메뉴 건너뛰기




Volumn 86, Issue 5, 2012, Pages 1031-1035

Bacterial growth does require peptidoglycan hydrolases

Author keywords

[No Author keywords available]

Indexed keywords

CWLO PROTEIN; HYDROLASE; LYTE PROTEIN; PEPTIDOGLYCAN; PEPTIDOGLYCAN HYDROLASE; SPR PROTEIN; UNCLASSIFIED DRUG; YDHO PROTEIN; YEBA PROTEIN;

EID: 84870246510     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12059     Document Type: Note
Times cited : (64)

References (29)
  • 1
    • 51849165615 scopus 로고    scopus 로고
    • Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad
    • Aramini, J.M., Rossi, P., Huang, Y.J., Zhao, L., Jiang, M., Maglaqui, M., etal. (2008) Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad. Biochemistry 47: 9715-9717.
    • (2008) Biochemistry , vol.47 , pp. 9715-9717
    • Aramini, J.M.1    Rossi, P.2    Huang, Y.J.3    Zhao, L.4    Jiang, M.5    Maglaqui, M.6
  • 3
    • 0038403691 scopus 로고    scopus 로고
    • The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases
    • Bateman, A., and Rawlings, N.D. (2003) The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem Sci 28: 234-237.
    • (2003) Trends Biochem Sci , vol.28 , pp. 234-237
    • Bateman, A.1    Rawlings, N.D.2
  • 4
    • 34250632446 scopus 로고    scopus 로고
    • The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis
    • Bisicchia, P., Noone, D., Lioliou, E., Howell, A., Quigley, S., Jensen, T., etal. (2007) The essential YycFG two-component system controls cell wall metabolism in Bacillus subtilis. Mol Microbiol 65: 180-200.
    • (2007) Mol Microbiol , vol.65 , pp. 180-200
    • Bisicchia, P.1    Noone, D.2    Lioliou, E.3    Howell, A.4    Quigley, S.5    Jensen, T.6
  • 5
    • 1842611616 scopus 로고    scopus 로고
    • Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases
    • Bochtler, M., Odintsov, S.G., Marcyjaniak, M., and Sabala, I. (2004) Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases. Protein Sci 13: 854-861.
    • (2004) Protein Sci , vol.13 , pp. 854-861
    • Bochtler, M.1    Odintsov, S.G.2    Marcyjaniak, M.3    Sabala, I.4
  • 6
    • 33748751261 scopus 로고    scopus 로고
    • In vitro synthesis of cross-linked murein and its attachment to sacculi by PBP1A from Escherichia coli
    • Born, P., Breukink, E., and Vollmer, W. (2006) In vitro synthesis of cross-linked murein and its attachment to sacculi by PBP1A from Escherichia coli. J Biol Chem 281: 26985-26993.
    • (2006) J Biol Chem , vol.281 , pp. 26985-26993
    • Born, P.1    Breukink, E.2    Vollmer, W.3
  • 7
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez, R., Formstone, A., Li, Y., Ehrlich, S.D., Noirot, P., and Errington, J. (2006) Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell 11: 399-409.
    • (2006) Dev Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 8
    • 84863088336 scopus 로고    scopus 로고
    • Structure of a peptidoglycan amidase effector targeted to Gram-negative bacteria by the type VI secretion system
    • Chou, S., Bui, N.K., Russell, A.B., Lexa, K.W., Gardiner, T.E., Leroux, M., etal. (2012) Structure of a peptidoglycan amidase effector targeted to Gram-negative bacteria by the type VI secretion system. Cell Rep 1: 656-664.
    • (2012) Cell Rep , vol.1 , pp. 656-664
    • Chou, S.1    Bui, N.K.2    Russell, A.B.3    Lexa, K.W.4    Gardiner, T.E.5    Leroux, M.6
  • 9
    • 84857073328 scopus 로고    scopus 로고
    • Synthetic lethality of the lytE cwlO genotype in Bacillus subtilis is caused by lack of D,L-endopeptidase activity at the lateral cell wall
    • Hashimoto, M., Ooiwa, S., and Sekiguchi, J. (2012) Synthetic lethality of the lytE cwlO genotype in Bacillus subtilis is caused by lack of D, L-endopeptidase activity at the lateral cell wall. J Bacteriol 194: 796-803.
    • (2012) J Bacteriol , vol.194 , pp. 796-803
    • Hashimoto, M.1    Ooiwa, S.2    Sekiguchi, J.3
  • 10
    • 0034945221 scopus 로고    scopus 로고
    • Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli
    • Heidrich, C., Templin, M.F., Ursinus, A., Merdanovic, M., Berger, J., Schwarz, H., etal. (2001) Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli. Mol Microbiol 41: 167-178.
    • (2001) Mol Microbiol , vol.41 , pp. 167-178
    • Heidrich, C.1    Templin, M.F.2    Ursinus, A.3    Merdanovic, M.4    Berger, J.5    Schwarz, H.6
  • 11
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J.-V. (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62: 181-203.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Höltje, J.-V.1
  • 12
    • 0024458975 scopus 로고
    • Peptidoglycan synthesis during the cell cycle of Escherichia coli: composition and mode of insertion
    • de Jonge, B.L., Wientjes, F.B., Jurida, I., Driehuis, F., Wouters, J.T., and Nanninga, N. (1989) Peptidoglycan synthesis during the cell cycle of Escherichia coli: composition and mode of insertion. J Bacteriol 171: 5783-5794.
    • (1989) J Bacteriol , vol.171 , pp. 5783-5794
    • de Jonge, B.L.1    Wientjes, F.B.2    Jurida, I.3    Driehuis, F.4    Wouters, J.T.5    Nanninga, N.6
  • 13
    • 84860904824 scopus 로고    scopus 로고
    • Specialized peptidoglycan hydrolases sculpt the intra-bacterial niche of predatory Bdellovibrio and increase population fitness
    • Lerner, T.R., Lovering, A.L., Bui, N.K., Uchida, K., Aizawa, S., Vollmer, W., and Sockett, R.E. (2012) Specialized peptidoglycan hydrolases sculpt the intra-bacterial niche of predatory Bdellovibrio and increase population fitness. PLoS Pathog 8: e1002524.
    • (2012) PLoS Pathog , vol.8
    • Lerner, T.R.1    Lovering, A.L.2    Bui, N.K.3    Uchida, K.4    Aizawa, S.5    Vollmer, W.6    Sockett, R.E.7
  • 14
    • 6344260684 scopus 로고    scopus 로고
    • Peptidoglycan amidase MepA is a LAS metallopeptidase
    • Marcyjaniak, M., Odintsov, S.G., Sabala, I., and Bochtler, M. (2004) Peptidoglycan amidase MepA is a LAS metallopeptidase. J Biol Chem 279: 43982-43989.
    • (2004) J Biol Chem , vol.279 , pp. 43982-43989
    • Marcyjaniak, M.1    Odintsov, S.G.2    Sabala, I.3    Bochtler, M.4
  • 15
    • 0037727706 scopus 로고    scopus 로고
    • Amidase domains from bacterial and phage autolysins define a family of gamma-D,L-glutamate-specific amidohydrolases
    • Rigden, D.J., Jedrzejas, M.J., and Galperin, M.Y. (2003) Amidase domains from bacterial and phage autolysins define a family of gamma-D, L-glutamate-specific amidohydrolases. Trends Biochem Sci 28: 230-234.
    • (2003) Trends Biochem Sci , vol.28 , pp. 230-234
    • Rigden, D.J.1    Jedrzejas, M.J.2    Galperin, M.Y.3
  • 16
    • 79960648176 scopus 로고    scopus 로고
    • Type VI secretion delivers bacteriolytic effectors to target cells
    • Russell, A.B., Hood, R.D., Bui, N.K., LeRoux, M., Vollmer, W., and Mougous, J.D. (2011) Type VI secretion delivers bacteriolytic effectors to target cells. Nature 475: 343-347.
    • (2011) Nature , vol.475 , pp. 343-347
    • Russell, A.B.1    Hood, R.D.2    Bui, N.K.3    LeRoux, M.4    Vollmer, W.5    Mougous, J.D.6
  • 17
    • 84861126596 scopus 로고    scopus 로고
    • A widespread bacterial type VI secretion effector superfamily identified using a heuristic approach
    • Russell, A.B., Singh, P., Brittnacher, M., Bui, N.K., Hood, R.D., Carl, M.A., etal. (2012) A widespread bacterial type VI secretion effector superfamily identified using a heuristic approach. Cell Host Microbe 11: 538-549.
    • (2012) Cell Host Microbe , vol.11 , pp. 538-549
    • Russell, A.B.1    Singh, P.2    Brittnacher, M.3    Bui, N.K.4    Hood, R.D.5    Carl, M.A.6
  • 18
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
    • Sauvage, E., Kerff, F., Terrak, M., Ayala, J.A., and Charlier, P. (2008) The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol Rev 32: 234-258.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 19
    • 81055126198 scopus 로고    scopus 로고
    • Essential PcsB putative peptidoglycan hydrolase interacts with the essential FtsXSpn cell division protein in Streptococcus pneumoniae D39
    • Sham, L.T., Barendt, S.M., Kopecky, K.E., and Winkler, M.E. (2011) Essential PcsB putative peptidoglycan hydrolase interacts with the essential FtsXSpn cell division protein in Streptococcus pneumoniae D39. Proc Natl Acad Sci USA 108: E1061-E1069.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Sham, L.T.1    Barendt, S.M.2    Kopecky, K.E.3    Winkler, M.E.4
  • 20
    • 84870185885 scopus 로고    scopus 로고
    • Three redundant murein endopeptidases catalyze an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12
    • Singh, S.K., SaiSree, L., Ravi, A.N., and Reddy, M. (2012) Three redundant murein endopeptidases catalyze an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12. Mol Microbiol 86: 1036-1051.
    • (2012) Mol Microbiol , vol.86 , pp. 1036-1051
    • Singh, S.K.1    SaiSree, L.2    Ravi, A.N.3    Reddy, M.4
  • 21
    • 77953265009 scopus 로고    scopus 로고
    • Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization
    • Sycuro, L.K., Pincus, Z., Gutierrez, K.D., Biboy, J., Stern, C.A., Vollmer, W., and Salama, N.R. (2010) Peptidoglycan crosslinking relaxation promotes Helicobacter pylori's helical shape and stomach colonization. Cell 141: 822-833.
    • (2010) Cell , vol.141 , pp. 822-833
    • Sycuro, L.K.1    Pincus, Z.2    Gutierrez, K.D.3    Biboy, J.4    Stern, C.A.5    Vollmer, W.6    Salama, N.R.7
  • 22
    • 84861220120 scopus 로고    scopus 로고
    • Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential
    • Sycuro, L.K., Wyckoff, T.J., Biboy, J., Born, P., Pincus, Z., Vollmer, W., and Salama, N.R. (2012) Multiple peptidoglycan modification networks modulate Helicobacter pylori's cell shape, motility, and colonization potential. PLoS Pathog 8: e1002603.
    • (2012) PLoS Pathog , vol.8
    • Sycuro, L.K.1    Wyckoff, T.J.2    Biboy, J.3    Born, P.4    Pincus, Z.5    Vollmer, W.6    Salama, N.R.7
  • 23
    • 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
  • 24
    • 77951470447 scopus 로고    scopus 로고
    • Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis
    • Uehara, T., Parzych, K.R., Dinh, T., and Bernhardt, T.G. (2010) Daughter cell separation is controlled by cytokinetic ring-activated cell wall hydrolysis. EMBO J 29: 1412-1422.
    • (2010) EMBO J , vol.29 , pp. 1412-1422
    • Uehara, T.1    Parzych, K.R.2    Dinh, T.3    Bernhardt, T.G.4
  • 25
    • 75349104798 scopus 로고    scopus 로고
    • Architecture of peptidoglycan: more data and more models
    • Vollmer, W., and Seligman, S.J. (2010) Architecture of peptidoglycan: more data and more models. Trends Microbiol 18: 59-66.
    • (2010) Trends Microbiol , vol.18 , pp. 59-66
    • Vollmer, W.1    Seligman, S.J.2
  • 27
    • 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
  • 28
    • 81055145336 scopus 로고    scopus 로고
    • An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring
    • Yang, D.C., Peters, N.T., Parzych, K.R., Uehara, T., Markovski, M., and Bernhardt, T.G. (2011) An ATP-binding cassette transporter-like complex governs cell-wall hydrolysis at the bacterial cytokinetic ring. Proc Natl Acad Sci USA 108: E1052-E1060.
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Yang, D.C.1    Peters, N.T.2    Parzych, K.R.3    Uehara, T.4    Markovski, M.5    Bernhardt, T.G.6
  • 29
    • 84864816426 scopus 로고    scopus 로고
    • A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division
    • Yang, D.C., Tan, K., Joachimiak, A., and Bernhardt, T.G. (2012) A conformational switch controls cell wall-remodelling enzymes required for bacterial cell division. Mol Microbiol 85: 768-781.
    • (2012) Mol Microbiol , vol.85 , pp. 768-781
    • Yang, D.C.1    Tan, K.2    Joachimiak, A.3    Bernhardt, T.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.