, R., Ruggiero, A., Lanzetta, R., Marasco, D., Dworkin, J., etal. (2011) Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy. J Am Chem Soc 133: 20676-20679.
    • (2011) J Am Chem Soc , vol.133 , pp. 20676-20679
    • Squeglia, F.1    Marchetti, R.2    Ruggiero, A.3    Lanzetta, R.4    Marasco, D.5    Dworkin, J.6
  • 69
    • 84455174351 scopus 로고    scopus 로고
    • Physics of bacterial morphogenesis
    • Sun, S.X., and Jiang, H. (2011) Physics of bacterial morphogenesis. Microbiol Mol Biol Rev 75: 543-565.
    • (2011) Microbiol Mol Biol Rev , vol.75 , pp. 543-565
    • Sun, S.X.1    Jiang, H.2
  • 70
    • 0035512266 scopus 로고    scopus 로고
    • An rpsL cassette, janus, for gene replacement through negative selection in Streptococcus pneumoniae
    • Sung, C.K., Li, H., Claverys, J.P., and Morrison, D.A. (2001) An rpsL cassette, janus, for gene replacement through negative selection in Streptococcus pneumoniae. 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
  • 71
    • 77957262782 scopus 로고    scopus 로고
    • Synchronization of chromosome dynamics and cell division in bacteria
    • Thanbichler, M. (2010) Synchronization of chromosome dynamics and cell division in bacteria. Cold Spring Harb Perspect Biol 2: a000331.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Thanbichler, M.1
  • 72
    • 80455158425 scopus 로고    scopus 로고
    • Dynamic distribution of the SecA and SecY translocase subunits and septal localization of the HtrA surface chaperone/protease during Streptococcus pneumoniae D39 cell division
    • pii: e00202-11. doi: 10.1128/mBio.00202-11.
    • Tsui, H.C., Keen, S.K., Sham, L.T., Wayne, K.J., and Winkler, M.E. (2011) Dynamic distribution of the SecA and SecY translocase subunits and septal localization of the HtrA surface chaperone/protease during Streptococcus pneumoniae D39 cell division. MBio 2. pii: e00202-11. doi: 10.1128/mBio.00202-11.
    • (2011) MBio , vol.2
    • Tsui, H.C.1    Keen, S.K.2    Sham, L.T.3    Wayne, K.J.4    Winkler, M.E.5
  • 73
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas, A., Banzhaf, M., Gross, C.A., and Vollmer, W. (2012) From the regulation of peptidoglycan synthesis to bacterial growth and morphology. Nat Rev Microbiol 10: 123-136.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 123-136
    • Typas, A.1    Banzhaf, M.2    Gross, C.A.3    Vollmer, W.4
  • 74
    • 84873775015 scopus 로고
    • Bagshaped macromolecules - a new outlook on bacterial cell walls
    • Weidel, W., and Pelzer, H. (1964) Bagshaped macromolecules - a new outlook on bacterial cell walls. Adv Enzymol Relat Areas Mol Biol 26: 193-232.
    • (1964) Adv Enzymol Relat Areas Mol Biol , vol.26 , pp. 193-232
    • Weidel, W.1    Pelzer, H.2
  • 75
    • 0030881627 scopus 로고    scopus 로고
    • Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole
    • Weiss, D.S., Pogliano, K., Carson, M., Guzman, L.M., Fraipont, C., Nguyen-Disteche, M., etal. (1997) Localization of the Escherichia coli cell division protein Ftsl (PBP3) to the division site and cell pole. Mol Microbiol 25: 671-681.
    • (1997) Mol Microbiol , vol.25 , pp. 671-681
    • Weiss, D.S.1    Pogliano, K.2    Carson, M.3    Guzman, L.M.4    Fraipont, C.5    Nguyen-Disteche, M.6
  • 76
    • 84856653970 scopus 로고    scopus 로고
    • MreB: pilot or passenger of cell wall synthesis?
    • White, C.L., and Gober, J.W. (2012) MreB: pilot or passenger of cell wall synthesis? Trends Microbiol 20: 74-79.
    • (2012) Trends Microbiol , vol.20 , pp. 74-79
    • White, C.L.1    Gober, J.W.2
  • 77
    • 0019218755 scopus 로고
    • In vivo interaction of β-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae
    • Williamson, R., Hakenbeck, R., and Tomasz, A. (1980) In vivo interaction of β-lactam antibiotics with the penicillin-binding proteins of Streptococcus pneumoniae. Antimicrob Agents Chemother 18: 629-637.
    • (1980) Antimicrob Agents Chemother , vol.18 , pp. 629-637
    • Williamson, R.1    Hakenbeck, R.2    Tomasz, A.3
  • 78
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pCU19 vectors
    • Yanish-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequence of the M13mp18 and pCU19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanish-Perron, C.1    Vieira, J.2    Messing, J.3
  • 79
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: a beta-lactam-binding domain
    • Yeats, C., Finn, R.D., and Bateman, A. (2002) The PASTA domain: a beta-lactam-binding domain. Trends Biochem Sci 27: 438.
    • (2002) Trends Biochem Sci , vol.27 , pp. 438
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 80
    • 39149104344 scopus 로고    scopus 로고
    • Penicillin-binding proteins and β-lactam resistance
    • Zapun, A., Contreras-Martel, C., and Vernet, T. (2008a) Penicillin-binding proteins and β-lactam resistance. FEMS Microbiol Rev 32: 361-385.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 361-385
    • Zapun, A.1    Contreras-Martel, C.2    Vernet, T.3
  • 82
    • 84899908696 scopus 로고    scopus 로고
    • PBP2x-mutationen in Streptococcus pneumoniae: auswirkungen auf β-lactam-resistenz und zellphysiologie. University of Kaiserslautern.
    • Zerfaß, I. PBP2x-mutationen in Streptococcus pneumoniae: auswirkungen auf β-lactam-resistenz und zellphysiologie. 2011. University of Kaiserslautern.
    • (2011)
    • Zerfaß, I.1
  • 83
    • 62949215691 scopus 로고    scopus 로고
    • An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338
    • Zerfaß, I., Hakenbeck, R., and Denapaite, D. (2009) An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338. Antimicrob Agents Chemother 53: 1107-1115.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 1107-1115
    • Zerfaß, I.1    Hakenbeck, R.2    Denapaite, D.3


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