메뉴 건너뛰기




Volumn 159, Issue PART 9, 2013, Pages 1842-1852

Phenotypic analysis of Eschericia coli mutants lacking L,D-transpeptidases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; EDETIC ACID; GAMMA GLUTAMYLTRANSFERASE; LIPOPROTEIN; METHIONINE; PERIPLASMIC PROTEIN;

EID: 84883404387     PISSN: 13500872     EISSN: 14652080     Source Type: Journal    
DOI: 10.1099/mic.0.069211-0     Document Type: Article
Times cited : (48)

References (46)
  • 2
    • 0021154432 scopus 로고
    • The structure and mode of action of glycopeptide antibiotics of the vancomycin group
    • Barna, J. C. & Williams, D. H. (1984). The structure and mode of action of glycopeptide antibiotics of the vancomycin group. Annu Rev Microbiol 38, 339-357.
    • (1984) Annu Rev Microbiol , vol.38 , pp. 339-357
    • Barna, J.C.1    Williams, D.H.2
  • 3
    • 30344465753 scopus 로고    scopus 로고
    • B. subtilis YkuD protein at 2.0 Åresolution: Insights into the structure and function of a novel, ubiquitous family of bacterial enzymes
    • Bielnicki, J., Devedjiev, Y., Derewenda, U., Dauter, Z., Joachimiak, A. & Derewenda, Z. S. (2006). B. subtilis YkuD protein at 2.0 Åresolution: insights into the structure and function of a novel, ubiquitous family of bacterial enzymes. Proteins 62, 144-151.
    • (2006) Proteins , vol.62 , pp. 144-151
    • Bielnicki, J.1    Devedjiev, Y.2    Derewenda, U.3    Dauter, Z.4    Joachimiak, A.5    Derewenda, Z.S.6
  • 4
    • 0031887807 scopus 로고    scopus 로고
    • Maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation
    • Boos, W. & Shuman, H. (1998). Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol Mol Biol Rev 62, 204-229.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, H.2
  • 5
    • 0016748566 scopus 로고
    • Covalent lipoprotein from the outer membrane of Escherichia coli
    • Braun, V. (1975). Covalent lipoprotein from the outer membrane of Escherichia coli. Biochim Biophys Acta 415, 335-377.
    • (1975) Biochim Biophys Acta , vol.415 , pp. 335-377
    • Braun, V.1
  • 6
    • 0014767677 scopus 로고
    • The covalent murein-lipoprotein structure of the Escherichia coli cell wall. The attachment site of the lipoprotein on the murein
    • Braun, V. & Sieglin, U. (1970). The covalent murein-lipoprotein structure of the Escherichia coli cell wall. The attachment site of the lipoprotein on the murein. Eur J Biochem 13, 336-346.
    • (1970) Eur J Biochem , vol.13 , pp. 336-346
    • Braun, V.1    Sieglin, U.2
  • 7
    • 0014806606 scopus 로고
    • The murein-lipoprotein linkage in the cell wall of Escherichia coli
    • Braun, V. & Wolff, H. (1970). The murein-lipoprotein linkage in the cell wall of Escherichia coli. Eur J Biochem 14, 387-391.
    • (1970) Eur J Biochem , vol.14 , pp. 387-391
    • Braun, V.1    Wolff, H.2
  • 8
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • Buist, G., Steen, A., Kok, J. & Kuipers, O. P. (2008). LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 68, 838-847.
    • (2008) Mol Microbiol , vol.68 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 9
    • 0020635850 scopus 로고
    • Changes in the composition of Escherichia coli murein as it ages during exponential growth
    • Burman, L. G. & Park, J. T. (1983). Changes in the composition of Escherichia coli murein as it ages during exponential growth. J Bacteriol 155, 447-453.
    • (1983) J Bacteriol , vol.155 , pp. 447-453
    • Burman, L.G.1    Park, J.T.2
  • 10
    • 80053614751 scopus 로고    scopus 로고
    • Distinct pathways for modification of the bacterial cell wall by non-canonical d-amino acids
    • Cava, F., de Pedro, M. A., Lam, H., Davis, B. M. & Waldor, M. K. (2011). Distinct pathways for modification of the bacterial cell wall by non-canonical d-amino acids. EMBO J 30, 3442-3453.
    • (2011) EMBO J , vol.30 , pp. 3442-3453
    • Cava, F.1    de Pedro, M.A.2    Lam, H.3    Davis, B.M.4    Waldor, M.K.5
  • 11
    • 79951809756 scopus 로고    scopus 로고
    • The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli
    • Cowles, C. E., Li, Y., Semmelhack, M. F., Cristea, I. M. & Silhavy, T. J. (2011). The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli. Mol Microbiol 79, 1168-1181.
    • (2011) Mol Microbiol , vol.79 , pp. 1168-1181
    • Cowles, C.E.1    Li, Y.2    Semmelhack, M.F.3    Cristea, I.M.4    Silhavy, T.J.5
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A. & Wanner, B. L. (2000). One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97, 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 14
    • 0025168851 scopus 로고
    • Growth pattern of the murein sacculus of Escherichia coli
    • Glauner, B. & Höltje, J. V. (1990). Growth pattern of the murein sacculus of Escherichia coli. J Biol Chem 265, 18988-18996.
    • (1990) J Biol Chem , vol.265 , pp. 18988-18996
    • Glauner, B.1    Höltje, J.V.2
  • 15
    • 0023677844 scopus 로고
    • The composition of the murein of Escherichia coli
    • Glauner, B., Höltje, J. V. & Schwarz, U. (1988). The composition of the murein of Escherichia coli. J Biol Chem 263, 10088-10095.
    • (1988) J Biol Chem , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.V.2    Schwarz, U.3
  • 16
    • 0036898699 scopus 로고    scopus 로고
    • Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent
    • Goffin, C. & Ghuysen, J. M. (2002). Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent. Microbiol Mol Biol Rev 66, 702-738.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 702-738
    • Goffin, C.1    Ghuysen, J.M.2
  • 17
    • 70449328574 scopus 로고
    • Cell division in a species of Erwinia. I. Inhibition of division by d-amino acids
    • Grula, E. A. (1960). Cell division in a species of Erwinia. I. Inhibition of division by d-amino acids. J Bacteriol 80, 375-385.
    • (1960) J Bacteriol , vol.80 , pp. 375-385
    • Grula, E.A.1
  • 18
    • 77950534682 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin
    • Gupta, R., Lavollay, M., Mainardi, J. L., Arthur, M., Bishai, W. R. & Lamichhane, G. (2010). The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat Med 16, 466-469.
    • (2010) Nat Med , vol.16 , pp. 466-469
    • Gupta, R.1    Lavollay, M.2    Mainardi, J.L.3    Arthur, M.4    Bishai, W.R.5    Lamichhane, G.6
  • 19
    • 0017610608 scopus 로고
    • On the process of cellular division in Escherichia coli: A mutant of E. coli lacking a murein-lipoprotein
    • Hirota, Y., Suzuki, H., Nishimura, Y. & Yasuda, S. (1977). On the process of cellular division in Escherichia coli: a mutant of E. coli lacking a murein-lipoprotein. Proc Natl Acad Sci U S A 74, 1417-1420.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 1417-1420
    • Hirota, Y.1    Suzuki, H.2    Nishimura, Y.3    Yasuda, S.4
  • 20
    • 0032575051 scopus 로고    scopus 로고
    • A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: Application for isolation of unmarked Pseudomonas aeruginosa mutants
    • Hoang, T. T., Karkhoff-Schweizer, R. R., Kutchma, A. J. & Schweizer, H. P. (1998). A broad-host-range Flp-FRT recombination system for site-specific excision of chromosomally-located DNA sequences: application for isolation of unmarked Pseudomonas aeruginosa mutants. Gene 212, 77-86.
    • (1998) Gene , vol.212 , pp. 77-86
    • Hoang, T.T.1    Karkhoff-Schweizer, R.R.2    Kutchma, A.J.3    Schweizer, H.P.4
  • 21
    • 84862015701 scopus 로고    scopus 로고
    • Peptidoglycan plasticity in bacteria: Stress-induced peptidoglycan editing by noncanonical Damino acids
    • Horcajo, P., de Pedro, M. A. & Cava, F. (2012). Peptidoglycan plasticity in bacteria: stress-induced peptidoglycan editing by noncanonical Damino acids. Microb Drug Resist 18, 306-313.
    • (2012) Microb Drug Resist , vol.18 , pp. 306-313
    • Horcajo, P.1    de Pedro, M.A.2    Cava, F.3
  • 22
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): Unique resources for biological research
    • Kitagawa, M., Ara, T., Arifuzzaman, M., Ioka-Nakamichi, T., Inamoto, E., Toyonaga, H. & Mori, H. (2006). Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res 12, 291-299.
    • (2006) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6    Mori, H.7
  • 24
    • 44949093590 scopus 로고    scopus 로고
    • The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L, D-transpeptidation
    • Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Gutmann, L. & Mainardi, J. L. (2008). The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L, D-transpeptidation. J Bacteriol 190, 4360-4366.
    • (2008) J Bacteriol , vol.190 , pp. 4360-4366
    • Lavollay, M.1    Arthur, M.2    Fourgeaud, M.3    Dubost, L.4    Marie, A.5    Veziris, N.6    Blanot, D.7    Gutmann, L.8    Mainardi, J.L.9
  • 26
    • 34250305970 scopus 로고    scopus 로고
    • Specificity of L, D-transpeptidases from Gram-positive bacteria producing different peptidoglycan chemotypes
    • Magnet, S., Arbeloa, A., Mainardi, J. L., Hugonnet, J. E., Fourgeaud, M., Dubost, L., Marie, A., Delfosse, V., Mayer, C. & other authors (2007a). Specificity of L, D-transpeptidases from Gram-positive bacteria producing different peptidoglycan chemotypes. J Biol Chem 282, 13151-13159.
    • (2007) J Biol Chem , vol.282 , pp. 13151-13159
    • Magnet, S.1    Arbeloa, A.2    Mainardi, J.L.3    Hugonnet, J.E.4    Fourgeaud, M.5    Dubost, L.6    Marie, A.7    Delfosse, V.8    Mayer, C.9
  • 28
    • 46049085808 scopus 로고    scopus 로고
    • Identification of the L, D-transpeptidases for peptidoglycan crosslinking in Escherichia coli
    • Magnet, S., Dubost, L., Marie, A., Arthur, M. & Gutmann, L. (2008). Identification of the L, D-transpeptidases for peptidoglycan crosslinking in Escherichia coli. J Bacteriol 190, 4782-4785.
    • (2008) J Bacteriol , vol.190 , pp. 4782-4785
    • Magnet, S.1    Dubost, L.2    Marie, A.3    Arthur, M.4    Gutmann, L.5
  • 29
    • 0034595991 scopus 로고    scopus 로고
    • Novel mechanism of β-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium
    • Mainardi, J. L., Legrand, R., Arthur, M., Schoot, B., van Heijenoort, J. & Gutmann, L. (2000). Novel mechanism of β-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium. J Biol Chem 275, 16490-16496.
    • (2000) J Biol Chem , vol.275 , pp. 16490-16496
    • Mainardi, J.L.1    Legrand, R.2    Arthur, M.3    Schoot, B.4    van Heijenoort, J.5    Gutmann, L.6
  • 33
    • 80052935371 scopus 로고    scopus 로고
    • Assembling new Escherichia coli strains by transduction using phage P1
    • Moore, S. D. (2011). Assembling new Escherichia coli strains by transduction using phage P1. Methods Mol Biol 765, 155-169.
    • (2011) Methods Mol Biol , vol.765 , pp. 155-169
    • Moore, S.D.1
  • 34
    • 80051695335 scopus 로고    scopus 로고
    • Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links
    • Peltier, J., Courtin, P., El Meouche, I., Lemée, L., Chapot-Chartier, M. P. & Pons, J. L. (2011). Clostridium difficile has an original peptidoglycan structure with a high level of N-acetylglucosamine deacetylation and mainly 3-3 cross-links. J Biol Chem 286, 29053-29062.
    • (2011) J Biol Chem , vol.286 , pp. 29053-29062
    • Peltier, J.1    Courtin, P.2    El Meouche, I.3    Lemée, L.4    Chapot-Chartier, M.P.5    Pons, J.L.6
  • 35
    • 0021944190 scopus 로고
    • Structural modifications in the peptidoglycan of Escherichia coli associated with changes in the state of growth of the culture
    • Pisabarro, A. G., de Pedro, M. A. & Vázquez, D. (1985). Structural modifications in the peptidoglycan of Escherichia coli associated with changes in the state of growth of the culture. J Bacteriol 161, 238-242.
    • (1985) J Bacteriol , vol.161 , pp. 238-242
    • Pisabarro, A.G.1    de Pedro, M.A.2    Vázquez, D.3
  • 37
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H. & Kandler, O. (1972). Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 36, 407-477.
    • (1972) Bacteriol Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 38
    • 0036142456 scopus 로고    scopus 로고
    • Modification of the peptidoglycan of Escherichia coli in the viable but nonculturable state
    • Signoretto, C., Lleò, M. M. & Canepari, P. (2002). Modification of the peptidoglycan of Escherichia coli in the viable but nonculturable state. Curr Microbiol 44, 125-131.
    • (2002) Curr Microbiol , vol.44 , pp. 125-131
    • Signoretto, C.1    Lleò, M.M.2    Canepari, P.3
  • 39
    • 84855889658 scopus 로고    scopus 로고
    • From the regulation of peptidoglycan synthesis to bacterial growth and morphology
    • Typas, A., Banzhaf, M., Gross, C. A. & 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
  • 40
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. (1992). Agents that increase the permeability of the outer membrane. Microbiol Rev 56, 395-411.
    • (1992) Microbiol Rev , vol.56 , pp. 395-411
    • Vaara, M.1
  • 41
    • 50049104157 scopus 로고    scopus 로고
    • Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
    • Vollmer, W. & Bertsche, U. (2008). Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim Biophys Acta 1778, 1714-1734.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1714-1734
    • Vollmer, W.1    Bertsche, U.2
  • 43
    • 84873775015 scopus 로고
    • Bagshapedmacromolecules-a new outlook on bacterial cell walls
    • Weidel, W. & Pelzer, H. (1964). Bagshapedmacromolecules-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
  • 44
    • 0016209670 scopus 로고
    • Occurrence of d-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria
    • Wietzerbin, J., Das, B. C., Petit, J. F., Lederer, E., Leyh-Bouille, M. & Ghuysen, J. M. (1974). Occurrence of d-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria. Biochemistry 13, 3471-3476.
    • (1974) Biochemistry , vol.13 , pp. 3471-3476
    • Wietzerbin, J.1    Das, B.C.2    Petit, J.F.3    Lederer, E.4    Leyh-Bouille, M.5    Ghuysen, J.M.6
  • 45
    • 0017665289 scopus 로고
    • Genetic characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein
    • Yem, D. W. & Wu, H. C. (1977). Genetic characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein. J Bacteriol 131, 759-764.
    • (1977) J Bacteriol , vol.131 , pp. 759-764
    • Yem, D.W.1    Wu, H.C.2
  • 46
    • 0017836107 scopus 로고
    • Physiological characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein
    • Yem, D. W. & Wu, H. C. (1978). Physiological characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein. J Bacteriol 133, 1419-1426.
    • (1978) J Bacteriol , vol.133 , pp. 1419-1426
    • Yem, D.W.1    Wu, H.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.