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Volumn 59, Issue 1, 2008, Pages 1-8

Auto-induction and purification of a Bacillus subtilis transglutaminase (Tgl) and its preliminary crystallographic characterization

Author keywords

Cross linking; Crystallization; Macromolecular assembly; Spore coat; Spore surface; Transglutaminase

Indexed keywords

PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 40849092856     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.12.004     Document Type: Article
Times cited : (20)

References (36)
  • 1
    • 0032969092 scopus 로고    scopus 로고
    • Bacillus subtilis spore coat
    • Driks A. Bacillus subtilis spore coat. Microbiol. Mol. Biol. Rev. 63 (1999) 1-20
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 1-20
    • Driks, A.1
  • 2
    • 0034006139 scopus 로고    scopus 로고
    • Structure and assembly of the bacterial endospore coat
    • Henriques A.O., and Moran Jr. C.P. Structure and assembly of the bacterial endospore coat. Methods 20 (2000) 95-110
    • (2000) Methods , vol.20 , pp. 95-110
    • Henriques, A.O.1    Moran Jr., C.P.2
  • 4
    • 34547640042 scopus 로고    scopus 로고
    • Structure, assembly, and function of the spore surface layers
    • Henriques A.O., and Moran Jr. C.P. Structure, assembly, and function of the spore surface layers. Annu. Rev. Microbiol. 61 (2007) 555-588
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 555-588
    • Henriques, A.O.1    Moran Jr., C.P.2
  • 5
    • 33744733251 scopus 로고    scopus 로고
    • Spores of Bacillus subtilis: their resistance to and killing by radiation, heat and chemicals
    • Setlow P. Spores of Bacillus subtilis: their resistance to and killing by radiation, heat and chemicals. J. Appl. Microbiol. 101 (2006) 514-525
    • (2006) J. Appl. Microbiol. , vol.101 , pp. 514-525
    • Setlow, P.1
  • 8
    • 0141594789 scopus 로고    scopus 로고
    • Bacterial spore germination and protein mobility
    • Moir A. Bacterial spore germination and protein mobility. Trends Microbiol. 11 (2003) 452-454
    • (2003) Trends Microbiol. , vol.11 , pp. 452-454
    • Moir, A.1
  • 9
    • 1842613501 scopus 로고    scopus 로고
    • Regulation of endospore formation in Bacillus subtilis
    • Errington J. Regulation of endospore formation in Bacillus subtilis. Nat. Rev. Microbiol. 1 (2003) 117-126
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 117-126
    • Errington, J.1
  • 11
    • 1342304139 scopus 로고    scopus 로고
    • Assembly of an oxalate decarboxylase produced under sK control into the Bacillus subtilis spore coat
    • Costa T.V., Martins L.O., Voelker U., and Henriques A.O. Assembly of an oxalate decarboxylase produced under sK control into the Bacillus subtilis spore coat. J. Bacteriol. 186 (2004) 1462-1474
    • (2004) J. Bacteriol. , vol.186 , pp. 1462-1474
    • Costa, T.V.1    Martins, L.O.2    Voelker, U.3    Henriques, A.O.4
  • 12
    • 0028989606 scopus 로고
    • Characterization of cotJ, a sE-controlled operon affecting the polypeptide composition of the coat of Bacillus subtilis spores
    • Henriques A.O., Beall B.W., Roland K., and Moran Jr. C.P. Characterization of cotJ, a sE-controlled operon affecting the polypeptide composition of the coat of Bacillus subtilis spores. J. Bacteriol. 177 (1995) 3394-3406
    • (1995) J. Bacteriol. , vol.177 , pp. 3394-3406
    • Henriques, A.O.1    Beall, B.W.2    Roland, K.3    Moran Jr., C.P.4
  • 13
    • 9844239368 scopus 로고    scopus 로고
    • Interactions and assembly of cotJ-encoded products, constituents of the inner layers of the Bacillus subtilis spore coat
    • Seyler R., Henriques A.O., Ozin A., and Moran Jr. C.P. Interactions and assembly of cotJ-encoded products, constituents of the inner layers of the Bacillus subtilis spore coat. Mol. Microbiol. 25 (1997) 955-966
    • (1997) Mol. Microbiol. , vol.25 , pp. 955-966
    • Seyler, R.1    Henriques, A.O.2    Ozin, A.3    Moran Jr., C.P.4
  • 14
    • 0034333425 scopus 로고    scopus 로고
    • The yabG gene of Bacillus subtilis encodes a sporulation specific protease which is involved in the processing of several coat proteins
    • Takamatsu H., Imamura A., Kodama T., Asai K., Ogasawara N., and Watabe K. The yabG gene of Bacillus subtilis encodes a sporulation specific protease which is involved in the processing of several coat proteins. FEMS Microbiol. Lett. 192 (2000) 33-38
    • (2000) FEMS Microbiol. Lett. , vol.192 , pp. 33-38
    • Takamatsu, H.1    Imamura, A.2    Kodama, T.3    Asai, K.4    Ogasawara, N.5    Watabe, K.6
  • 15
    • 0031955996 scopus 로고    scopus 로고
    • Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis
    • Henriques A.O., Melsen L.R., and Moran Jr. C.P. Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis. J. Bacteriol. 180 (1998) 2285-2291
    • (1998) J. Bacteriol. , vol.180 , pp. 2285-2291
    • Henriques, A.O.1    Melsen, L.R.2    Moran Jr., C.P.3
  • 16
    • 0037166265 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat
    • Martins L.O., Soares C.M., Pereira M.M., Teixeira M., Costa T., Jones G.H., and Henriques A.O. Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J. Biol. Chem. 277 (2002) 18849-18859
    • (2002) J. Biol. Chem. , vol.277 , pp. 18849-18859
    • Martins, L.O.1    Soares, C.M.2    Pereira, M.M.3    Teixeira, M.4    Costa, T.5    Jones, G.H.6    Henriques, A.O.7
  • 17
    • 0038143259 scopus 로고    scopus 로고
    • Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties
    • Enguita F.J., Martins L.O., Henriques A.O., and Carrondo M.A. Crystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability properties. J. Biol. Chem. 278 (2003) 19416-19425
    • (2003) J. Biol. Chem. , vol.278 , pp. 19416-19425
    • Enguita, F.J.1    Martins, L.O.2    Henriques, A.O.3    Carrondo, M.A.4
  • 19
    • 0029888257 scopus 로고    scopus 로고
    • Identification and characterization of a gene cluster involved in manganese oxidation by spores of the marine Bacillus sp. strain SG-1
    • Waasbergen L.G., Hildebrand M., and Tebo B.M. Identification and characterization of a gene cluster involved in manganese oxidation by spores of the marine Bacillus sp. strain SG-1. J. Bacteriol. 178 (1996) 3517-3530
    • (1996) J. Bacteriol. , vol.178 , pp. 3517-3530
    • Waasbergen, L.G.1    Hildebrand, M.2    Tebo, B.M.3
  • 20
    • 0036431686 scopus 로고    scopus 로고
    • Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp. strain SG-1
    • Francis C.A., Casciotti K.L., and Tebo B.M. Localization of Mn(II)-oxidizing activity and the putative multicopper oxidase, MnxG, to the exosporium of the marine Bacillus sp. strain SG-1. Arch. Microbiol. 178 (2002) 450-456
    • (2002) Arch. Microbiol. , vol.178 , pp. 450-456
    • Francis, C.A.1    Casciotti, K.L.2    Tebo, B.M.3
  • 21
    • 33947161385 scopus 로고    scopus 로고
    • A novel lipolytic enzyme, Ycsk (LipC), located in the spore coat of Bacillus subtilis, is involved in spore germination
    • Masayama A., Kuwana R., Takamatsu H., Hemmi H., Yoshimura T., et al. A novel lipolytic enzyme, Ycsk (LipC), located in the spore coat of Bacillus subtilis, is involved in spore germination. J. Bacteriol. (2007) 2369-2375
    • (2007) J. Bacteriol. , pp. 2369-2375
    • Masayama, A.1    Kuwana, R.2    Takamatsu, H.3    Hemmi, H.4    Yoshimura, T.5
  • 22
    • 0030297463 scopus 로고    scopus 로고
    • e-(g-glutamyl)lysine cross-links of spore coat proteins and transglutaminase activity in Bacillus subtilis
    • Kobayashi K., Kumazawa Y., Miwa K., and Yamanaka S. e-(g-glutamyl)lysine cross-links of spore coat proteins and transglutaminase activity in Bacillus subtilis. FEMS Microbiol. Lett. 144 (1996) 157-160
    • (1996) FEMS Microbiol. Lett. , vol.144 , pp. 157-160
    • Kobayashi, K.1    Kumazawa, Y.2    Miwa, K.3    Yamanaka, S.4
  • 23
    • 0032088105 scopus 로고    scopus 로고
    • Molecular cloning of the transglutaminase gene from Bacillus subtilis and its expression in Escherichia coli
    • Kobayashi K., Hashiguchi K., Yokozeki K., and Yamanaka S. Molecular cloning of the transglutaminase gene from Bacillus subtilis and its expression in Escherichia coli. Biosci. Biotechnol. Biochem. 62 (1998) 1109-1114
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1109-1114
    • Kobayashi, K.1    Hashiguchi, K.2    Yokozeki, K.3    Yamanaka, S.4
  • 26
    • 4344718438 scopus 로고    scopus 로고
    • Transglutaminase-mediated cross-linking of GerQ in the coats of Bacillus subtilis spores
    • Ragkousi K., and Setlow P. Transglutaminase-mediated cross-linking of GerQ in the coats of Bacillus subtilis spores. J. Bacteriol. 186 (2004) 5567-5575
    • (2004) J. Bacteriol. , vol.186 , pp. 5567-5575
    • Ragkousi, K.1    Setlow, P.2
  • 28
    • 33745763019 scopus 로고    scopus 로고
    • Modification of GerQ reveals a functional relationship between Tgl and YabG in the coat of Bacillus subtilis spore
    • Kuwana R., Okuda N., Takamatsu H., and Watabe K. Modification of GerQ reveals a functional relationship between Tgl and YabG in the coat of Bacillus subtilis spore. J. Biochem. 139 (2006) 887-901
    • (2006) J. Biochem. , vol.139 , pp. 887-901
    • Kuwana, R.1    Okuda, N.2    Takamatsu, H.3    Watabe, K.4
  • 30
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., and Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4 (2003) 140-156
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 32
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie A.G. Integration of macromolecular diffraction data. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1696-1702
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1696-1702
    • Leslie, A.G.1
  • 33
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763.
    • The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763.
  • 34
    • 1142310715 scopus 로고    scopus 로고
    • Interactions among CotB, CotG, and CotH during assembly of the Bacillus subtilis spore coat
    • Zilhao R., Serrano M., Isticato R., Ricca E., Moran Jr. C.P., and Henriques A.O. Interactions among CotB, CotG, and CotH during assembly of the Bacillus subtilis spore coat. J. Bacteriol. 186 (2004) 1110-1119
    • (2004) J. Bacteriol. , vol.186 , pp. 1110-1119
    • Zilhao, R.1    Serrano, M.2    Isticato, R.3    Ricca, E.4    Moran Jr., C.P.5    Henriques, A.O.6
  • 35
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 36
    • 10844238943 scopus 로고    scopus 로고
    • Unattened high-density cell growth and induction of protein expression with the overnight express autoinduction system
    • Grabski A., Mehler M., and Drott D. Unattened high-density cell growth and induction of protein expression with the overnight express autoinduction system. Innovations 17 (2003) 3-6
    • (2003) Innovations , vol.17 , pp. 3-6
    • Grabski, A.1    Mehler, M.2    Drott, D.3


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