메뉴 건너뛰기




Volumn 71, Issue 4, 2007, Pages 884-892

Mode of action of a germination-specific cortex-lytic enzyme, SleC, of Clostridium perfringens S40

Author keywords

Bacterial spore; Clostridium perfringens; Cortex lytic enzyme; Germination

Indexed keywords

AMINO ACIDS; BACTERIA; DIGESTIVE SYSTEM; HYDROLYSIS; MASS SPECTROMETRY; PEPTIDES;

EID: 34247463427     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60511     Document Type: Article
Times cited : (31)

References (29)
  • 1
    • 0025186755 scopus 로고
    • Pulling the triggers: The mechanism of bacterial spore germination
    • Foster, S. J., and Johnstone, K., Pulling the triggers: the mechanism of bacterial spore germination. Mol. Microbiol., 4, 137-141 (1990).
    • (1990) Mol. Microbiol , vol.4 , pp. 137-141
    • Foster, S.J.1    Johnstone, K.2
  • 2
    • 0036594056 scopus 로고    scopus 로고
    • Hydrolysis of cortex peptidoglycan during bacterial spore germination
    • Makino, S., and Moriyama, R., Hydrolysis of cortex peptidoglycan during bacterial spore germination. Med. Sci. Monit., 8, RA119-127 (2002).
    • (2002) Med. Sci. Monit , vol.8
    • Makino, S.1    Moriyama, R.2
  • 3
    • 0029267226 scopus 로고
    • Purification and partial characterization of a spore cortex-lytic enzyme of Clostridium perfringens S40 spores
    • Miyata, S., Moriyama, R., Sugimoto, K., and Makino, S., Purification and partial characterization of a spore cortex-lytic enzyme of Clostridium perfringens S40 spores. Biosci. Biotechnol. Biochem., 59, 514-515 (1995).
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 514-515
    • Miyata, S.1    Moriyama, R.2    Sugimoto, K.3    Makino, S.4
  • 4
    • 0028865562 scopus 로고
    • A gene (sleC) encoding a spore cortex-lytic enzyme from Clostridium perfringens S40 spores: Cloning, sequence analysis and molecular characterization
    • Miyata, S., Moriyama, R., Miyahara, N., and Makino, S., A gene (sleC) encoding a spore cortex-lytic enzyme from Clostridium perfringens S40 spores: cloning, sequence analysis and molecular characterization. Microbiology, 141, 2643-2650 (1995).
    • (1995) Microbiology , vol.141 , pp. 2643-2650
    • Miyata, S.1    Moriyama, R.2    Miyahara, N.3    Makino, S.4
  • 5
    • 0030924599 scopus 로고    scopus 로고
    • Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene
    • Chen, Y., Miyata, S., Makino, S., and Moriyama, R., Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene. J. Bacteriol., 179, 3181-3187 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 3181-3187
    • Chen, Y.1    Miyata, S.2    Makino, S.3    Moriyama, R.4
  • 6
    • 0018712070 scopus 로고
    • Spore lytic enzyme released from Clostridium perfringens spores during germination
    • Ando, Y., Spore lytic enzyme released from Clostridium perfringens spores during germination. J. Bacteriol., 140, 59-64 (1979).
    • (1979) J. Bacteriol , vol.140 , pp. 59-64
    • Ando, Y.1
  • 7
    • 0029819171 scopus 로고    scopus 로고
    • A gene (sleB) encoding a spore cortex-lytic enzyme from Bacillus subtilis and response of the enzyme to L-alanine-mediated germination
    • Moriyama, R., Hattori, A., Miyata, S., Kudoh, S., and Makino, S., A gene (sleB) encoding a spore cortex-lytic enzyme from Bacillus subtilis and response of the enzyme to L-alanine-mediated germination. J. Bacteriol., 178, 6059-6063 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 6059-6063
    • Moriyama, R.1    Hattori, A.2    Miyata, S.3    Kudoh, S.4    Makino, S.5
  • 9
    • 0033861689 scopus 로고    scopus 로고
    • The N-terminal prepeptide is required for the production of spore cortex-lytic enzyme from its inactive precursor during germination of Clostridium perfringens S40 spores
    • Okamura, S., Urakami, K., Kimata, M., Aoshima, T., Shimamoto, S., Moriyama, R., and Makino, S., The N-terminal prepeptide is required for the production of spore cortex-lytic enzyme from its inactive precursor during germination of Clostridium perfringens S40 spores. Mol. Microbiol., 37, 821-827 (2000).
    • (2000) Mol. Microbiol , vol.37 , pp. 821-827
    • Okamura, S.1    Urakami, K.2    Kimata, M.3    Aoshima, T.4    Shimamoto, S.5    Moriyama, R.6    Makino, S.7
  • 10
    • 0034981754 scopus 로고    scopus 로고
    • Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involved in the activity
    • Shimamoto, S., Moriyama, R., Sugimoto, K., Miyata, S., and Makino, S., Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involved in the activity. J. Bacteriol., 183, 3742-3751 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 3742-3751
    • Shimamoto, S.1    Moriyama, R.2    Sugimoto, K.3    Miyata, S.4    Makino, S.5
  • 11
    • 0030875212 scopus 로고    scopus 로고
    • Localization of germination-specific spore-lytic enzymes in Clostridium perfringens S40 spores detected by immunoelectron microscopy
    • Miyata, S., Kozuka, S., Yasuda, Y., Chen, Y., Moriyama, R., Tochikubo, K., and Makino, S., Localization of germination-specific spore-lytic enzymes in Clostridium perfringens S40 spores detected by immunoelectron microscopy. FEMS Microbiol. Lett., 152, 243-247 (1997).
    • (1997) FEMS Microbiol. Lett , vol.152 , pp. 243-247
    • Miyata, S.1    Kozuka, S.2    Yasuda, Y.3    Chen, Y.4    Moriyama, R.5    Tochikubo, K.6    Makino, S.7
  • 12
    • 0029858519 scopus 로고    scopus 로고
    • Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation
    • Atrih, A., Zöllner, P., Allmaier, G., and Foster, S. J., Structural analysis of Bacillus subtilis 168 endospore peptidoglycan and its role during differentiation. J. Bacteriol., 178, 6173-6183 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 6173-6183
    • Atrih, A.1    Zöllner, P.2    Allmaier, G.3    Foster, S.J.4
  • 13
    • 0029904736 scopus 로고    scopus 로고
    • Analysis of the peptidoglycan structure of Bacillus subtilis endospores
    • Popham, D. L., Helin, J., Costello, C., and Setlow, P., Analysis of the peptidoglycan structure of Bacillus subtilis endospores. J. Bacteriol., 178, 6451-6458 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 6451-6458
    • Popham, D.L.1    Helin, J.2    Costello, C.3    Setlow, P.4
  • 15
    • 0014585139 scopus 로고
    • Structure of the peptidoglycan of bacterial spores: Occurrence of the lactam of muramic acid
    • Warth, A. D., and Strominger, J. L., Structure of the peptidoglycan of bacterial spores: occurrence of the lactam of muramic acid. Proc. Natl. Acad. Sci. USA, 64, 528-535 (1969).
    • (1969) Proc. Natl. Acad. Sci. USA , vol.64 , pp. 528-535
    • Warth, A.D.1    Strominger, J.L.2
  • 16
    • 0031754136 scopus 로고    scopus 로고
    • Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores
    • Atrih, A., Zöllner, P., Allmaier, G., Williamson, M. P., and Foster, S. J., Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores. J. Bacteriol., 180, 4603-4612 (1998).
    • (1998) J. Bacteriol , vol.180 , pp. 4603-4612
    • Atrih, A.1    Zöllner, P.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 17
    • 0033979067 scopus 로고    scopus 로고
    • Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB
    • Boland, F. M., Atrih, A., Chirakkal, H., Foster, J. F., and Moir, A., Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB. Microbiology, 146, 57-64 (2000).
    • (2000) Microbiology , vol.146 , pp. 57-64
    • Boland, F.M.1    Atrih, A.2    Chirakkal, H.3    Foster, J.F.4    Moir, A.5
  • 18
    • 0036667425 scopus 로고    scopus 로고
    • Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination
    • Chirakkal, H., O'Rouke, M., Atrih, A., Foster, S. J., and Moir, A., Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination. Microbiology, 148, 2383-2392 (2002).
    • (2002) Microbiology , vol.148 , pp. 2383-2392
    • Chirakkal, H.1    O'Rouke, M.2    Atrih, A.3    Foster, S.J.4    Moir, A.5
  • 19
    • 0034050364 scopus 로고    scopus 로고
    • Chen, Y., Fukuoka, S., and Makino, S., A novel spore peptidoglycan hydrolase of Bacillus cereus: biochemical characterization and nucleotide sequence of the corresponding gene, sleL. J. Bacteriol., 182, 1499-1506 (2000).
    • Chen, Y., Fukuoka, S., and Makino, S., A novel spore peptidoglycan hydrolase of Bacillus cereus: biochemical characterization and nucleotide sequence of the corresponding gene, sleL. J. Bacteriol., 182, 1499-1506 (2000).
  • 20
    • 0032793688 scopus 로고    scopus 로고
    • The Bacillus subtilis yaaH gene is transcribed by SigE RNA polymerase during sporulation, and its product is involved in germination of spores
    • Kodama, T., Takamatsu, H., Asai, K., Kobayashi, K., Ogasawara, N., and Watabe, K., The Bacillus subtilis yaaH gene is transcribed by SigE RNA polymerase during sporulation, and its product is involved in germination of spores. J. Bacteriol., 181, 4584-4591 (1999).
    • (1999) J. Bacteriol , vol.181 , pp. 4584-4591
    • Kodama, T.1    Takamatsu, H.2    Asai, K.3    Kobayashi, K.4    Ogasawara, N.5    Watabe, K.6
  • 21
    • 0031941630 scopus 로고    scopus 로고
    • Regulation and characterization of a newly deduced cell wall hydrolase gene (cwlJ) which affects germination of Bacillus subtilis spores
    • Ishikawa, S., Yamane, K., and Sekiguchi, J., Regulation and characterization of a newly deduced cell wall hydrolase gene (cwlJ) which affects germination of Bacillus subtilis spores. J. Bacteriol., 180, 1375-1380 (1998).
    • (1998) J. Bacteriol , vol.180 , pp. 1375-1380
    • Ishikawa, S.1    Yamane, K.2    Sekiguchi, J.3
  • 23
    • 0030731108 scopus 로고    scopus 로고
    • Kunst, F, Ogasawara, N, Moszer, I, Albertini, A. M, Alloni, G, Azevedo, V, Bertero, M. G, Bessières, P, Bolotin, A, Borchert, S, Borriss, R, Boursier, L, Brans, A, Braun, M, Brignell, S. C, Bron, S, Brouillet, S, Bruschi, C. V, Caldwell, B, Capuano, V, Carter, N. M, Choi, S.-K, Codani, J.-J, Connerton, I. F, Cummings, N. J, Daniel, R. A, Denizot, F, Devine, K. M, Düsterhöft, A, Ehrlich, S. D, Emmerson, P. T, Entian, K. D, Errington, J, Fabret, C, Ferrari, E, Foulger, D, Fritz, C, Fujita, M, Fujita, Y, Fuma, S, Galizzi, A, Galleron, N, Ghim, S.-Y, Glaser, P, Goffeau, A, Golightly, E. J, Grandi, G, Guiseppi, G, Guy, B. J, Haga, K, Haiech, J, Harwood, C. R, Hénaut, A, Hilbert, H, Holsappel, S, Hosono, S, Hullo, M.-F, Itaya, M, Jones, L, Joris, B, Karamata, D, Kasahara, Y, Klaerr-Blanchard, M, Klein, C, Kobayashi, Y, Koetter, P, Koningstein, G, Krogh, S, Kumano, M, Kurita, K, Lapidus, A, Lardinoi
    • Kunst, F., Ogasawara, N., Moszer, I., Albertini, A. M., Alloni, G., Azevedo, V., Bertero, M. G., Bessières, P., Bolotin, A., Borchert, S., Borriss, R., Boursier, L., Brans, A., Braun, M., Brignell, S. C., Bron, S., Brouillet, S., Bruschi, C. V., Caldwell, B., Capuano, V., Carter, N. M., Choi, S.-K., Codani, J.-J., Connerton, I. F., Cummings, N. J., Daniel, R. A., Denizot, F., Devine, K. M., Düsterhöft, A., Ehrlich, S. D., Emmerson, P. T., Entian, K. D., Errington, J., Fabret, C., Ferrari, E., Foulger, D., Fritz, C., Fujita, M., Fujita, Y., Fuma, S., Galizzi, A., Galleron, N., Ghim, S.-Y., Glaser, P., Goffeau, A., Golightly, E. J., Grandi, G., Guiseppi, G., Guy, B. J., Haga, K., Haiech, J., Harwood, C. R., Hénaut, A., Hilbert, H., Holsappel, S., Hosono, S., Hullo, M.-F., Itaya, M., Jones, L., Joris, B., Karamata, D., Kasahara, Y., Klaerr-Blanchard, M., Klein, C., Kobayashi, Y., Koetter, P., Koningstein, G., Krogh, S., Kumano, M., Kurita, K., Lapidus, A., Lardinois, S., Lauber, J., Lazarevic, V., Lee, S.-M., Levine, A., Liu, H., Masuda, S., Mauël, C., Médigue, C., Medina, N., Mellado, R. P., Mizuno, M., Moestl, D., Nakai, S., Noback, M., Noone, D., O'Reilly, M., Ogawa, K., Ogiwara, A., Oudega, B., Park, S.-H., Parro, V., Pohl, T. M., Portetelle, D., Porwollik, S., Prescott, A. M., Presecan, E., Pujic, P., Purnelle, B., Rapoport, G., Rey, M., Reynolds, S., Rieger, M., Rivolta, C., Rocha, E., Roche, B., Rose, M., Sadaie, Y., Sato, T., Scanlan, E., Schleich, S., Schroeter, R., Scoffone, F., Sekiguchi, J., Sekowska, A., Seror, S. J., Serror, P., Shin, B.-S., Soldo, B., Sorokin, A., Tacconi, E., Takagi, T., Takahashi, H., Takemaru, K., Takeuchi, M., Tamakoshi, A., Tanaka, T., Terpstra, P., Tognoni, A., Tosato, V., Uchiyama, S., Vandenbol, M., Vannier, F., Vassarotti, A., Viari, A., Wambutt, R., Wedler, E., Wedler, H., Weitzenegger, T., Winters, P., Wipat, A., Yamamoto, H., Yamane, K., Yasumoto, K., Yata, K., Yoshida, K., Yoshikawa, H.-F., Zumstein, E., Yoshikawa, H., and Danchin, A., The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature, 390, 249-256 (1997).
  • 24
    • 0028908856 scopus 로고    scopus 로고
    • Oshida, T., Sugai, M., Komatuzawa, H., Hong, Y.-M., Suginaka, H., and Tomasz, A., A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization. Proc. Natl. Acad. Sci. USA, 92, 285-289 (1995).
    • Oshida, T., Sugai, M., Komatuzawa, H., Hong, Y.-M., Suginaka, H., and Tomasz, A., A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization. Proc. Natl. Acad. Sci. USA, 92, 285-289 (1995).
  • 25
    • 0033026268 scopus 로고    scopus 로고
    • Multiple enzymatic activities of the murein hydrolases from Staphylococcal phage φ11
    • Navarre, W. W., Ton-That, H., Faull, K. F., and Schneewind, O., Multiple enzymatic activities of the murein hydrolases from Staphylococcal phage φ11. J. Biol. Chem., 274, 15847-15856 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 15847-15856
    • Navarre, W.W.1    Ton-That, H.2    Faull, K.F.3    Schneewind, O.4
  • 27
    • 33645090205 scopus 로고    scopus 로고
    • Muralytic activity of Micrococcus leteus Rpf and its relationship to physiological activity in promoting bacterial growth and resuscitation
    • Mujamolova, G. V., Murzin, A. G., Salina, E. G., Demina, G. R., Kell, D. B., Kaprelyants, A. S., and Young, M., Muralytic activity of Micrococcus leteus Rpf and its relationship to physiological activity in promoting bacterial growth and resuscitation. Mol. Microbiol., 59, 84-98 (2006).
    • (2006) Mol. Microbiol , vol.59 , pp. 84-98
    • Mujamolova, G.V.1    Murzin, A.G.2    Salina, E.G.3    Demina, G.R.4    Kell, D.B.5    Kaprelyants, A.S.6    Young, M.7
  • 28
    • 33744748575 scopus 로고    scopus 로고
    • Wake up! Peptidoglycan lysis and bacterial non-growth states
    • Keep, N. H., Ward, J. M., Cohen-Gonsaud, M., and Henderson, B., Wake up! Peptidoglycan lysis and bacterial non-growth states. Trends Microbiol., 14, 271-276 (2006).
    • (2006) Trends Microbiol , vol.14 , pp. 271-276
    • Keep, N.H.1    Ward, J.M.2    Cohen-Gonsaud, M.3    Henderson, B.4
  • 29
    • 0029564162 scopus 로고
    • Nucleotide sequence and regulation of a new putative cell wall hydrolase gene, cwlD, which affects germination in Bacillus subtilis
    • Sekiguchi, J., Akeo, K., Yamamoto, H., Khasanov, F. K., Alonso, J. C., and Kuroda, A., Nucleotide sequence and regulation of a new putative cell wall hydrolase gene, cwlD, which affects germination in Bacillus subtilis. J. Bacteriol., 177, 5582-5589 (1995).
    • (1995) J. Bacteriol , vol.177 , pp. 5582-5589
    • Sekiguchi, J.1    Akeo, K.2    Yamamoto, H.3    Khasanov, F.K.4    Alonso, J.C.5    Kuroda, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.