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Volumn 191, Issue 4, 2009, Pages 1200-1210

Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYTIDINE DIPHOSPHATE; GENE PRODUCT; RIBITOL; RIBITOL 5 PHOSPHATE CYTIDYLYL TRANSFERASE; RIBULOSE 5 PHOSPHATE REDUCTASE; TARI PROTEIN; TARJ PROTEIN; TEICHOIC ACID; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

EID: 60849110560     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01120-08     Document Type: Article
Times cited : (47)

References (56)
  • 1
    • 35648988999 scopus 로고    scopus 로고
    • Predicted functions and linkage specificities of the products of the Streptococcus pneumoniae capsular biosynthetic loci
    • Aanensen, D. M., A. Mavroidi, S. D. Bentley, P. R. Reeves, and B. G. Spratt 2007. Predicted functions and linkage specificities of the products of the Streptococcus pneumoniae capsular biosynthetic loci. J. Bacteriol. 189:7856-7876.
    • (2007) J. Bacteriol , vol.189 , pp. 7856-7876
    • Aanensen, D.M.1    Mavroidi, A.2    Bentley, S.D.3    Reeves, P.R.4    Spratt, B.G.5
  • 2
    • 24644505760 scopus 로고    scopus 로고
    • Badger, J., J. M. Sauder, J. M. Adams, S. Antonysamy, K. Bain, M. G. Bergseid, S. G. Buchanan, M. D. Buchanan, Y. Batiyenko, J. A. Christopher, S. Emtage, A. Eroshkina, I. Feil, E. B. Furlong, K. S. Gajiwala, X. Gao, D. He, J. Hendle, A. Huber, K. Hoda, P. Kearins, C. Kissinger, B. Laubert, H. A. Lewis, J. Lin, K. Loomis, D. Lorimer, G. Louie, M. Maletic, C. D. Marsh, I. Miller, J. Molinari, H. J. Muller-Dieckmann, J. M. Newman, B. W. Noland, B. Pagarigan, F. Park, T. S. Peat, K. W. Post, S. Radojicic, A. Ramos, R. Romero, M. E. Rutter, W. E. Sanderson, K. D. Schwinn, J. Tresser, J. Winhoven, T. A. Wright, L. Wu, J. Xu, and T. J. Harris. 2005. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 60:787-796.
    • Badger, J., J. M. Sauder, J. M. Adams, S. Antonysamy, K. Bain, M. G. Bergseid, S. G. Buchanan, M. D. Buchanan, Y. Batiyenko, J. A. Christopher, S. Emtage, A. Eroshkina, I. Feil, E. B. Furlong, K. S. Gajiwala, X. Gao, D. He, J. Hendle, A. Huber, K. Hoda, P. Kearins, C. Kissinger, B. Laubert, H. A. Lewis, J. Lin, K. Loomis, D. Lorimer, G. Louie, M. Maletic, C. D. Marsh, I. Miller, J. Molinari, H. J. Muller-Dieckmann, J. M. Newman, B. W. Noland, B. Pagarigan, F. Park, T. S. Peat, K. W. Post, S. Radojicic, A. Ramos, R. Romero, M. E. Rutter, W. E. Sanderson, K. D. Schwinn, J. Tresser, J. Winhoven, T. A. Wright, L. Wu, J. Xu, and T. J. Harris. 2005. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 60:787-796.
  • 3
    • 0023917654 scopus 로고
    • A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay
    • Baykov, A. A., O. A. Evtushenko, and S. M. Avaeva. 1988. A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay. Anal. Biochem. 171:266-270.
    • (1988) Anal. Biochem , vol.171 , pp. 266-270
    • Baykov, A.A.1    Evtushenko, O.A.2    Avaeva, S.M.3
  • 5
    • 11844301664 scopus 로고    scopus 로고
    • A colorimetric assay for the determination of 4-diphosphocytidyl-2-C-methyl-D- eiythritol 4-phosphate synthase activity
    • Bernai, C., C. Palacin, A. Boronat, and S. Imperial. 2005. A colorimetric assay for the determination of 4-diphosphocytidyl-2-C-methyl-D- eiythritol 4-phosphate synthase activity. Anal. Biochem. 337:55-61.
    • (2005) Anal. Biochem , vol.337 , pp. 55-61
    • Bernai, C.1    Palacin, C.2    Boronat, A.3    Imperial, S.4
  • 6
    • 0027495480 scopus 로고
    • Complementation of growth defect in an ampC deletion mutant of Escherichia coli
    • Bishop, R. E., and J. H. Weiner. 1993. Complementation of growth defect in an ampC deletion mutant of Escherichia coli. FEMS Microbiol. Lett. 114: 349-354.
    • (1993) FEMS Microbiol. Lett , vol.114 , pp. 349-354
    • Bishop, R.E.1    Weiner, J.H.2
  • 7
    • 0002815512 scopus 로고    scopus 로고
    • Buehner, M., G. C. Ford, D. Moras, K. W. Olsen, and M. G. Rossman. 1973. D-Glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance. Proc. Natl. Acad. Sci. USA 70w:3052-3054.
    • Buehner, M., G. C. Ford, D. Moras, K. W. Olsen, and M. G. Rossman. 1973. D-Glyceraldehyde-3-phosphate dehydrogenase: three-dimensional structure and evolutionary significance. Proc. Natl. Acad. Sci. USA 70w:3052-3054.
  • 8
    • 0035977459 scopus 로고    scopus 로고
    • Campbell, H. A., and C. Kent. 2001. The CTP:phosphocholine cytidylyltrans-ferase encoded by the licC gene of Streptococcus pneumoniae: cloning, expression, purification, and characterization. Biochim. Biophys. Acta 1534: 85-95.
    • Campbell, H. A., and C. Kent. 2001. The CTP:phosphocholine cytidylyltrans-ferase encoded by the licC gene of Streptococcus pneumoniae: cloning, expression, purification, and characterization. Biochim. Biophys. Acta 1534: 85-95.
  • 9
    • 0023887565 scopus 로고
    • Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae
    • Chen, J. D., and D. A. Morrison. 1988. Construction and properties of a new insertion vector, pJDC9, that is protected by transcriptional terminators and useful for cloning of DNA from Streptococcus pneumoniae. Gene 64:155-164.
    • (1988) Gene , vol.64 , pp. 155-164
    • Chen, J.D.1    Morrison, D.A.2
  • 10
  • 11
    • 34948850302 scopus 로고    scopus 로고
    • The essential tacF gene is responsible for the choline-dependent growth phenotype of Streptococcus pneumoniae
    • Damjanovic, M., A. S. Kharat, A. Eberhardt, A. Tomasz, and W. Vollmer. 2007. The essential tacF gene is responsible for the choline-dependent growth phenotype of Streptococcus pneumoniae. J. Bacteriol. 189:7105-7111.
    • (2007) J. Bacteriol , vol.189 , pp. 7105-7111
    • Damjanovic, M.1    Kharat, A.S.2    Eberhardt, A.3    Tomasz, A.4    Vollmer, W.5
  • 12
    • 0036980198 scopus 로고    scopus 로고
    • From ecological reservoir to disease: The nasopharynx, day-care centres and drug-resistant clones of Streptococcus pneumoniae. microb
    • De Lencastre, H., and A. Tomasz. From ecological reservoir to disease: the nasopharynx, day-care centres and drug-resistant clones of Streptococcus pneumoniae. microb. Chemother. 50(Suppl. S2):75-81.
    • Chemother , vol.50 , Issue.SUPPL. S2 , pp. 75-81
    • De Lencastre, H.1    Tomasz, A.2
  • 14
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and K. Cowtan. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60:2126-2132.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 15
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans, P. 2006. Scaling and assessment of data quality. Acta Crystallogr. D62:72-82.
    • (2006) Acta Crystallogr. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 16
    • 0033863915 scopus 로고    scopus 로고
    • Phosphocholine of pneumococcal teichoic acids: Role in bacterial physiology and pneumococcal infection
    • Fischer, W. 2000. Phosphocholine of pneumococcal teichoic acids: role in bacterial physiology and pneumococcal infection. Res. Microbiol. 151:421-427.
    • (2000) Res. Microbiol , vol.151 , pp. 421-427
    • Fischer, W.1
  • 17
    • 0031415055 scopus 로고    scopus 로고
    • Fischer, W. 1997. Pneumococcal lipoteichoic and teichoic acid. Microb. Drng Resist. 3:309-325.
    • Fischer, W. 1997. Pneumococcal lipoteichoic and teichoic acid. Microb. Drng Resist. 3:309-325.
  • 18
    • 0027181992 scopus 로고
    • Teichoic acid and lipoteichoic acid of Streptococcus pneumoniae possess identical chain structures. A reinvestigation of teichoid acid (C polysaccharide)
    • Fischer, W., T. Behr, R. Hartmann, J. Peter-Katalinic, and H, Egge. 1993. Teichoic acid and lipoteichoic acid of Streptococcus pneumoniae possess identical chain structures. A reinvestigation of teichoid acid (C polysaccharide). Eur. J. Biochem. 215:851-857.
    • (1993) Eur. J. Biochem , vol.215 , pp. 851-857
    • Fischer, W.1    Behr, T.2    Hartmann, R.3    Peter-Katalinic, J.4    Egge, H.5
  • 19
    • 0032956875 scopus 로고    scopus 로고
    • acsl of Haemophilus influenzae type a capsulation locus region 11 encodes a bifunctional ribulose 5-phosphate reductase-CDP-ribitol pyro-phosphorylase
    • Follens, A., M. Veiga-da-Cunha, R. Merckx, E. van Schaftingen, and J. van Eldere. 1999. acsl of Haemophilus influenzae type a capsulation locus region 11 encodes a bifunctional ribulose 5-phosphate reductase-CDP-ribitol pyro-phosphorylase. J. Bacteriol. 181 :2001-2007.
    • (1999) J. Bacteriol , vol.181 , pp. 2001-2007
    • Follens, A.1    Veiga-da-Cunha, M.2    Merckx, R.3    van Schaftingen, E.4    van Eldere, J.5
  • 20
    • 34347269622 scopus 로고    scopus 로고
    • Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus
    • Grundling, A., and O. Schneewind. 2007. Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 104: 8478-8483.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8478-8483
    • Grundling, A.1    Schneewind, O.2
  • 21
    • 34548700626 scopus 로고    scopus 로고
    • Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: Five out of 15 promotors drive expression of small non-coding RNAs
    • Halfmann, A., M. Kovacs, R. Hakenbeck, and R. Brückner. 2007. Identification of the genes directly controlled by the response regulator CiaR in Streptococcus pneumoniae: five out of 15 promotors drive expression of small non-coding RNAs. Mol. Microbiol. 66:110-126.
    • (2007) Mol. Microbiol , vol.66 , pp. 110-126
    • Halfmann, A.1    Kovacs, M.2    Hakenbeck, R.3    Brückner, R.4
  • 22
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plas-mids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plas-mids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 23
    • 0027234835 scopus 로고
    • Isoprenoid biosynthesis in bacteria: Two different pathways?
    • Horbach, S., H. Sahm, and R. Welle. 1993. Isoprenoid biosynthesis in bacteria: two different pathways? FEMS Microbiol. Lett. 111:135-140.
    • (1993) FEMS Microbiol. Lett , vol.111 , pp. 135-140
    • Horbach, S.1    Sahm, H.2    Welle, R.3
  • 24
    • 0034806849 scopus 로고    scopus 로고
    • Hoskins, J., W. E. Alborn, Jr., J. Arnold, L. C. Blaszczak, S. Burgett, B. S. DeHoff, S. T. Estrem, L. Fritz, D. J. Fu, W. Fuller, C. Geringer, R. Gilmour, J. S. Glass, H. Khoja, A. R. Kraft, R. E. Lagace, D. J. LeBlanc, L. N. Lee, E. J. Lefkowitz, J. Lu, P. Matsushima, S. M. McAhren, M. McHenney, K. McLeaster, C. W. Mundy, T. I. Nicas, F. H. Norris, M. O'Gara, R. B. Peery, G. T. Robertson, P. Rockey, P. M. Sun, M. E. Winkler, Y. Yang, M. Young-Bellido, G. Zhao, C. A. Zook, R. H. Baltz, S. R. Jaskunas, P. R. Rosteck, Jr., P. L. Skatrud, and J. I. Glass. 2001. Genome of the bacterium Streptococcus pneumoniae strain R6. J. Bacteriol. 183:5709-5717.
    • Hoskins, J., W. E. Alborn, Jr., J. Arnold, L. C. Blaszczak, S. Burgett, B. S. DeHoff, S. T. Estrem, L. Fritz, D. J. Fu, W. Fuller, C. Geringer, R. Gilmour, J. S. Glass, H. Khoja, A. R. Kraft, R. E. Lagace, D. J. LeBlanc, L. N. Lee, E. J. Lefkowitz, J. Lu, P. Matsushima, S. M. McAhren, M. McHenney, K. McLeaster, C. W. Mundy, T. I. Nicas, F. H. Norris, M. O'Gara, R. B. Peery, G. T. Robertson, P. Rockey, P. M. Sun, M. E. Winkler, Y. Yang, M. Young-Bellido, G. Zhao, C. A. Zook, R. H. Baltz, S. R. Jaskunas, P. R. Rosteck, Jr., P. L. Skatrud, and J. I. Glass. 2001. Genome of the bacterium Streptococcus pneumoniae strain R6. J. Bacteriol. 183:5709-5717.
  • 25
    • 0037348430 scopus 로고    scopus 로고
    • Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidy-lyltransferase
    • Kemp, L. E., C. S. Bond, and W. N. Hunter. 2003. Structure of a tetragonal crystal form of Escherichia coli 2-C-methyl-D-erythritol 4-phosphate cytidy-lyltransferase. Acta Crystallogr. D 59:607-610.
    • (2003) Acta Crystallogr. D , vol.59 , pp. 607-610
    • Kemp, L.E.1    Bond, C.S.2    Hunter, W.N.3
  • 26
    • 50249114035 scopus 로고    scopus 로고
    • Different pathways of choline metabolism in two choline-independent strains of Streptococcus pneumoniae and their impact on virulence
    • Kharat, A. S., D. Denapaite, F. Gehre, R. Brückner, W. Vollmer, R. Hakenbeck, and A. Tomasz. 2008. Different pathways of choline metabolism in two choline-independent strains of Streptococcus pneumoniae and their impact on virulence. J. Bacteriol. 190:5907-5914.
    • (2008) J. Bacteriol , vol.190 , pp. 5907-5914
    • Kharat, A.S.1    Denapaite, D.2    Gehre, F.3    Brückner, R.4    Vollmer, W.5    Hakenbeck, R.6    Tomasz, A.7
  • 27
    • 33644844445 scopus 로고    scopus 로고
    • Drastic reduction in the virulence of Streptococcus pneumoniae expressing type 2 capsular polysaccharide but lacking choline residues in the wall
    • Kharat, A. S., and A. Tomasz. 2006. Drastic reduction in the virulence of Streptococcus pneumoniae expressing type 2 capsular polysaccharide but lacking choline residues in the wall. Mol. Microbiol. 60:93-97.
    • (2006) Mol. Microbiol , vol.60 , pp. 93-97
    • Kharat, A.S.1    Tomasz, A.2
  • 28
    • 33748670479 scopus 로고    scopus 로고
    • A functional dit operon, encoding proteins required for incorporation of d-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae
    • Kovacs, M., A. Halfmann, I. Fedtke, M. Heintz, A, Peschel, W. Vollmer, R. Hakenbeck, and R. Brückner. 2006. A functional dit operon, encoding proteins required for incorporation of d-alanine in teichoic acids in gram-positive bacteria, confers resistance to cationic antimicrobial peptides in Streptococcus pneumoniae. J. Bacteriol. 188:5797-5805.
    • (2006) J. Bacteriol , vol.188 , pp. 5797-5805
    • Kovacs, M.1    Halfmann, A.2    Fedtke, I.3    Heintz, M.4    Peschel, A.5    Vollmer, W.6    Hakenbeck, R.7    Brückner, R.8
  • 29
    • 0037040235 scopus 로고    scopus 로고
    • Structure and mechanism of CTP:phosphocholine cytidylyltransferase (LicC) from Streptococcus pneumoniae
    • Kwak, B. Y., Y. M. Zhang, M. Yun, R. J. Heath, C. O. Rock, S. Jackowski, and H. W. Park. 2002. Structure and mechanism of CTP:phosphocholine cytidylyltransferase (LicC) from Streptococcus pneumoniae. J. Biol. Chem. 277:4343-4350.
    • (2002) J. Biol. Chem , vol.277 , pp. 4343-4350
    • Kwak, B.Y.1    Zhang, Y.M.2    Yun, M.3    Heath, R.J.4    Rock, C.O.5    Jackowski, S.6    Park, H.W.7
  • 30
    • 0013861147 scopus 로고
    • Integration efficiency and genetic recombination in pneumococcal transformation
    • Lacks, S. 1966. Integration efficiency and genetic recombination in pneumococcal transformation. Genetics 53:207-235.
    • (1966) Genetics , vol.53 , pp. 207-235
    • Lacks, S.1
  • 31
    • 4243819309 scopus 로고
    • Formation of amylomaltase after genetic transformation of pneumococcus
    • Lacks, S., and R. D. Hotchkiss. 1960. Formation of amylomaltase after genetic transformation of pneumococcus. Biochim. Biophys. Acta 45:155-163.
    • (1960) Biochim. Biophys. Acta , vol.45 , pp. 155-163
    • Lacks, S.1    Hotchkiss, R.D.2
  • 32
    • 0036006036 scopus 로고    scopus 로고
    • Comparison of ribitol and glycerol teichoic acid genes in Bacillus subtilis W23 and 168: Identical function, similar divergent organization, but different regulation
    • Lazarevic, V., F. X. Abellan, S. B. Moller, D. Karamata, and C. Mauel. 2002. Comparison of ribitol and glycerol teichoic acid genes in Bacillus subtilis W23 and 168: identical function, similar divergent organization, but different regulation. Microbiology 148:815-824.
    • (2002) Microbiology , vol.148 , pp. 815-824
    • Lazarevic, V.1    Abellan, F.X.2    Moller, S.B.3    Karamata, D.4    Mauel, C.5
  • 33
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie, A. G. 2006. The integration of macromolecular diffraction data. Acta Crystallogr. D 62:48-57.
    • (2006) Acta Crystallogr. D , vol.62 , pp. 48-57
    • Leslie, A.G.1
  • 34
    • 0031000618 scopus 로고    scopus 로고
    • Streptococcal competence for genetic transformation: Regulation by peptide pheromones
    • Morrison, D. A. 1997. Streptococcal competence for genetic transformation: regulation by peptide pheromones. Microb. Drug Resist. 3:27-37.
    • (1997) Microb. Drug Resist , vol.3 , pp. 27-37
    • Morrison, D.A.1
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., A, A, Vagin, and E. J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53:240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.A.A.1    Vagin2    Dodson, E.J.3
  • 36
    • 0347479228 scopus 로고    scopus 로고
    • A continuum of anionic charge: Structures and functions of D-alanyl-teichoic acids in gram-positive bacteria
    • Neuhaus, F. C, and J. Baddiley. 2003. A continuum of anionic charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol. Mol. Biol. Rev. 67:686-723.
    • (2003) Microbiol. Mol. Biol. Rev , vol.67 , pp. 686-723
    • Neuhaus, F.C.1    Baddiley, J.2
  • 37
    • 0028982844 scopus 로고
    • Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation
    • Perego, M,, P. Glaser, A, Minutello, M. A. Strauch, K. Leopold, and W. Fischer. 1995. Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation. J. Biol. Chem. 270:15598-15606.
    • (1995) J. Biol. Chem , vol.270 , pp. 15598-15606
    • Perego, M.P.1    Glaser, A.2    Minutello, M.3    Strauch, A.4    Leopold, K.5    Fischer, W.6
  • 38
    • 4644350080 scopus 로고    scopus 로고
    • Bifunctional catalysis by CDP-ribitol synthase: Convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus
    • Pereira, M. P., and E. D. Brown. 2004. Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus. Biochemistry 43: 11802-11812.
    • (2004) Biochemistry , vol.43 , pp. 11802-11812
    • Pereira, M.P.1    Brown, E.D.2
  • 39
    • 49449086631 scopus 로고    scopus 로고
    • Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases
    • Pereira, M. P., M. A. D'Elia, J. Troczynska, and E. D. Brown. 2008. Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. J. Bacteriol. 190:5642-5649.
    • (2008) J. Bacteriol , vol.190 , pp. 5642-5649
    • Pereira, M.P.1    D'Elia, M.A.2    Troczynska, J.3    Brown, E.D.4
  • 40
    • 0033605557 scopus 로고    scopus 로고
    • Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins. protegrins, and other antimicrobial peptides
    • Peschel, A., M. Otto, R. W. Jack, H. Kaibacher, G. Jung, and F. Götz. 1999. Inactivation of the dlt operon in Staphylococcus aureus confers sensitivity to defensins. protegrins, and other antimicrobial peptides. J. Biol. Chem. 274: 8405-8410.
    • (1999) J. Biol. Chem , vol.274 , pp. 8405-8410
    • Peschel, A.1    Otto, M.2    Jack, R.W.3    Kaibacher, H.4    Jung, G.5    Götz, F.6
  • 41
    • 33646362031 scopus 로고    scopus 로고
    • Genomic characterization of ribitol teichoic acid synthesis in Staphylococcus aureus: Genes, genomic organization and gene duplication
    • Qian, Z., Y. Yin, Y. Zhang, L. Lu, Y. Li, and Y. Jiang. 2006. Genomic characterization of ribitol teichoic acid synthesis in Staphylococcus aureus: genes, genomic organization and gene duplication. BMC Genomics 7:74.
    • (2006) BMC Genomics , vol.7 , pp. 74
    • Qian, Z.1    Yin, Y.2    Zhang, Y.3    Lu, L.4    Li, Y.5    Jiang, Y.6
  • 42
    • 0034953307 scopus 로고    scopus 로고
    • Structure of 4-diphosphocytidyl-2- C-methylerythritol synthetase involved in mevalonate-independent isopre-noid biosynthesis
    • Richard, S. B., M. E. Bowman, W. Kwiatkowski, I. Kang, C. Chow, A. M. Lillo, D. E. Cane, and J. P. Noel. 2001. Structure of 4-diphosphocytidyl-2- C-methylerythritol synthetase involved in mevalonate-independent isopre-noid biosynthesis. Nat. Struct. Biol. 8:641-648.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 641-648
    • Richard, S.B.1    Bowman, M.E.2    Kwiatkowski, W.3    Kang, I.4    Chow, C.5    Lillo, A.M.6    Cane, D.E.7    Noel, J.P.8
  • 43
    • 0034897158 scopus 로고    scopus 로고
    • The licC gene of Streptococcus pneumoniae encodes a CTP:phosphocholine cytidylyltrans-ferase
    • Rock, C. O., R. J. Heath, H. W. Park, and S. Jackowski. 2001. The licC gene of Streptococcus pneumoniae encodes a CTP:phosphocholine cytidylyltrans-ferase. J. Bacteriol. 183:4927-4931.
    • (2001) J. Bacteriol , vol.183 , pp. 4927-4931
    • Rock, C.O.1    Heath, R.J.2    Park, H.W.3    Jackowski, S.4
  • 45
    • 0014200202 scopus 로고
    • Choline in the cell wall of a bacterium: Novel type of polymer-linked choline in Pneumococcus
    • Tomasz, A. 1967. Choline in the cell wall of a bacterium: novel type of polymer-linked choline in Pneumococcus. Science 157:694-697.
    • (1967) Science , vol.157 , pp. 694-697
    • Tomasz, A.1
  • 46
    • 0000455877 scopus 로고
    • Regulation of the transformability of the pneumococcal cultures by macromolecular cell products
    • Tomasz, A., and R. D. Hotchkiss. 1964. Regulation of the transformability of the pneumococcal cultures by macromolecular cell products. Proc. Natl. Acad. Sci. USA 51:480-487.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 480-487
    • Tomasz, A.1    Hotchkiss, R.D.2
  • 47
    • 35948960351 scopus 로고    scopus 로고
    • Multidrug-resistant Streptococcus pneumoniae infections: Current and future therapeutic options
    • Van Bambeke, F., R. R. Reinert, P. C. Appelbaum, P. M. Tnlkens, and W. E. Peetermans. 2007. Multidrug-resistant Streptococcus pneumoniae infections: current and future therapeutic options. Drugs 67:2355-2382.
    • (2007) Drugs , vol.67 , pp. 2355-2382
    • Van Bambeke, F.1    Reinert, R.R.2    Appelbaum, P.C.3    Tnlkens, P.M.4    Peetermans, W.E.5
  • 48
    • 11144334092 scopus 로고    scopus 로고
    • The teichoic acid (C-polysaccharide) synthesized by Streptococcus pneumoniae serotype 5 has a specific structure
    • Vialle, S., P. Sepulcri, J. Dubayle, and P. Talaga. 2005. The teichoic acid (C-polysaccharide) synthesized by Streptococcus pneumoniae serotype 5 has a specific structure. Carbohydr. Res. 340:91-96.
    • (2005) Carbohydr. Res , vol.340 , pp. 91-96
    • Vialle, S.1    Sepulcri, P.2    Dubayle, J.3    Talaga, P.4
  • 50
    • 40949089662 scopus 로고    scopus 로고
    • Teichoic acids and related cell-wall glycopolymers in gram-positive physiology and host interactions
    • Weidenmaier, C., and A. Peschel. 2008. Teichoic acids and related cell-wall glycopolymers in gram-positive physiology and host interactions. Nat. Rev. Microbiol. 6:276-287.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 276-287
    • Weidenmaier, C.1    Peschel, A.2
  • 51
    • 0029899176 scopus 로고    scopus 로고
    • Incorporation of choline into Streptococcus pneumoniae cell wall antigens: Evidence for choline kinase activity
    • Whiting, G. C, and S. H. Gillespie. 1996. Incorporation of choline into Streptococcus pneumoniae cell wall antigens: evidence for choline kinase activity. FEMS Microbiol. Lett. 138:141-145.
    • (1996) FEMS Microbiol. Lett , vol.138 , pp. 141-145
    • Whiting, G.C.1    Gillespie, S.H.2
  • 53
    • 0037208360 scopus 로고    scopus 로고
    • An overview of the CCP4 project in protein crystallography: An example of a collaborative project
    • Winn, M. D. 2003. An overview of the CCP4 project in protein crystallography: an example of a collaborative project. J. Synchrotron Radiat. 10:23-25.
    • (2003) J. Synchrotron Radiat , vol.10 , pp. 23-25
    • Winn, M.D.1
  • 55
    • 0033022866 scopus 로고    scopus 로고
    • Zhang, J, R., L Idanpaan-Heikkila, W. Fischer, and E. I. Tuomanen. 1999. Pneumococcal licD2 gene is involved in phosphorylcholine metabolism. Mol. Microbiol. 31:1477-1488.
    • Zhang, J, R., L Idanpaan-Heikkila, W. Fischer, and E. I. Tuomanen. 1999. Pneumococcal licD2 gene is involved in phosphorylcholine metabolism. Mol. Microbiol. 31:1477-1488.
  • 56
    • 0035942335 scopus 로고    scopus 로고
    • Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunc-tional CDP-ribitol synthase from Haemophilus influenzae
    • Zolli, M., D. J. Kobric, and E. D, Brown. 2001. Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunc-tional CDP-ribitol synthase from Haemophilus influenzae. Biochemistry 40: 5041-5048.
    • (2001) Biochemistry , vol.40 , pp. 5041-5048
    • Zolli, M.1    Kobric, D.J.2    Brown, E.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.