메뉴 건너뛰기




Volumn 8, Issue 5-6, 2006, Pages 823-834

Role of membrane-bound thiol-disulfide oxidoreductases in endospore-forming bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; CCDA PROTEIN; CYSTEINE; DISULFIDE; MEMBRANE ENZYME; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); SPOIVH PROTEIN; STOA PROTEIN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33745865551     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.823     Document Type: Review
Times cited : (27)

References (63)
  • 1
    • 15944399025 scopus 로고    scopus 로고
    • Screening for Bacillus subtilis mutants deficient in pressure induced spore germination: Identification of ykvU as a novel germination gene
    • Aertsen A, Opstal IV, Vanmuysen SC, Wuytack EY, and Michaels CW. Screening for Bacillus subtilis mutants deficient in pressure induced spore germination: identification of ykvU as a novel germination gene. FEMS Microbiol Lett 243: 385-391, 2005.
    • (2005) FEMS Microbiol Lett , vol.243 , pp. 385-391
    • Aertsen, A.1    Opstal, I.V.2    Vanmuysen, S.C.3    Wuytack, E.Y.4    Michaels, C.W.5
  • 2
    • 0017153825 scopus 로고
    • Structure and morphogenesis of the bacterial spore coat
    • Aronson AI and Fitz-James P. Structure and morphogenesis of the bacterial spore coat. Bacteriol Rev 40: 360-402, 1976.
    • (1976) Bacteriol Rev , vol.40 , pp. 360-402
    • Aronson, A.I.1    Fitz-James, P.2
  • 4
    • 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, 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, S.J.4    Moir, A.5
  • 5
    • 0033609929 scopus 로고    scopus 로고
    • Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis
    • Bolhuis A, Venema G, Quax WJ, Bron S, and van Dijl JM. Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis. J Biol Chem 274: 24531-24538, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 24531-24538
    • Bolhuis, A.1    Venema, G.2    Quax, W.J.3    Bron, S.4    Van Dijl, J.M.5
  • 7
    • 0022444246 scopus 로고
    • Correlation of penicillin-binding protein composition with different functions of two membranes in Bacillus subtilis forespores
    • Buchanan CE and Neyman SL. Correlation of penicillin-binding protein composition with different functions of two membranes in Bacillus subtilis forespores. J Bacteriol 165: 498-503, 1986.
    • (1986) J Bacteriol , vol.165 , pp. 498-503
    • Buchanan, C.E.1    Neyman, S.L.2
  • 9
    • 0028983824 scopus 로고
    • Mechanisms and catalysts of disulfide bond formation in proteins
    • Creighton TE, Zapun A, and Darby NJ. Mechanisms and catalysts of disulfide bond formation in proteins. Trends Biotechnol 13: 18-23, 1995.
    • (1995) Trends Biotechnol , vol.13 , pp. 18-23
    • Creighton, T.E.1    Zapun, A.2    Darby, N.J.3
  • 10
    • 2542430403 scopus 로고    scopus 로고
    • Structural basis of redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA
    • Crow A, Acheson RM, Le Brun NE, and Oubrie A. Structural basis of redox-coupled protein substrate selection by the cytochrome c biosynthesis protein ResA. J Biol Chem 279: 23654-23660, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 23654-23660
    • Crow, A.1    Acheson, R.M.2    Le Brun, N.E.3    Oubrie, A.4
  • 11
    • 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, and Errington J. The Bacillus subtilis spoVD gene encodes a mother-cell-specific penicillin-binding protein required for spore morphogenesis. J Mol Biol 215: 209-220, 1994.
    • (1994) J Mol Biol , vol.215 , pp. 209-220
    • Daniel, R.A.1    Drake, S.2    Buchanan, C.E.3    Scholle, R.4    Errington, J.5
  • 12
    • 0033982955 scopus 로고    scopus 로고
    • Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes
    • Deshmukh M, Brasseur G, and Daldal F. Novel Rhodobacter capsulatus genes required for the biogenesis of various c-type cytochromes. Mol Microbiol 35: 123-138, 2000.
    • (2000) Mol Microbiol , vol.35 , pp. 123-138
    • Deshmukh, M.1    Brasseur, G.2    Novel, D.F.3
  • 13
    • 0037053393 scopus 로고    scopus 로고
    • Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168
    • Dorenbos R, Stein T, Kabel J, Bruand C, Bolhuis A, Bron S, and Quax WJ. Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168. J Biol Chem 111: 16682-16688, 2002.
    • (2002) J Biol Chem , vol.111 , pp. 16682-16688
    • Dorenbos, R.1    Stein, T.2    Kabel, J.3    Bruand, C.4    Bolhuis, A.5    Bron, S.6    Quax, W.J.7
  • 14
    • 13444288096 scopus 로고    scopus 로고
    • Biogenesis of a putative channel protein, ComEC, required for DNA uptake: Membrane topology, oligomerization and formation of disulphide bonds
    • Draskovic I and Dubnau D. Biogenesis of a putative channel protein, ComEC, required for DNA uptake: membrane topology, oligomerization and formation of disulphide bonds. Mol Microbiol 55: 881-896, 2004.
    • (2004) Mol Microbiol , vol.55 , pp. 881-896
    • Draskovic, I.1    Dubnau, D.2
  • 15
    • 0002092720 scopus 로고    scopus 로고
    • Proteins of the spore core and coat
    • Hoch JA, Sonenshein AL, and Losick R. (eds.). Washington DC: American Society for Microbiology Press
    • Driks A. Proteins of the spore core and coat. In: Bacillus subtilis and its closests relatives. From genes to cells. Hoch JA, Sonenshein AL, and Losick R. (eds.). Washington DC: American Society for Microbiology Press, 2000, pp. 527-535.
    • (2000) Bacillus subtilis and Its Closests Relatives. From Genes to Cells , pp. 527-535
    • Driks, A.1
  • 16
    • 0002782639 scopus 로고    scopus 로고
    • Morphogenesis and properties of the bacterial spore
    • Brun YV and Shimkets LJ (eds.). Washington DC: American Society for Microbiology Press
    • Driks A and Setlow P. Morphogenesis and properties of the bacterial spore. In: Prokaryotic development, Brun YV and Shimkets LJ (eds.). Washington DC: American Society for Microbiology Press, 2000. pp. 191-218.
    • (2000) Prokaryotic Development , pp. 191-218
    • Driks, A.1    Setlow, P.2
  • 17
    • 0002208186 scopus 로고    scopus 로고
    • Transformation and recombination
    • Hoch JA, Sonenshein AL, and Losick R (eds.). Washington DC: American Society for Microbiology Press
    • Dubnau D and Lovett J. Transformation and recombination. In: Bacillus subtilis and its closests relatives. From genes to cells. Hoch JA, Sonenshein AL, and Losick R (eds.). Washington DC: American Society for Microbiology Press, 2002, pp. 453-471.
    • (2002) Bacillus subtilis and Its Closests Relatives. From Genes to Cells , pp. 453-471
    • Dubnau, D.1    Lovett, J.2
  • 20
    • 0038381449 scopus 로고    scopus 로고
    • Bacillus subtilis ResA is a thiol-disulfide oxidoredutase involved in cytochrome c synthesis
    • Erlendsson LS, Acheson R, Hederstedt L, and Le Brun NE. Bacillus subtilis ResA is a thiol-disulfide oxidoredutase involved in cytochrome c synthesis. J Biol Chem 278: 17852-17858, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 17852-17858
    • Erlendsson, L.S.1    Acheson, R.2    Hederstedt, L.3    Le Brun, N.E.4
  • 21
    • 0036175133 scopus 로고    scopus 로고
    • Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can supress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells
    • Erlendsson LS and Hederstedt L. Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can supress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells. J Bacteriol 184: 1423-1429, 2002.
    • (2002) J Bacteriol , vol.184 , pp. 1423-1429
    • Erlendsson, L.S.1    Hederstedt, L.2
  • 22
    • 4444319828 scopus 로고    scopus 로고
    • Bacillus subtilis StoA is a thiol-disulfide oxidoreductase important for spore cortex synthesis
    • Erlendsson LS, Möller M, and Hederstedt L. Bacillus subtilis StoA is a thiol-disulfide oxidoreductase important for spore cortex synthesis. J Bacteriol 186: 6230-6238, 2004.
    • (2004) J Bacteriol , vol.186 , pp. 6230-6238
    • Erlendsson, L.S.1    Möller, M.2    Hederstedt, L.3
  • 23
    • 1842613501 scopus 로고    scopus 로고
    • Regulation of endospore formation in Bacillus subtilis
    • Errington J. Regulation of endospore formation in Bacillus subtilis. Nature Rev Microbiol 1: 117-126, 2003.
    • (2003) Nature Rev Microbiol , vol.1 , pp. 117-126
    • Errington, J.1
  • 24
    • 0001904527 scopus 로고    scopus 로고
    • Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers and capsules
    • Hoch JA, Sonenshein AL, and Losick R (eds.). Washington DC: American Society for Microbiology Press
    • Foster SJ and Popham DL. Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers and capsules. In: Bacillus subtilis and its closest relatives. From genes to cells, Hoch JA, Sonenshein AL, and Losick R (eds.). Washington DC: American Society for Microbiology Press, 2002, pp. 21-41.
    • (2002) Bacillus subtilis and Its Closest Relatives. From Genes to Cells , pp. 21-41
    • Foster, S.J.1    Popham, D.L.2
  • 25
    • 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 HT, Atrih A, Foster SJ, and Sekiguchi J. 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.
    • (2002) J Bacteriol , vol.184 , pp. 6007-6015
    • Fukushima, T.1    Yamamoto, H.T.2    Atrih, A.3    Foster, S.J.4    Sekiguchi, J.5
  • 28
    • 2942616403 scopus 로고    scopus 로고
    • Compartmentalization of gene expression during Bacillus subtilis spore formation
    • Hilbert DW and Piggot PJ. Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol Mol Biol Rev 68: 234-262, 2004.
    • (2004) Microbiol Mol Biol Rev , vol.68 , pp. 234-262
    • Hilbert, D.W.1    Piggot, P.J.2
  • 30
    • 23844544940 scopus 로고    scopus 로고
    • The use of bacterial spore formers as probiotics
    • Hong HA, Duc LH, and Cutting SM. The use of bacterial spore formers as probiotics. FEMS Microbiol Rev 29: 813-835, 2005.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 813-835
    • Hong, H.A.1    Duc, L.H.2    Cutting, S.M.3
  • 31
    • 3843119815 scopus 로고    scopus 로고
    • SpoIVH (ykvV), a requisite cortex formation gene, is expressed in both sporulating compartments of Bacillus subtilis
    • Imamura D, Kobayashi K, Sekiguchi J, Ogasawara N, Takeuchi M, and Sato T. spoIVH (ykvV), a requisite cortex formation gene, is expressed in both sporulating compartments of Bacillus subtilis. J Bacteriol 186: 5450-5459, 2004.
    • (2004) J Bacteriol , vol.186 , pp. 5450-5459
    • Imamura, D.1    Kobayashi, K.2    Sekiguchi, J.3    Ogasawara, N.4    Takeuchi, M.5    Sato, T.6
  • 32
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • Kadokura H, Katzen F, and Beckwith J. Protein disulfide bond formation in prokaryotes. Ann Rev Biochem 72: 111-135, 2003.
    • (2003) Ann Rev Biochem , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 33
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen F, and Beckwith J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103: 769-779, 2000.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 34
    • 0036682611 scopus 로고    scopus 로고
    • Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD
    • Katzen F, Deshmukh M, Daldal F, and Beckwith J. Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J 21: 3960-3969, 2002.
    • (2002) EMBO J , vol.21 , pp. 3960-3969
    • Katzen, F.1    Deshmukh, M.2    Daldal, F.3    Beckwith, J.4
  • 35
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azvedo V, et al. The complete genome sequence of the Gram-positive bacterium Bacillus subtilis. Nature 390: 249-256, 1997.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Alloni, G.5    Azvedo, V.6
  • 37
    • 16244387909 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space
    • Matias VRF and Beveridge TJ. Cryo-electron microscopy reveals native polymeric cell wall structure in Bacillus subtilis 168 and the existence of a periplasmic space. Mol Microbiol 56: 240-251, 2005.
    • (2005) Mol Microbiol , vol.56 , pp. 240-251
    • Matias, V.R.F.1    Beveridge, T.J.2
  • 38
    • 0033891426 scopus 로고    scopus 로고
    • Structural analysis of Bacillus subtilis spore peptidoglycan during sporulation
    • Meador-Parton J and Popham DL. Structural analysis of Bacillus subtilis spore peptidoglycan during sporulation. J Bacteriol 182: 4491-4499, 2000.
    • (2000) J Bacteriol , vol.182 , pp. 4491-4499
    • Meador-Parton, J.1    Popham, D.L.2
  • 41
    • 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, Hattori A, Kozuka S, Yasuda Y, Tochikubo K, and Makino S. 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.
    • (1999) J Bacteriol , vol.181 , pp. 2373-2378
    • Moriyama, R.1    Fukuoka, H.2    Miyata, S.3    Hattori, A.4    Kozuka, S.5    Yasuda, Y.6    Tochikubo, K.7    Makino, S.8
  • 42
    • 4644321084 scopus 로고    scopus 로고
    • a and redox properties in the thioredoxin superfamily
    • a and redox properties in the thioredoxin superfamily. Protein Sci 13: 2744-2752, 2004.
    • (2004) Protein Sci , vol.13 , pp. 2744-2752
    • Moutevelis, E.1    Warwicker, J.2
  • 43
    • 0036204947 scopus 로고    scopus 로고
    • Roles of Bacillus endospores in the environment
    • Nicholson WN. Roles of Bacillus endospores in the environment. Cell Mol Life Sci 59: 410-416, 2002.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 410-416
    • Nicholson, W.N.1
  • 44
    • 0033818517 scopus 로고    scopus 로고
    • Resistance of Bacillus endospores to extreme terrestrial and extraterrestrial environments
    • Nicholson WN, Munakata N, Horneck G, Melosh HJ, and Setlow P. Resistance of Bacillus endospores to extreme terrestrial and extraterrestrial environments. Microbiol Mol Biol Rev 64: 548-572, 2000.
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 548-572
    • Nicholson, W.N.1    Munakata, N.2    Horneck, G.3    Melosh, H.J.4    Setlow, P.5
  • 46
    • 0002527560 scopus 로고    scopus 로고
    • Spore germination and outgrowth
    • Hoch JA. Sonenshein AL, and Losick RL (eds.). Washington DC: American Society for Microbiology Press
    • Paidhungat M and Setlow P. Spore germination and outgrowth. In: Bacillus subtilis and its closest relatives. From genes to cells, Hoch JA. Sonenshein AL, and Losick RL (eds.). Washington DC: American Society for Microbiology Press, 2002, pp. 537-548.
    • (2002) Bacillus subtilis and Its Closest Relatives. From Genes to Cells , pp. 537-548
    • Paidhungat, M.1    Setlow, P.2
  • 47
    • 0032483367 scopus 로고    scopus 로고
    • Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, Sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168
    • Paik SH, Chakicherla A, and Hansen JN. Identification and characterization of the structural and transporter genes for, and the chemical and biological properties of, Sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168. J Biol Chem 273: 23134-23142, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 23134-23142
    • Paik, S.H.1    Chakicherla, A.2    Hansen, J.N.3
  • 49
    • 0002305548 scopus 로고    scopus 로고
    • Sporulation genes and intercompartemental regulation
    • Hoch JA, Sonenshein AL, and Losick R (eds.), Washington DC: American Society for Microbiology Press
    • Piggot PJ and Losick R. Sporulation genes and intercompartemental regulation. In: Bacillus subtilis and its closest relatives. From genes to cells, Hoch JA, Sonenshein AL, and Losick R (eds.), Washington DC: American Society for Microbiology Press, 2002, pp. 483-517.
    • (2002) Bacillus subtilis and Its Closest Relatives. From Genes to Cells , pp. 483-517
    • Piggot, P.J.1    Losick, R.2
  • 50
    • 0036203186 scopus 로고    scopus 로고
    • Specialized peptidoglycan of the bacterial endospore: The inner wall of the lockbox
    • Popham DL. Specialized peptidoglycan of the bacterial endospore: the inner wall of the lockbox. Cell Mol Life Sci 59: 426-433, 2002.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 426-433
    • Popham, D.L.1
  • 51
    • 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, and Setlow P Roles of low-molecular-weight penicillin-binding proteins in Bacillus subtilis spore peptidoglycan synthesis and spore properties. J Bacteriol 181: 126-132, 1999.
    • (1999) J Bacteriol , vol.181 , pp. 126-132
    • Popham, D.L.1    Gilmore, M.E.2    Setlow, P.3
  • 52
    • 0029904736 scopus 로고    scopus 로고
    • Analysis of the peptidoglycan structure of Bacillus subtilis endospores
    • Popham DL, Helin J, Costello CE, 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.E.3    Setlow, P.4
  • 53
    • 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, and Setlow P. 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.
    • (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
  • 54
    • 0026345897 scopus 로고
    • Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis
    • Popham DL and Stragier P. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. J Bacteriol 173: 7942-7949, 1991.
    • (1991) J Bacteriol , vol.173 , pp. 7942-7949
    • Popham, D.L.1    Stragier, P.2
  • 55
    • 0030765627 scopus 로고    scopus 로고
    • Making and breaking disulfide bonds
    • Raina S and Missiakas D. Making and breaking disulfide bonds. Ann Rev Microbiol 51: 179-202, 1997.
    • (1997) Ann Rev Microbiol , vol.51 , pp. 179-202
    • Raina, S.1    Missiakas, D.2
  • 57
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch A, Bessette P, Georgiou G, and Beckwith J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol 179: 6602-6608, 1997.
    • (1997) J Bacteriol , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 58
    • 0038755703 scopus 로고    scopus 로고
    • Efficient spore synthesis in Bacillus subtilis depends on the CcdA protein
    • Schiött T and Hederstedt L. Efficient spore synthesis in Bacillus subtilis depends on the CcdA protein. J Bacteriol 182: 2845-2854, 2000.
    • (2000) J Bacteriol , vol.182 , pp. 2845-2854
    • Schiött, T.1    Hederstedt, L.2
  • 59
    • 0038228616 scopus 로고    scopus 로고
    • Bacillus subtilis CcdA defective mutants are blocked in a late step of cytochrome c biogenesis
    • Schiött T, Throne-Holst M, and Hederstedt L. Bacillus subtilis CcdA defective mutants are blocked in a late step of cytochrome c biogenesis. J Bacteriol 179: 4523-4529, 1997.
    • (1997) J Bacteriol , vol.179 , pp. 4523-4529
    • Schiött, T.1    Throne-Holst, M.2    Hederstedt, L.3
  • 60
    • 0030897419 scopus 로고    scopus 로고
    • Identification and characterization of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis
    • Schiött T, von Wachenfeldt C, and Hederstedt L. Identification and characterization of the ccdA gene, required for cytochrome c synthesis in Bacillus subtilis. J Bacteriol 179: 1962-1973, 1997.
    • (1997) J Bacteriol , vol.179 , pp. 1962-1973
    • Schiött, T.1    Von Wachenfeldt, C.2    Hederstedt, L.3
  • 62
    • 0000043728 scopus 로고    scopus 로고
    • Endospore-forming bacteria: An overview
    • Brun YV and Shimkets LJ (eds.). Washington DC: American Society for Microbiology Press
    • Sonenshein AL. Endospore-forming bacteria: An overview. In: Prokaryotic development, Brun YV and Shimkets LJ (eds.). Washington DC: American Society for Microbiology Press, 2000, pp. 133-150.
    • (2000) Prokaryotic Development , pp. 133-150
    • Sonenshein, A.L.1
  • 63
    • 0013132577 scopus 로고    scopus 로고
    • Respiratory cytochromes, other heme proteins, and heme biosynthesis
    • Sonenshein AL, Hoch JA, and Losick R (eds.). Washington DC: American Society for Microbiology Press
    • von Wachenfeldt C and Hederstedt L. Respiratory cytochromes, other heme proteins, and heme biosynthesis. In: Bacillus subtilis and its closest relatives: from genes to cells, Sonenshein AL, Hoch JA, and Losick R (eds.). Washington DC: American Society for Microbiology Press, 2001, pp. 163-179.
    • (2001) Bacillus subtilis and Its Closest Relatives: From Genes to Cells , pp. 163-179
    • Von Wachenfeldt, C.1    Hederstedt, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.