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Volumn , Issue , 2016, Pages 157-177

Spore peptidoglycan

Author keywords

Cortex lysis; Germ cell wall; GSLE; N acetylmuramic acid; Precursor; Spore peptidoglycan

Indexed keywords


EID: 85102916297     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1128/9781555819323.ch8     Document Type: Chapter
Times cited : (5)

References (136)
  • 1
    • 0036603643 scopus 로고    scopus 로고
    • Maximum shields:the assembly and function of the bacterial spore coat
    • Driks A. 2002. Maximum shields:the assembly and function of the bacterial spore coat. Trends Microbiol 10:251-254.
    • (2002) Trends Microbiol , vol.10 , pp. 251-254
    • Driks, A.1
  • 2
    • 0021213984 scopus 로고
    • Resistance, germination, and permeability correlates of Bacillus megaterium spores successively divested of integument layers
    • Koshikawa T, Beaman TC, Pankratz HS, Nakashio S, Corner TR, Gerhardt P. 1984. Resistance, germination, and permeability correlates of Bacillus megaterium spores successively divested of integument layers. J Bacteriol 159:624-632.
    • (1984) J Bacteriol , vol.159 , pp. 624-632
    • Koshikawa, T.1    Beaman, T.C.2    Pankratz, H.S.3    Nakashio, S.4    Corner, T.R.5    Gerhardt, P.6
  • 3
    • 0023035367 scopus 로고
    • Heat resistance of bacterial spores correlated with protoplast dehydration, mineralization, and thermal adaptation
    • Beaman TC, Gerhardt P. 1986. Heat resistance of bacterial spores correlated with protoplast dehydration, mineralization, and thermal adaptation. Appl Environ Microbiol 52:1242-1246.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1242-1246
    • Beaman, T.C.1    Gerhardt, P.2
  • 4
    • 0021839660 scopus 로고
    • Protoplast dehydration correlated with heat resistance of bacterial spores
    • Nakashio S, Gerhardt P. 1985. Protoplast dehydration correlated with heat resistance of bacterial spores. J Bacteriol 162:571-578.
    • (1985) J Bacteriol , vol.162 , pp. 571-578
    • Nakashio, S.1    Gerhardt, P.2
  • 5
    • 0029151295 scopus 로고
    • The Bacillus subtilis dacB gene, encoding penicillin-binding protein 5, is part of a three-gene operon required for proper spore cortex synthesis and spore core dehydration
    • Popham DL, Illades-Aguiar B, Setlow P. 1995. The Bacillus subtilis dacB gene, encoding penicillin-binding protein 5, is part of a three-gene operon required for proper spore cortex synthesis and spore core dehydration. J Bacteriol 177:4721-4729.
    • (1995) J Bacteriol , vol.177 , pp. 4721-4729
    • Popham, D.L.1    Illades-Aguiar, B.2    Setlow, P.3
  • 6
    • 33744733251 scopus 로고    scopus 로고
    • Spores of Bacillus subtilis:their resistance to and killing by radiation, heat and chemicals
    • Setlow P. 2006. Spores of Bacillus subtilis:their resistance to and killing by radiation, heat and chemicals. J Appl Microbiol 101:514-525.
    • (2006) J Appl Microbiol , vol.101 , pp. 514-525
    • Setlow, P.1
  • 7
    • 84953910824 scopus 로고    scopus 로고
    • Spore resistance properties
    • TBS-0003-2012
    • Setlow P. 2014. Spore resistance properties. Microbiol Spectrum 2(4):TBS-0003-2012. doi:10.1128/microbiolspec. TBS-0003-2012.
    • (2014) Microbiol Spectrum , vol.2 , Issue.4
    • Setlow, P.1
  • 8
    • 0030463418 scopus 로고    scopus 로고
    • Muramic lactam in peptidoglycan of Bacillus subtilis spores is required for spore outgrowth but not for spore dehydration or heat resistance
    • Popham DL, Helin J, Costello CE, Setlow P. 1996. Muramic lactam in peptidoglycan of Bacillus subtilis spores is required for spore outgrowth but not for spore dehydration or heat resistance. Proc Natl Acad Sci USA 93:15405-15410.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15405-15410
    • Popham, D.L.1    Helin, J.2    Costello, C.E.3    Setlow, P.4
  • 9
    • 0034907975 scopus 로고    scopus 로고
    • Properties of spores of Bacillus subtilis blocked at an intermediate stage in spore germination
    • Setlow B, Melly E, Setlow P. 2001. Properties of spores of Bacillus subtilis blocked at an intermediate stage in spore germination. J Bacteriol 183:4894-4899.
    • (2001) J Bacteriol , vol.183 , pp. 4894-4899
    • Setlow, B.1    Melly, E.2    Setlow, P.3
  • 10
    • 79952465087 scopus 로고    scopus 로고
    • Germination of spores of Bacillales and Clostridiales species:mechanisms and proteins involved
    • Paredes-Sabja D, Setlow P, Sarker MR. 2011. Germination of spores of Bacillales and Clostridiales species:mechanisms and proteins involved. Trends Microbiol 19:85-94.
    • (2011) Trends Microbiol , vol.19 , pp. 85-94
    • Paredes-Sabja, D.1    Setlow, P.2    Sarker, M.R.3
  • 11
    • 84865980732 scopus 로고    scopus 로고
    • Degradation of spore peptidoglycan during germination
    • In Abel-Santos E (ed), Caister Academic Press, Norwich, UK
    • Popham DL, Heffron JD, Lambert EA. 2012. Degradation of spore peptidoglycan during germination, p 121142. In Abel-Santos E (ed), Bacterial Spores:Current Research and Applications. Caister Academic Press, Norwich, UK.
    • (2012) Bacterial Spores:Current Research and Applications , pp. 121142
    • Popham, D.L.1    Heffron, J.D.2    Lambert, E.A.3
  • 12
    • 0035018011 scopus 로고    scopus 로고
    • Formation of the glycan chains in the synthesis of bacterial peptidoglycan
    • van Heijenoort J. 2001. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11:25R-36R.
    • (2001) Glycobiology , vol.11 , pp. 25R-36R
    • van Heijenoort, J.1
  • 13
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • Vollmer W. 2008. Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol Rev 32:287-306.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 14
    • 0031754136 scopus 로고    scopus 로고
    • Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores
    • Atrih A, Zöllner P, Allmaier G, Williamson MP, Foster SJ. 1998. Peptidoglycan structural dynamics during germination of Bacillus subtilis 168 endospores. J Bacteriol 180:4603-4612.
    • (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
  • 15
    • 0033891426 scopus 로고    scopus 로고
    • Structural analysis of Bacillus subtilis spore peptidoglycan during sporulation
    • Meador-Parton J, Popham DL. 2000. Structural analysis of Bacillus subtilis spore peptidoglycan during sporulation. J Bacteriol 182:4491-4499.
    • (2000) J Bacteriol , vol.182 , pp. 4491-4499
    • Meador-Parton, J.1    Popham, D.L.2
  • 16
    • 0029858519 scopus 로고    scopus 로고
    • Structural analysis of Bacillus subtilis 168 endospore pepti-doglycan and its role during differentiation
    • Atrih A, Zöllner P, Allmaier G, Foster SJ. 1996. Structural analysis of Bacillus subtilis 168 endospore pepti-doglycan and its role during differentiation. J Bacteriol 178:6173-6183.
    • (1996) J Bacteriol , vol.178 , pp. 6173-6183
    • Atrih, A.1    Zöllner, P.2    Allmaier, G.3    Foster, S.J.4
  • 17
    • 0032898033 scopus 로고    scopus 로고
    • Structural analysis of Bacillus megaterium KM spore peptidoglycan and its dynamics during germination
    • Atrih A, Bacher G, Körner R, Allmaier G, Foster SJ. 1999. Structural analysis of Bacillus megaterium KM spore peptidoglycan and its dynamics during germination. Microbiology 145:1033-1041.
    • (1999) Microbiology , vol.145 , pp. 1033-1041
    • Atrih, A.1    Bacher, G.2    Körner, R.3    Allmaier, G.4    Foster, S.J.5
  • 18
    • 0034920242 scopus 로고    scopus 로고
    • Analysis of the role of bacterial endospore cortex structure in resistance properties and demonstration of its conservation amongst species
    • Atrih A, Foster SJ. 2001. Analysis of the role of bacterial endospore cortex structure in resistance properties and demonstration of its conservation amongst species. J Appl Microbiol 91:364-372.
    • (2001) J Appl Microbiol , vol.91 , pp. 364-372
    • Atrih, A.1    Foster, S.J.2
  • 19
    • 46049095480 scopus 로고    scopus 로고
    • Cortex peptidoglycan lytic activity in germinating Bacillus anthracis spores
    • Dowd MM, Orsburn B, Popham DL. 2008. Cortex peptidoglycan lytic activity in germinating Bacillus anthracis spores. J Bacteriol 190:4541-4548.
    • (2008) J Bacteriol , vol.190 , pp. 4541-4548
    • Dowd, M.M.1    Orsburn, B.2    Popham, D.L.3
  • 20
    • 44949140751 scopus 로고    scopus 로고
    • Factors contributing to heat resistance of Clostridium perfringens endospores
    • Orsburn B, Melville SB, Popham DL. 2008. Factors contributing to heat resistance of Clostridium perfringens endospores. Appl Environ Microbiol 74:3328-3335.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 3328-3335
    • Orsburn, B.1    Melville, S.B.2    Popham, D.L.3
  • 21
    • 0002309026 scopus 로고
    • Structure of the bacterial endospore
    • In Halvorson HO, Hanson R, Campbell LL (ed), American Society for Microbiology, Washington, DC
    • Tipper DJ, Gauthier JJ. 1972. Structure of the bacterial endospore, p 3-12. In Halvorson HO, Hanson R, Campbell LL (ed), Spores V. American Society for Microbiology, Washington, DC.
    • (1972) Spores V , pp. 3-12
    • Tipper, D.J.1    Gauthier, J.J.2
  • 22
    • 0014585139 scopus 로고
    • Structure of the pepti-doglycan of bacterial spores:occurrence of the lactam of muramic acid
    • Warth AD, Strominger JL. 1969. Structure of the pepti-doglycan of bacterial spores:occurrence of the lactam of muramic acid. Proc Natl Acad Sci USA 64:528-535.
    • (1969) Proc Natl Acad Sci USA , vol.64 , pp. 528-535
    • Warth, A.D.1    Strominger, J.L.2
  • 23
    • 0017225072 scopus 로고
    • Distribution of peptido-glycan synthetase activities between sporangia and forespores in sporulating cells of Bacillus sphaericus
    • Tipper DJ, Linnett PE. 1976. Distribution of peptido-glycan synthetase activities between sporangia and forespores in sporulating cells of Bacillus sphaericus. J Bacteriol 126:213-221.
    • (1976) J Bacteriol , vol.126 , pp. 213-221
    • Tipper, D.J.1    Linnett, P.E.2
  • 24
    • 0015502657 scopus 로고
    • Structure of the pepti-doglycan from spores of Bacillus subtilis
    • Warth AD, Strominger JL. 1972. Structure of the pepti-doglycan from spores of Bacillus subtilis. Biochemistry 11:1389-1396.
    • (1972) Biochemistry , vol.11 , pp. 1389-1396
    • Warth, A.D.1    Strominger, J.L.2
  • 27
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih A, Bacher G, Allmaier G, Williamson MP, Foster SJ. 1999. Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J Bacteriol 181:3956-3966.
    • (1999) J Bacteriol , vol.181 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 28
    • 0015237808 scopus 로고
    • Structure of the peptidoglycan from vegetative cell walls of Bacillus subtilis
    • Warth AD, Strominger JL. 1971. Structure of the peptidoglycan from vegetative cell walls of Bacillus subtilis. Biochemistry 10:4349-4358.
    • (1971) Biochemistry , vol.10 , pp. 4349-4358
    • Warth, A.D.1    Strominger, J.L.2
  • 29
    • 0032932349 scopus 로고    scopus 로고
    • Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties
    • Popham DL, Gilmore ME, Setlow P. 1999. Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties. J Bacteriol 181:126-132.
    • (1999) J Bacteriol , vol.181 , pp. 126-132
    • Popham, D.L.1    Gilmore, M.E.2    Setlow, P.3
  • 30
    • 0017070174 scopus 로고
    • Relationship between cortex content and properties of Bacillus sphaericus spores
    • Imae Y, Strominger JL. 1976. Relationship between cortex content and properties of Bacillus sphaericus spores. J Bacteriol 126:907-913.
    • (1976) J Bacteriol , vol.126 , pp. 907-913
    • Imae, Y.1    Strominger, J.L.2
  • 31
    • 0020286697 scopus 로고
    • Bacterial spore heat resistance correlated with water content, wet density, and protoplast/ sporoplast volume ratio
    • Beaman TC, Greenamyre JT, Corner TR, Pankratz HS, Gerhardt P. 1982. Bacterial spore heat resistance correlated with water content, wet density, and protoplast/ sporoplast volume ratio. J Bacteriol 150:870-877.
    • (1982) J Bacteriol , vol.150 , pp. 870-877
    • Beaman, T.C.1    Greenamyre, J.T.2    Corner, T.R.3    Pankratz, H.S.4    Gerhardt, P.5
  • 32
    • 0037701542 scopus 로고    scopus 로고
    • Characterization of LytH, a differentiation-associated peptidoglycan hydrolase of Bacillus subtilis involved in endospore cortex maturation
    • Horsburgh GJ, Atrih A, Foster SJ. 2003. Characterization of LytH, a differentiation-associated peptidoglycan hydrolase of Bacillus subtilis involved in endospore cortex maturation. J Bacteriol 185:3813-3820.
    • (2003) J Bacteriol , vol.185 , pp. 3813-3820
    • Horsburgh, G.J.1    Atrih, A.2    Foster, S.J.3
  • 33
    • 0029904736 scopus 로고    scopus 로고
    • Analysis of the peptidoglycan structure of Bacillus subtilis endospores
    • Popham DL, Helin J, Costello CE, Setlow P. 1996. Analysis of the peptidoglycan structure of Bacillus subtilis endospores. J Bacteriol 178:6451-6458.
    • (1996) J Bacteriol , vol.178 , pp. 6451-6458
    • Popham, D.L.1    Helin, J.2    Costello, C.E.3    Setlow, P.4
  • 34
    • 0032819206 scopus 로고    scopus 로고
    • Spore peptidoglycan structure in a cwlD dacB double mutant of Bacillus subtilis
    • Popham DL, Meador-Parton J, Costello CE, Setlow P. 1999. Spore peptidoglycan structure in a cwlD dacB double mutant of Bacillus subtilis. J Bacteriol 181:6205-6209.
    • (1999) J Bacteriol , vol.181 , pp. 6205-6209
    • Popham, D.L.1    Meador-Parton, J.2    Costello, C.E.3    Setlow, P.4
  • 35
    • 0014711579 scopus 로고
    • Electromechanical interactions in cell walls of gram-positive cocci
    • Ou L-T, Marquis RE. 1970. Electromechanical interactions in cell walls of gram-positive cocci. J Bacteriol 101:92-101.
    • (1970) J Bacteriol , vol.101 , pp. 92-101
    • Ou, L.-T.1    Marquis, R.E.2
  • 36
    • 0000383219 scopus 로고
    • Water permeability of bacterial spores and the concept of a contractile cortex
    • Lewis JC, Snell NS, Burr HK. 1960. Water permeability of bacterial spores and the concept of a contractile cortex. Science 132:544-545.
    • (1960) Science , vol.132 , pp. 544-545
    • Lewis, J.C.1    Snell, N.S.2    Burr, H.K.3
  • 37
    • 0001427470 scopus 로고
    • Mechanisms of heat resistance
    • In Dring GJ, Ellar DJ, Gould GW (ed), Academic Press, Inc, London, UK
    • Warth AD. 1985. Mechanisms of heat resistance, p 209225. In Dring GJ, Ellar DJ, Gould GW (ed), Fundamental and Applied Aspects of Bacterial Spores. Academic Press, Inc, London, UK.
    • (1985) Fundamental and Applied Aspects of Bacterial Spores , pp. 209225
    • Warth, A.D.1
  • 38
    • 0037452969 scopus 로고    scopus 로고
    • Kinetics of size changes of individual Bacillus thurin-giensis spores in response to changes in relative humidity
    • Westphal AJ, Price PB, Leighton TJ, Wheeler KE. 2003. Kinetics of size changes of individual Bacillus thurin-giensis spores in response to changes in relative humidity. Proc Natl Acad Sci USA 100:3461-3466.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3461-3466
    • Westphal, A.J.1    Price, P.B.2    Leighton, T.J.3    Wheeler, K.E.4
  • 39
    • 84862907855 scopus 로고    scopus 로고
    • Effects of cortex peptidoglycan structure and cortex hydrolysis on the kinetics of Ca(2+)-dipicolinic acid release during Bacillus subtilis spore germination
    • Zhang P, Thomas S, Li YQ, Setlow P. 2012. Effects of cortex peptidoglycan structure and cortex hydrolysis on the kinetics of Ca(2+)-dipicolinic acid release during Bacillus subtilis spore germination. J Bacteriol 194:646-652.
    • (2012) J Bacteriol , vol.194 , pp. 646-652
    • Zhang, P.1    Thomas, S.2    Li, Y.Q.3    Setlow, P.4
  • 40
    • 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 FK, Alonso JC, Kuroda A. 1995. 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) 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
  • 41
    • 0015385521 scopus 로고
    • Appearance of muramic lactam during cortex synthesis in sporulating cultures of Bacillus cereus and Bacillus megaterium
    • Wickus GG, Warth AD, Strominger JL. 1972. Appearance of muramic lactam during cortex synthesis in sporulating cultures of Bacillus cereus and Bacillus megaterium. J Bacteriol 111:625-627.
    • (1972) J Bacteriol , vol.111 , pp. 625-627
    • Wickus, G.G.1    Warth, A.D.2    Strominger, J.L.3
  • 42
    • 33947252355 scopus 로고    scopus 로고
    • Engulfment during sporulation in Bacillus subtilis is governed by a multi-protein complex containing tandemly acting autolysins
    • Chastanet A, Losick R. 2007. Engulfment during sporulation in Bacillus subtilis is governed by a multi-protein complex containing tandemly acting autolysins. Mol Microbiol 64:139-152.
    • (2007) Mol Microbiol , vol.64 , pp. 139-152
    • Chastanet, A.1    Losick, R.2
  • 43
    • 77952224336 scopus 로고    scopus 로고
    • SpoIID-mediated peptidoglycan degradation is required throughout en-gulfment during Bacillus subtilis sporulation
    • Gutierrez J, Smith R, Pogliano K. 2010. SpoIID-mediated peptidoglycan degradation is required throughout en-gulfment during Bacillus subtilis sporulation. J Bacteriol 192:3174-3186.
    • (2010) J Bacteriol , vol.192 , pp. 3174-3186
    • Gutierrez, J.1    Smith, R.2    Pogliano, K.3
  • 44
    • 76749120537 scopus 로고    scopus 로고
    • A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis
    • Morlot C, Uehara T, Marquis KA, Bernhardt TG, Rudner DZ. 2010. A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis. Genes Dev 24:411-422.
    • (2010) Genes Dev , vol.24 , pp. 411-422
    • Morlot, C.1    Uehara, T.2    Marquis, K.A.3    Bernhardt, T.G.4    Rudner, D.Z.5
  • 45
    • 77952161340 scopus 로고    scopus 로고
    • Cell wall synthesis is necessary for membrane dynamics during sporulation of Bacillus subtilis
    • Meyer P, Gutierrez J, Pogliano K, Dworkin J. 2010. Cell wall synthesis is necessary for membrane dynamics during sporulation of Bacillus subtilis. Mol Microbiol 76:956-970.
    • (2010) Mol Microbiol , vol.76 , pp. 956-970
    • Meyer, P.1    Gutierrez, J.2    Pogliano, K.3    Dworkin, J.4
  • 47
    • 84952322198 scopus 로고    scopus 로고
    • Protein targeting during Bacillus subtilis sporulation
    • TBS-0006-2013
    • Dworkin J. 2014. Protein targeting during Bacillus subtilis sporulation. Microbiol Spectrum 2(1):TBS-0006-2013. doi:10.1128/microbiolspec.TBS-0006-2013.
    • (2014) Microbiol Spectrum , vol.2 , Issue.1
    • Dworkin, J.1
  • 48
    • 0034603830 scopus 로고    scopus 로고
    • Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis
    • Pedersen LB, Ragkousi K, Cammett TJ, Melly E, Sekowska A, Schopick E, Murray T, Setlow P. 2000. Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis. Gene 246:187-196.
    • (2000) Gene , vol.246 , pp. 187-196
    • Pedersen, L.B.1    Ragkousi, K.2    Cammett, T.J.3    Melly, E.4    Sekowska, A.5    Schopick, E.6    Murray, T.7    Setlow, P.8
  • 49
    • 0027203788 scopus 로고
    • Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class A high-molecular-weight penicillin-binding protein
    • Popham DL, Setlow P. 1993. Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpF gene, which codes for a putative class A high-molecular-weight penicillin-binding protein. J Bacteriol 175:48704876.
    • (1993) J Bacteriol , vol.175 , pp. 48704876
    • Popham, D.L.1    Setlow, P.2
  • 50
    • 34548358987 scopus 로고    scopus 로고
    • Spore cortex formation in Bacillus subtilis is regulated by accumulation of peptidoglycan precursors under the control of sigma K
    • Vasudevan P, Weaver A, Reichert ED, Linnstaedt SD, Popham DL. 2007. Spore cortex formation in Bacillus subtilis is regulated by accumulation of peptidoglycan precursors under the control of sigma K. Mol Microbiol 65:1582-1594.
    • (2007) Mol Microbiol , vol.65 , pp. 1582-1594
    • Vasudevan, P.1    Weaver, A.2    Reichert, E.D.3    Linnstaedt, S.D.4    Popham, D.L.5
  • 51
    • 0021029204 scopus 로고
    • Stability and synthesis of the penicillin-binding proteins during sporulation
    • Buchanan CE, Sowell MO. 1983. Stability and synthesis of the penicillin-binding proteins during sporulation. J Bacteriol 156:545-551.
    • (1983) J Bacteriol , vol.156 , pp. 545-551
    • Buchanan, C.E.1    Sowell, M.O.2
  • 52
    • 0034816354 scopus 로고    scopus 로고
    • Two class A high-molecular-weight penicillin-binding proteins of Bacillus subtilis play redundant roles in sporulation
    • McPherson DC, Driks A, Popham DL. 2001. Two class A high-molecular-weight penicillin-binding proteins of Bacillus subtilis play redundant roles in sporulation. J Bacteriol 183:6046-6053.
    • (2001) J Bacteriol , vol.183 , pp. 6046-6053
    • McPherson, D.C.1    Driks, A.2    Popham, D.L.3
  • 53
    • 0028104377 scopus 로고
    • Cloning, nucleotide sequence, mutagenesis, and mapping of the Bacillus subtilis pbpD gene, which codes for penicillin-binding protein 4
    • Popham DL, Setlow P. 1994. Cloning, nucleotide sequence, mutagenesis, and mapping of the Bacillus subtilis pbpD gene, which codes for penicillin-binding protein 4. J Bacteriol 176:7197-7205.
    • (1994) J Bacteriol , vol.176 , pp. 7197-7205
    • Popham, D.L.1    Setlow, P.2
  • 54
    • 0028835462 scopus 로고
    • Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-related factor
    • Popham DL, Setlow P. 1995. Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-related factor. J Bacteriol 177:326335.
    • (1995) J Bacteriol , vol.177 , pp. 326335
    • Popham, D.L.1    Setlow, P.2
  • 55
    • 0020558202 scopus 로고
    • Changes in penicillinbinding proteins during sporulation of Bacillus subtilis
    • Sowell MO, Buchanan CE. 1983. Changes in penicillinbinding proteins during sporulation of Bacillus subtilis. J Bacteriol 153:1331-1337.
    • (1983) J Bacteriol , vol.153 , pp. 1331-1337
    • Sowell, M.O.1    Buchanan, C.E.2
  • 56
    • 0037315095 scopus 로고    scopus 로고
    • Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis
    • McPherson DC, Popham DL. 2003. Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis. J Bacteriol 185:1423-1431.
    • (2003) J Bacteriol , vol.185 , pp. 1423-1431
    • McPherson, D.C.1    Popham, D.L.2
  • 57
    • 0028011141 scopus 로고
    • The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis
    • Daniel RA, Drake S, Buchanan CE, Scholle R, Errington J. 1994. The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis. J Mol Biol 235:209-220.
    • (1994) J Mol Biol , vol.235 , pp. 209-220
    • Daniel, R.A.1    Drake, S.2    Buchanan, C.E.3    Scholle, R.4    Errington, J.5
  • 58
    • 77954763191 scopus 로고    scopus 로고
    • Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation
    • Fay A, Meyer P, Dworkin J. 2010. Interactions between late-acting proteins required for peptidoglycan synthesis during sporulation. J Mol Biol 399:547-561.
    • (2010) J Mol Biol , vol.399 , pp. 547-561
    • Fay, A.1    Meyer, P.2    Dworkin, J.3
  • 59
    • 84881372843 scopus 로고    scopus 로고
    • Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD
    • Bukowska-Faniband E, Hederstedt L. 2013. Cortex synthesis during Bacillus subtilis sporulation depends on the transpeptidase activity of SpoVD. FEMS Microbiol Lett 346:65-72.
    • (2013) FEMS Microbiol Lett , vol.346 , pp. 65-72
    • Bukowska-Faniband, E.1    Hederstedt, L.2
  • 60
    • 0024439301 scopus 로고
    • Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively
    • Ikeda M, Sato T, Wachi M, Jung HK, Ishino F, Kobayashi Y, Matsuhashi M. 1989. Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. J Bacteriol 171:6375-6378.
    • (1989) J Bacteriol , vol.171 , pp. 6375-6378
    • Ikeda, M.1    Sato, T.2    Wachi, M.3    Jung, H.K.4    Ishino, F.5    Kobayashi, Y.6    Matsuhashi, M.7
  • 61
    • 0025346860 scopus 로고
    • The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures
    • Joris B, Dive G, Henriques A, Piggot PJ, Ghuysen JM. 1990. The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures. Mol Microbiol 4:513-517.
    • (1990) Mol Microbiol , vol.4 , pp. 513-517
    • Joris, B.1    Dive, G.2    Henriques, A.3    Piggot, P.J.4    Ghuysen, J.M.5
  • 62
    • 0026345897 scopus 로고
    • Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis
    • Popham DL, Stragier P. 1991. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. J Bacteriol 173:7942-7949.
    • (1991) J Bacteriol , vol.173 , pp. 7942-7949
    • Popham, D.L.1    Stragier, P.2
  • 63
    • 70349130412 scopus 로고    scopus 로고
    • Homologues of the Bacillus subtilis SpoVB protein are involved in cell wall metabolism
    • Vasudevan P, McElligott J, Attkisson C, Betteken M, Popham DL. 2009. Homologues of the Bacillus subtilis SpoVB protein are involved in cell wall metabolism. J Bacteriol 191:6012-6019.
    • (2009) J Bacteriol , vol.191 , pp. 6012-6019
    • Vasudevan, P.1    McElligott, J.2    Attkisson, C.3    Betteken, M.4    Popham, D.L.5
  • 64
    • 0015524239 scopus 로고
    • Five penicillinbinding components occur in Bacillus subtilis membranes
    • Blumberg PM, Strominger JL. 1972. Five penicillinbinding components occur in Bacillus subtilis membranes. J Biol Chem 247:8107-8113.
    • (1972) J Biol Chem , vol.247 , pp. 8107-8113
    • Blumberg, P.M.1    Strominger, J.L.2
  • 65
    • 0020576536 scopus 로고
    • Differential expression of penicillin-binding protein structural genes during Bacillus subtilis sporulation
    • Todd JA, Bone EJ, Piggot PJ, Ellar DJ. 1983. Differential expression of penicillin-binding protein structural genes during Bacillus subtilis sporulation. FEMS Microbiol Lett 18:197-202.
    • (1983) FEMS Microbiol Lett , vol.18 , pp. 197-202
    • Todd, J.A.1    Bone, E.J.2    Piggot, P.J.3    Ellar, D.J.4
  • 66
    • 0027959484 scopus 로고
    • Transcriptional control of dacB, which encodes a major sporulation-specific penicillin-binding protein
    • Simpson EB, Hancock TW, Buchanan CE. 1994. Transcriptional control of dacB, which encodes a major sporulation-specific penicillin-binding protein. J Bacte-riol 176:7767-7769.
    • (1994) J Bacte-riol , vol.176 , pp. 7767-7769
    • Simpson, E.B.1    Hancock, T.W.2    Buchanan, C.E.3
  • 67
    • 0026634121 scopus 로고
    • Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase sigma factor and for a putative DD-carboxypeptidase
    • Wu J-J, Schuch R, Piggot PJ. 1992. Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase sigma factor and for a putative DD-carboxypeptidase. J Bacteriol 174:48854892.
    • (1992) J Bacteriol , vol.174 , pp. 48854892
    • Wu, J.-J.1    Schuch, R.2    Piggot, P.J.3
  • 68
    • 0036837769 scopus 로고    scopus 로고
    • A polysaccharide deacetylase gene (pdaA) is required for germination and for production of muramic delta-lactam residues in the spore cortex of Bacillus subtilis
    • Fukushima T, Yamamoto H, Atrih A, Foster SJ, Sekiguchi J. 2002. A polysaccharide deacetylase gene (pdaA) is required for germination and for production of muramic delta-lactam residues in the spore cortex of Bacillus subtilis. J Bacteriol 184:6007-6015.
    • (2002) J Bacteriol , vol.184 , pp. 6007-6015
    • Fukushima, T.1    Yamamoto, H.2    Atrih, A.3    Foster, S.J.4    Sekiguchi, J.5
  • 70
    • 84958765816 scopus 로고    scopus 로고
    • Genome diversity of spore-forming firmicutes
    • TBS-0015-2012
    • Galperin MY. 2013. Genome diversity of spore-forming firmicutes. Microbiol Spectrum 1(2):TBS-0015-2012. doi:10.1128/microbiolspectrum.TBS-0015-2012.
    • (2013) Microbiol Spectrum , vol.1 , Issue.2
    • Galperin, M.Y.1
  • 71
    • 37349041697 scopus 로고    scopus 로고
    • Lipid intermediates in the biosynthesis of bacterial peptidoglycan
    • van Heijenoort J. 2007. Lipid intermediates in the biosynthesis of bacterial peptidoglycan. Microbiol Mol Biol Rev 71:620-635.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 620-635
    • van Heijenoort, J.1
  • 72
    • 0020987521 scopus 로고
    • The surface stress theory of microbial morphogenesis
    • Koch AL. 1983. The surface stress theory of microbial morphogenesis. Adv Microb Physiol 24:301-366.
    • (1983) Adv Microb Physiol , vol.24 , pp. 301-366
    • Koch, A.L.1
  • 73
    • 0036594056 scopus 로고    scopus 로고
    • Hydrolysis of cortex peptidoglycan during bacterial spore germination
    • Makino S, Moriyama R. 2002. Hydrolysis of cortex peptidoglycan during bacterial spore germination. Med Sci Monit 8:RA119-RA127.
    • (2002) Med Sci Monit , vol.8 , pp. RA119-RA127
    • Makino, S.1    Moriyama, R.2
  • 74
    • 0036667425 scopus 로고    scopus 로고
    • Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination
    • Chirakkal H, O'Rourke M, Atrih A, Foster SJ, Moir A. 2002. Analysis of spore cortex lytic enzymes and related proteins in Bacillus subtilis endospore germination. Microbiology 148:2383-2392.
    • (2002) Microbiology , vol.148 , pp. 2383-2392
    • Chirakkal, H.1    O'Rourke, M.2    Atrih, A.3    Foster, S.J.4    Moir, A.5
  • 75
    • 0034050364 scopus 로고    scopus 로고
    • A novel spore peptidoglycan hydrolase of Bacillus cereus:biochemical characterization and nucleotide sequence of the corresponding gene, sleL
    • Chen Y, Fukuoka S, Makino S. 2000. A novel spore peptidoglycan hydrolase of Bacillus cereus:biochemical characterization and nucleotide sequence of the corresponding gene, sleL. J Bacteriol 182:1499-1506.
    • (2000) J Bacteriol , vol.182 , pp. 1499-1506
    • Chen, Y.1    Fukuoka, S.2    Makino, S.3
  • 76
    • 66849118916 scopus 로고    scopus 로고
    • Characterization of the germination of Bacillus megaterium spores lacking enzymes that degrade the spore cortex
    • Setlow B, Peng L, Loshon CA, Li Y-Q, Christie G, Setlow P. 2009. Characterization of the germination of Bacillus megaterium spores lacking enzymes that degrade the spore cortex. J Appl Microbiol 107:318-328.
    • (2009) J Appl Microbiol , vol.107 , pp. 318-328
    • Setlow, B.1    Peng, L.2    Loshon, C.A.3    Li, Y.-Q.4    Christie, G.5    Setlow, P.6
  • 77
    • 64049117377 scopus 로고    scopus 로고
    • Roles of germination-specific lytic enzymes CwlJ and SleB in Bacillus anthracis
    • Heffron JD, Orsburn B, Popham DL. 2009. Roles of germination-specific lytic enzymes CwlJ and SleB in Bacillus anthracis. J Bacteriol 191:2237-2247.
    • (2009) J Bacteriol , vol.191 , pp. 2237-2247
    • Heffron, J.D.1    Orsburn, B.2    Popham, D.L.3
  • 78
    • 69949106986 scopus 로고    scopus 로고
    • The germination-specific lytic enzymes SleB, CwlJ1, and CwlJ2 each contribute to Bacillus anthracis spore germination and virulence
    • Giebel JD, Carr KA, Anderson EC, Hanna PC. 2009. The germination-specific lytic enzymes SleB, CwlJ1, and CwlJ2 each contribute to Bacillus anthracis spore germination and virulence. J Bacteriol 191:5569-5576.
    • (2009) J Bacteriol , vol.191 , pp. 5569-5576
    • Giebel, J.D.1    Carr, K.A.2    Anderson, E.C.3    Hanna, P.C.4
  • 79
    • 75149124883 scopus 로고    scopus 로고
    • Contributions of four cortex lytic enzymes to germination of Bacillus anthracis spores
    • Heffron JD, Lambert EA, Sherry N, Popham DL. 2010. Contributions of four cortex lytic enzymes to germination of Bacillus anthracis spores. J Bacteriol 192:763770.
    • (2010) J Bacteriol , vol.192 , pp. 763770
    • Heffron, J.D.1    Lambert, E.A.2    Sherry, N.3    Popham, D.L.4
  • 80
    • 0034896712 scopus 로고    scopus 로고
    • Genetic requirements for induction of germination of spores of Bacillus subtilis by Ca(2+)-dipicolinate
    • Paidhungat M, Ragkousi K, Setlow P. 2001. Genetic requirements for induction of germination of spores of Bacillus subtilis by Ca(2+)-dipicolinate. J Bacteriol 183:4886-4893.
    • (2001) J Bacteriol , vol.183 , pp. 4886-4893
    • Paidhungat, M.1    Ragkousi, K.2    Setlow, P.3
  • 81
    • 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, Sekiguchi J. 1998. 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) J Bacteriol , vol.180 , pp. 1375-1380
    • Ishikawa, S.1    Yamane, K.2    Sekiguchi, J.3
  • 82
    • 0033979067 scopus 로고    scopus 로고
    • Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB
    • Boland FM, Atrih A, Chirakkal H, Foster SJ, Moir A. 2000. Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB. Microbiology 146:57-64.
    • (2000) Microbiology , vol.146 , pp. 57-64
    • Boland, F.M.1    Atrih, A.2    Chirakkal, H.3    Foster, S.J.4    Moir, A.5
  • 83
    • 0032931055 scopus 로고    scopus 로고
    • Expression of a germination-specific amidase, SleB, of bacilli in the forespore compartment of sporulating cells and its localization on the exterior side of the cortex in dormant spores
    • Moriyama R, Fukuoka H, Miyata S, Kudoh S, Hattori A, Kozuka S, Yasuda Y, Tochikubo K, Makino S. 1999. Expression of a germination-specific amidase, SleB, of bacilli in the forespore compartment of sporulating cells and its localization on the exterior side of the cortex in dormant spores. J Bacteriol 181:2373-2378.
    • (1999) J Bacteriol , vol.181 , pp. 2373-2378
    • Moriyama, R.1    Fukuoka, H.2    Miyata, S.3    Kudoh, S.4    Hattori, A.5    Kozuka, S.6    Yasuda, Y.7    Tochikubo, K.8    Makino, S.9
  • 84
    • 0032496659 scopus 로고    scopus 로고
    • Characterization of yhcN, a new forespore-specific gene of Bacillus subtilis
    • Bagyan I, Noback M, Bron S, Paidhungat M, Setlow P. 1998. Characterization of yhcN, a new forespore-specific gene of Bacillus subtilis. Gene 212:179-188.
    • (1998) Gene , vol.212 , pp. 179-188
    • Bagyan, I.1    Noback, M.2    Bron, S.3    Paidhungat, M.4    Setlow, P.5
  • 86
    • 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, Makino S. 1996. 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) J Bacteriol , vol.178 , pp. 6059-6063
    • Moriyama, R.1    Hattori, A.2    Miyata, S.3    Kudoh, S.4    Makino, S.5
  • 87
    • 0029832937 scopus 로고    scopus 로고
    • A germination-specific spore cortex-lytic enzyme from Bacillus cereus spores:cloning and sequencing of the gene and molecular characterization of the enzyme
    • Moriyama R, Kudoh S, Miyata S, Nonobe S, Hattori A, Makino S. 1996. A germination-specific spore cortex-lytic enzyme from Bacillus cereus spores:cloning and sequencing of the gene and molecular characterization of the enzyme. J Bacteriol 178:5330-5332.
    • (1996) J Bacteriol , vol.178 , pp. 5330-5332
    • Moriyama, R.1    Kudoh, S.2    Miyata, S.3    Nonobe, S.4    Hattori, A.5    Makino, S.6
  • 88
    • 33947408762 scopus 로고    scopus 로고
    • Cloning and identification of a gene encoding spore cortex-lytic enzyme in Bacillus thuringiensis
    • Hu K, Yang H, Liu G, Tan H. 2007. Cloning and identification of a gene encoding spore cortex-lytic enzyme in Bacillus thuringiensis. Curr Microbiol 54:292-295.
    • (2007) Curr Microbiol , vol.54 , pp. 292-295
    • Hu, K.1    Yang, H.2    Liu, G.3    Tan, H.4
  • 89
    • 78650122220 scopus 로고    scopus 로고
    • In vitro studies of peptidoglycan binding and hydrolysis by the Bacillus anthracis germination-specific lytic enzyme SleB
    • Heffron JD, Sherry N, Popham DL. 2011. In vitro studies of peptidoglycan binding and hydrolysis by the Bacillus anthracis germination-specific lytic enzyme SleB. J Bacteriol 193:125-131.
    • (2011) J Bacteriol , vol.193 , pp. 125-131
    • Heffron, J.D.1    Sherry, N.2    Popham, D.L.3
  • 90
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis:a genome-based survey of the secretome
    • Tjalsma H, Bolhuis A, Jongbloed JDH, Bron S, van Dijl JM. 2000. Signal peptide-dependent protein transport in Bacillus subtilis:a genome-based survey of the secretome. Microbiol Mol Biol Rev 64:515-547.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.H.3    Bron, S.4    van Dijl, J.M.5
  • 91
    • 0035164263 scopus 로고    scopus 로고
    • In vivo roles of the germination-specific lytic enzymes of Bacillus subtilis 168
    • Atrih A, Foster SJ. 2001. In vivo roles of the germination-specific lytic enzymes of Bacillus subtilis 168. Microbiology 147:2925-2932.
    • (2001) Microbiology , vol.147 , pp. 2925-2932
    • Atrih, A.1    Foster, S.J.2
  • 92
    • 33747187232 scopus 로고    scopus 로고
    • Subcellular localization of a germiantion-specific cortex-lytic enzyme, SleB, of bacilli during sporulation
    • Masayama A, Fukuoka H, Kato S, Yoshimura T, Moriyama M, Moriyama R. 2006. Subcellular localization of a germiantion-specific cortex-lytic enzyme, SleB, of bacilli during sporulation. Genes Genet syst 81:163-169.
    • (2006) Genes Genet syst , vol.81 , pp. 163-169
    • Masayama, A.1    Fukuoka, H.2    Kato, S.3    Yoshimura, T.4    Moriyama, M.5    Moriyama, R.6
  • 93
    • 84877947352 scopus 로고    scopus 로고
    • Activity and regulation of various forms of CwlJ, SleB, and YpeB proteins in degrading cortex peptidoglycan of spores of Bacillus species in vitro and during spore germination
    • Li Y, Butzin XY, Davis A, Setlow B, Korza G, Üstok FI, Christie G, Setlow P, Hao B. 2013. Activity and regulation of various forms of CwlJ, SleB, and YpeB proteins in degrading cortex peptidoglycan of spores of Bacillus species in vitro and during spore germination. J Bacte-riol 195:2530-2540.
    • (2013) J Bacte-riol , vol.195 , pp. 2530-2540
    • Li, Y.1    Butzin, X.Y.2    Davis, A.3    Setlow, B.4    Korza, G.5    Üstok, F.I.6    Christie, G.7    Setlow, P.8    Hao, B.9
  • 94
    • 77957853839 scopus 로고    scopus 로고
    • Mutational analysis of Bacillus megaterium QM B1551 cortex-lytic enzymes
    • Christie G, Üstok FI, Lu Q, Packman LC, Lowe CR. 2010. Mutational analysis of Bacillus megaterium QM B1551 cortex-lytic enzymes. J Bacteriol 192:5378-5389.
    • (2010) J Bacteriol , vol.192 , pp. 5378-5389
    • Christie, G.1    Üstok, F.I.2    Lu, Q.3    Packman, L.C.4    Lowe, C.R.5
  • 95
    • 84907016410 scopus 로고    scopus 로고
    • Role of YpeB in cortex hydrolysis during germination of Bacillus anthracis spores
    • Bernhards CB, Popham DL. 2014. Role of YpeB in cortex hydrolysis during germination of Bacillus anthracis spores. J Bacteriol 196:3399-3409.
    • (2014) J Bacteriol , vol.196 , pp. 3399-3409
    • Bernhards, C.B.1    Popham, D.L.2
  • 96
    • 0028282964 scopus 로고
    • A spore-lytic enzyme released from Bacillus cereus spores during germination
    • Makino S, Ito N, Inoue T, Miyata S, Moriyama R. 1994. A spore-lytic enzyme released from Bacillus cereus spores during germination. Microbiology 140:1403-1410.
    • (1994) Microbiology , vol.140 , pp. 1403-1410
    • Makino, S.1    Ito, N.2    Inoue, T.3    Miyata, S.4    Moriyama, R.5
  • 97
    • 84919632585 scopus 로고    scopus 로고
    • HtrC is involved in proteolysis of YpeB during germination of Bacillus anthracis and Bacillus subtilis spores
    • Bernhards CB, Chen Y, Toutkoushian H, Popham DL. 2015. HtrC is involved in proteolysis of YpeB during germination of Bacillus anthracis and Bacillus subtilis spores. J Bacteriol 197:326-336.
    • (2015) J Bacteriol , vol.197 , pp. 326-336
    • Bernhards, C.B.1    Chen, Y.2    Toutkoushian, H.3    Popham, D.L.4
  • 98
    • 0037378730 scopus 로고    scopus 로고
    • Identification of a new gene essential for germination of Bacillus subtilis spores with Ca2+-dipicolinate
    • Ragkousi K, Eichenberger P, van Ooij C, Setlow P. 2003. Identification of a new gene essential for germination of Bacillus subtilis spores with Ca2+-dipicolinate. J Bacteriol 185:2315-2329.
    • (2003) J Bacteriol , vol.185 , pp. 2315-2329
    • Ragkousi, K.1    Eichenberger, P.2    van Ooij, C.3    Setlow, P.4
  • 99
    • 0036068690 scopus 로고    scopus 로고
    • Germination of Bacillus cereus spores in response to L-alanine and to inosine:the roles of gerL and gerQ operons
    • Barlass PJ, Houston CW, Clements MO, Moir A. 2002. Germination of Bacillus cereus spores in response to L-alanine and to inosine:the roles of gerL and gerQ operons. Microbiology 148:2089-2095.
    • (2002) Microbiology , vol.148 , pp. 2089-2095
    • Barlass, P.J.1    Houston, C.W.2    Clements, M.O.3    Moir, A.4
  • 100
    • 0036152303 scopus 로고    scopus 로고
    • Localization of the cortex lytic enzyme CwlJ in spores of Bacillus subtilis
    • Bagyan I, Setlow P. 2002. Localization of the cortex lytic enzyme CwlJ in spores of Bacillus subtilis. J Bacteriol 184:1219-1224.
    • (2002) J Bacteriol , vol.184 , pp. 1219-1224
    • Bagyan, I.1    Setlow, P.2
  • 101
    • 84855804122 scopus 로고    scopus 로고
    • Dynamics of spore coat morphogenesis in Bacillus subtilis
    • McKenney PT, Eichenberger P. 2012. Dynamics of spore coat morphogenesis in Bacillus subtilis. Mol Microbiol 83:245-260.
    • (2012) Mol Microbiol , vol.83 , pp. 245-260
    • McKenney, P.T.1    Eichenberger, P.2
  • 102
    • 0032969092 scopus 로고    scopus 로고
    • Bacillus subtilis spore coat
    • Driks A. 1999. Bacillus subtilis spore coat. Microbiol Mol Biol Rev 63:1-20.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 1-20
    • Driks, A.1
  • 103
    • 73649139213 scopus 로고    scopus 로고
    • Localization of proteins to different layers and regions of Bacillus subtilis spore coats
    • Imamura D, Kuwana R, Takamatsu H, Watabe K. 2010. Localization of proteins to different layers and regions of Bacillus subtilis spore coats. J Bacteriol 192:518-524.
    • (2010) J Bacteriol , vol.192 , pp. 518-524
    • Imamura, D.1    Kuwana, R.2    Takamatsu, H.3    Watabe, K.4
  • 104
    • 80051988071 scopus 로고    scopus 로고
    • YwdL in Bacillus cereus:its role in germination and exosporium structure
    • Terry C, Shepherd A, Radford DS, Moir A, Bullough PA. 2011. YwdL in Bacillus cereus:its role in germination and exosporium structure. PLos One 6:e23801. doi:10.1371/journal.pone.0023801.
    • (2011) PLos One , vol.6
    • Terry, C.1    Shepherd, A.2    Radford, D.S.3    Moir, A.4    Bullough, P.A.5
  • 106
    • 4344718438 scopus 로고    scopus 로고
    • Transglutaminase-mediated cross-linking of GerQ in the coats of Bacillus subtilis spores
    • Ragkousi K, Setlow P. 2004. Transglutaminase-mediated cross-linking of GerQ in the coats of Bacillus subtilis spores. J Bacteriol 186:5567-5575.
    • (2004) J Bacteriol , vol.186 , pp. 5567-5575
    • Ragkousi, K.1    Setlow, P.2
  • 107
    • 33750463770 scopus 로고    scopus 로고
    • Localization of the transglutaminase cross-linking sites in the Bacillus subtilis spore coat protein GerQ
    • Monroe A, Setlow P. 2006. Localization of the transglutaminase cross-linking sites in the Bacillus subtilis spore coat protein GerQ. J Bacteriol 188:7609-7616.
    • (2006) J Bacteriol , vol.188 , pp. 7609-7616
    • Monroe, A.1    Setlow, P.2
  • 108
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • Blackburn NT, Clarke AJ. 2001. Identification of four families of peptidoglycan lytic transglycosylases. J Mol Evol 52:78-84.
    • (2001) J Mol Evol , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 109
  • 110
    • 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, Watabe K. 1999. 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) 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
  • 111
    • 57349191124 scopus 로고    scopus 로고
    • The Bacillus anthracis SleL (YaaH) protein is an N-acetylglucosaminidase involved in spore cortex depolymerization
    • Lambert EA, Popham DL. 2008. The Bacillus anthracis SleL (YaaH) protein is an N-acetylglucosaminidase involved in spore cortex depolymerization. J Bacteriol 190:7601-7607.
    • (2008) J Bacteriol , vol.190 , pp. 7601-7607
    • Lambert, E.A.1    Popham, D.L.2
  • 113
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido) glycans
    • Buist G, Steen A, Kok J, Kuipers OP. 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
  • 114
    • 84893776820 scopus 로고    scopus 로고
    • Spore germination mediated by Bacillus megaterium qM B1551 SleL and YpeB
    • Üstok FI, Packman LC, Lowe CR, Christie G. 2014. Spore germination mediated by Bacillus megaterium qM B1551 SleL and YpeB. J Bacteriol 196:10451054.
    • (2014) J Bacteriol , vol.196 , pp. 10451054
    • Üstok, F.I.1    Packman, L.C.2    Lowe, C.R.3    Christie, G.4
  • 115
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis
    • Papanikolau Y, Prag G, Tavlas G, Vorgias CE, Oppenheim AB, Petratos K. 2001. High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry 40:11338-11343.
    • (2001) Biochemistry , vol.40 , pp. 11338-11343
    • Papanikolau, Y.1    Prag, G.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6
  • 116
    • 84860512983 scopus 로고    scopus 로고
    • In vitro and in vivo analyses of the Bacillus anthracis spore cortex lytic protein SleL
    • Lambert EA, Sherry N, Popham DL. 2012. In vitro and in vivo analyses of the Bacillus anthracis spore cortex lytic protein SleL. Microbiology 158:1359-1368.
    • (2012) Microbiology , vol.158 , pp. 1359-1368
    • Lambert, E.A.1    Sherry, N.2    Popham, D.L.3
  • 117
    • 75149112859 scopus 로고    scopus 로고
    • SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate
    • Burns DA, Heap JT, Minton NP. 2010. SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate. J Bacteriol 192:657-664.
    • (2010) J Bacteriol , vol.192 , pp. 657-664
    • Burns, D.A.1    Heap, J.T.2    Minton, N.P.3
  • 118
    • 65249186376 scopus 로고    scopus 로고
    • SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens
    • Paredes-Sabja D, Setlow P, Sarker MR. 2009. SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens. J Bacteriol 191:2711-2720.
    • (2009) J Bacteriol , vol.191 , pp. 2711-2720
    • Paredes-Sabja, D.1    Setlow, P.2    Sarker, M.R.3
  • 120
    • 0029267226 scopus 로고
    • purification and partial characterization of a spore cortex-lytic enzyme of Clostridium perfringens S40 spores
    • Miyata S, Moriyama R, Sugimoto K, Makino S. 1995. purification and partial characterization of a spore cortex-lytic enzyme of Clostridium perfringens S40 spores. Biosci Biotechnol Biochem 59:514-515.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 514-515
    • Miyata, S.1    Moriyama, R.2    Sugimoto, K.3    Makino, S.4
  • 121
    • 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, Moriyama R. 1997. 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) J Bacteriol , vol.179 , pp. 3181-3187
    • Chen, Y.1    Miyata, S.2    Makino, S.3    Moriyama, R.4
  • 122
    • 33749653115 scopus 로고    scopus 로고
    • Expression of germination-related enzymes, CspA, CspB, CspC, SleC, and SleM, of Clostridium perfringens S40 in the mother cell compartment of sporulating cells
    • Masayama A, Hamasaki K, Urakami K, Shimamoto S, Kato S, Makino S, Yoshimura T, Moriyama M, Moriyama R. 2006. Expression of germination-related enzymes, CspA, CspB, CspC, SleC, and SleM, of Clostridium perfringens S40 in the mother cell compartment of sporulating cells. Genes Genet Syst 81:227-234.
    • (2006) Genes Genet Syst , vol.81 , pp. 227-234
    • Masayama, A.1    Hamasaki, K.2    Urakami, K.3    Shimamoto, S.4    Kato, S.5    Makino, S.6    Yoshimura, T.7    Moriyama, M.8    Moriyama, R.9
  • 123
    • 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, Makino S. 1995. 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) Microbiology , vol.141 , pp. 2643-2650
    • Miyata, S.1    Moriyama, R.2    Miyahara, N.3    Makino, S.4
  • 124
    • 0032971733 scopus 로고    scopus 로고
    • Germination-specific cortex-lytic enzymes from Clostridium perfringens S40 spores:time of synthesis, precursor structure and regulation of enzymatic activity
    • Urakami K, Miyata S, Moriyama R, Sugimoto K, Makino S. 1999. Germination-specific cortex-lytic enzymes from Clostridium perfringens S40 spores:time of synthesis, precursor structure and regulation of enzymatic activity. FEMS Microbiol Lett 173:467-473.
    • (1999) FEMS Microbiol Lett , vol.173 , pp. 467-473
    • Urakami, K.1    Miyata, S.2    Moriyama, R.3    Sugimoto, K.4    Makino, S.5
  • 125
    • 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, Makino S. 2000. 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) 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
  • 126
    • 84891621197 scopus 로고    scopus 로고
    • Functional analysis of SleC from Clostridium difficile:an essential lytic transglycosylase involved in spore germination
    • Gutelius D, Hokeness K, Logan SM, Reid CW. 2014. Functional analysis of SleC from Clostridium difficile:an essential lytic transglycosylase involved in spore germination. Microbiology 160:209-216.
    • (2014) Microbiology , vol.160 , pp. 209-216
    • Gutelius, D.1    Hokeness, K.2    Logan, S.M.3    Reid, C.W.4
  • 127
    • 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, Makino S. 2001. 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) J Bacteriol , vol.183 , pp. 3742-3751
    • Shimamoto, S.1    Moriyama, R.2    Sugimoto, K.3    Miyata, S.4    Makino, S.5
  • 129
    • 70349421685 scopus 로고    scopus 로고
    • The protease CspB is essential for initiation of cortex hydrolysis and dipicolinic acid (DPA) release during germination of spores of Clostridium perfringens type A food poisoning isolates
    • Paredes-Sabja D, Setlow P, Sarker MR. 2009. The protease CspB is essential for initiation of cortex hydrolysis and dipicolinic acid (DPA) release during germination of spores of Clostridium perfringens type A food poisoning isolates. Microbiology 155:3464-3472.
    • (2009) Microbiology , vol.155 , pp. 3464-3472
    • Paredes-Sabja, D.1    Setlow, P.2    Sarker, M.R.3
  • 130
    • 84874760766 scopus 로고    scopus 로고
    • Structural and functional analysis of the CspB protease required for Clostridium spore germination
    • Adams CM, Eckenroth BE, Putnam EE, Doublie S, Shen A. 2013. Structural and functional analysis of the CspB protease required for Clostridium spore germination. PLoS Pathog 9:e1003165.
    • (2013) PLoS Pathog , vol.9
    • Adams, C.M.1    Eckenroth, B.E.2    Putnam, E.E.3    Doublie, S.4    Shen, A.5
  • 131
    • 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, Makino S. 1997. Localization of germination-specific spore-lytic enzymes in Clostridium perfringens S40 spores detected by immunoelectron microscopy. FEMS Microbiol Lett 152:243-247.
    • (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
  • 132
    • 0347364722 scopus 로고    scopus 로고
    • Spore germination
    • Setlow P. 2003. Spore germination. Curr Opin Microbiol 6:550-556.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 550-556
    • Setlow, P.1
  • 135
    • 80052022747 scopus 로고    scopus 로고
    • Whole-genome phylogenies of the family Bacillaceae and expansion of the sigma factor gene family in the Bacillus cereus species-group
    • Schmidt TR, Scott EJ II, Dyer DW. 2011. Whole-genome phylogenies of the family Bacillaceae and expansion of the sigma factor gene family in the Bacillus cereus species-group. BMC Genomics 12:430.
    • (2011) BMC Genomics , vol.12 , pp. 430
    • Schmidt, T.R.1    Scott E.J, I.I.2    Dyer, D.W.3
  • 136
    • 0002449232 scopus 로고    scopus 로고
    • Phylogenetic relationships
    • In Rood JI, McClane BA, Songer JG, Titball RW (ed), Academic Press, San Diego, CA
    • Stackebrandt E, Rainey FA. 1997. Phylogenetic relationships, p 3-20. In Rood JI, McClane BA, Songer JG, Titball RW (ed), The Clostridia:Molecular Biology and Pathogenesis. Academic Press, San Diego, CA.
    • (1997) The Clostridia:Molecular Biology and Pathogenesis , pp. 3-20
    • Stackebrandt, E.1    Rainey, F.A.2


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