메뉴 건너뛰기




Volumn 287, Issue 28, 2012, Pages 23381-23396

Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BACTERIAL CELLS; BACTERIOCINS; CRITICAL SIZE; DELETION MUTANTS; DISULFIDE BONDS; FULL-LENGTH PROTEINS; IMMUNITY PROTEINS; IN-VITRO; IN-VIVO; INNER MEMBRANES; MECHANISTIC STUDIES; N-TERMINALS; PEPTIDOGLYCANS; PERIPLASM; RECEPTOR-BINDING DOMAINS; STRUCTURAL ANALOGIES; T4 LYSOZYME; TARGET SITES; UPTAKE MECHANISM; WILD TYPES; WILD-TYPE ENZYMES; YERSINIA PESTIS;

EID: 84863613709     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.362913     Document Type: Article
Times cited : (43)

References (53)
  • 2
    • 0020366141 scopus 로고
    • ColicinMis an inhibitor of murein biosynthesis
    • Schaller, K., Höltje, J. V., and Braun, V. (1982) ColicinMis an inhibitor of murein biosynthesis. J. Bacteriol. 152, 994-1000
    • (1982) J. Bacteriol. , vol.152 , pp. 994-1000
    • Schaller, K.1    Höltje, J.V.2    Braun, V.3
  • 3
    • 0018087063 scopus 로고
    • Pesticin-dependent generation of osmotically stable spheroplast-like structures
    • Hall, P. J., and Brubaker, R. R. (1978) Pesticin-dependent generation of somotically stable spheroplast-like structures. J. Bacteriol. 136, 786-789 (Pubitemid 9068376)
    • (1978) Journal of Bacteriology , vol.136 , Issue.2 , pp. 786-789
    • Hall, P.J.1    Brubaker, R.R.2
  • 5
    • 0029994995 scopus 로고    scopus 로고
    • Periplasmic location of the pesticin immunity protein suggests inactivation of pesticin in the periplasm
    • Pilsl, H., Killmann, H., Hantke, K., and Braun, V. (1996) Periplasmic location of the pesticin immunity protein suggests inactivation of pesticin in the periplasm. J. Bacteriol. 178, 2431-2435 (Pubitemid 26124444)
    • (1996) Journal of Bacteriology , vol.178 , Issue.8 , pp. 2431-2435
    • Pilsl, H.1    Killmann, H.2    Hantke, K.3    Braun, V.4
  • 7
    • 34548179597 scopus 로고    scopus 로고
    • Structure of the complex of the colicin E2 R-domain and its BtuB receptor: The outer membrane colicin translocon
    • DOI 10.1074/jbc.M703004200
    • Sharma, O., Yamashita, E., Zhalnina, M. V., Zakharov, S. D., Datsenko, K. A., Wanner, B. L., and Cramer, W. A. (2007) Structure of the complex of the colicin E2 R domain and its BtuB receptor. The outer membrane colicin translocon. J. Biol. Chem. 282, 23163-23170 (Pubitemid 47311941)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23163-23170
    • Sharma, O.1    Yamashita, E.2    Zhalnina, M.V.3    Zakharov, S.D.4    Datsenko, K.A.5    Wanner, B.L.6    Cramer, W.A.7
  • 8
    • 34249095469 scopus 로고    scopus 로고
    • Structure of colicin I receptor bound to the R-domain of colicin Ia: Implications for protein import
    • DOI 10.1038/sj.emboj.7601693, PII 7601693
    • Buchanan, S. K., Lukacik, P., Grizot, S., Ghirlando, R., Ali, M. M., Barnard, T. J., Jakes, K. S., Kienker, P. K., and Esser, L. (2007) Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import. EMBO J. 26, 2594-2604 (Pubitemid 46788319)
    • (2007) EMBO Journal , vol.26 , Issue.10 , pp. 2594-2604
    • Buchanan, S.K.1    Lukacik, P.2    Grizot, S.3    Ghirlando, R.4    Ali, M.M.U.5    Barnard, T.J.6    Jakes, K.S.7    Kienker, P.K.8    Esser, L.9
  • 9
    • 75149196290 scopus 로고    scopus 로고
    • The colicin Ia receptor, Cir, is also the translocator for colicin Ia
    • Jakes, K. S., and Finkelstein, A. (2010) The colicin Ia receptor, Cir, is also the translocator for colicin Ia. Mol. Microbiol. 75, 567-578
    • (2010) Mol. Microbiol. , vol.75 , pp. 567-578
    • Jakes, K.S.1    Finkelstein, A.2
  • 10
    • 0030472245 scopus 로고    scopus 로고
    • Structural and functional organization of the Yersinia pestis bacteriocin pesticin gene cluster
    • Rakin, A., Boolgakowa, E., and Heesemann, J. (1996) Structural and functional organization of the Yersinia pestis bacteriocin pesticin gene cluster. Microbiology 142, 3415-3424 (Pubitemid 27026367)
    • (1996) Microbiology , vol.142 , Issue.12 , pp. 3415-3424
    • Rakin, A.1    Boolgakowa, E.2    Heesemann, J.3
  • 12
    • 79953219089 scopus 로고    scopus 로고
    • Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone
    • Helbig, S., Patzer, S. I., Schiene-Fischer, C., Zeth, K., and Braun, V. (2011) Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone. J. Biol. Chem. 286, 6280-6290
    • (2011) J. Biol. Chem. , vol.286 , pp. 6280-6290
    • Helbig, S.1    Patzer, S.I.2    Schiene-Fischer, C.3    Zeth, K.4    Braun, V.5
  • 13
    • 0002014756 scopus 로고    scopus 로고
    • Site-directed mutagenesis in 1 day with >80% efficiency
    • Papworth, C., Bauer, J. C., Braman, J., and Wright, D. A. (1996) Site-directed mutagenesis in 1 day with >80% efficiency. Strategies 9, 3-4
    • (1996) Strategies , vol.9 , pp. 3-4
    • Papworth, C.1    Bauer, J.C.2    Braman, J.3    Wright, D.A.4
  • 14
    • 4143117919 scopus 로고    scopus 로고
    • Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans
    • DOI 10.1016/j.jmb.2004.07.004, PII S0022283604008149
    • Hanoulle, X., Rollet, E., Clantin, B., Landrieu, I., Odberg-Ferragut, C., Lippens, G., Bohin, J. P., and Villeret, V. (2004) Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans. J. Mol. Biol. 342, 195-205 (Pubitemid 39094515)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.1 , pp. 195-205
    • Hanoulle, X.1    Rollet, E.2    Clantin, B.3    Landrieu, I.4    Odberg-Ferragut, C.5    Lippens, G.6    Bohin, J.-P.7    Villeret, V.8
  • 15
    • 76449106188 scopus 로고    scopus 로고
    • Integration, scaling, space-group assignment and post-refinement
    • Kabsch, W. (2010) Integration, scaling, space-group assignment and post-refinement. Acta Crystallogr. D Biol. Crystallogr. 66, 133-144
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 133-144
    • Kabsch, W.1
  • 16
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein, C., Blanc, E., Roversi, P., and Bricogne, G. (2007) Automated structure solution with autoSHARP. Methods Mol. Biol. 364, 215-230 (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 17
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E. Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E. Combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 18
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for x-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S., and Perrakis, A. (2008) Automated macromolecular model building for x-ray crystallography using ARP/wARP version 7. Nat. Protoc. 3, 1171-1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 19
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D Biol. Crystallogr. 62, 1002-1011
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 22
    • 0000243829 scopus 로고
    • PROCHECK. A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK. A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm, L., Kääriäinen, S., Rosenström, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite version 3. Bioinformatics 24, 2780-2781 (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 24
    • 13444283414 scopus 로고    scopus 로고
    • Control of bacteriophage T4 tail lysozyme activity during the infection process
    • DOI 10.1016/j.jmb.2004.12.042
    • Kanamaru, S., Ishiwata, Y., Suzuki, T., Rossmann, M. G., and Arisaka, F. (2005) Control of bacteriophage T4 tail lysozyme activity during the infection process. J. Mol. Biol. 346, 1013-1020 (Pubitemid 40215526)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.4 , pp. 1013-1020
    • Kanamaru, S.1    Ishiwata, Y.2    Suzuki, T.3    Rossmann, M.G.4    Arisaka, F.5
  • 25
    • 0028794520 scopus 로고
    • The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue
    • Weaver, L. H., Grütter, M. G., and Matthews, B. W. (1995) The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J. Mol. Biol. 245, 54-68
    • (1995) J. Mol. Biol. , vol.245 , pp. 54-68
    • Weaver, L.H.1    Grütter, M.G.2    Matthews, B.W.3
  • 26
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • DOI 10.1038/35090602
    • Vocadlo, D. J., Davies, G. J., Laine, R., and Withers, S. G. (2001) Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835-838 (Pubitemid 32801467)
    • (2001) Nature , vol.412 , Issue.6849 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 27
    • 0025049224 scopus 로고
    • Import-defective colicin B derivatives mutated in the TonB box
    • Mende, J., and Braun, V. (1990) Import-defective colicin B derivatives mutated in the TonB box. Mol. Microbiol. 4, 1523-1533
    • (1990) Mol. Microbiol. , vol.4 , pp. 1523-1533
    • Mende, J.1    Braun, V.2
  • 28
    • 16844366149 scopus 로고    scopus 로고
    • Import of the transfer RNase colicin D requires site-specific interaction with the energy-transducing protein TonB
    • DOI 10.1128/JB.187.8.2693-2697.2005
    • Mora, L., Diaz, N., Buckingham, R. H., and de Zamaroczy, M. (2005) Import of the transfer RNase colicin D requires site-specific interaction with the energy-transducing protein TonB. J. Bacteriol. 187, 2693-2697 (Pubitemid 40490373)
    • (2005) Journal of Bacteriology , vol.187 , Issue.8 , pp. 2693-2697
    • Mora, L.1    Diaz, N.2    Buckingham, R.H.3    De Zamaroczy, M.4
  • 29
    • 54449087613 scopus 로고    scopus 로고
    • Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli
    • Zeth, K., Römer, C., Patzer, S. I., and Braun, V. (2008) Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli. J. Biol. Chem. 283, 25324-25331
    • (2008) J. Biol. Chem. , vol.283 , pp. 25324-25331
    • Zeth, K.1    Römer, C.2    Patzer, S.I.3    Braun, V.4
  • 30
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Å resolution
    • DOI 10.1111/j.1365-2958.2003.03884.x
    • Hilsenbeck, J. L., Park, H., Chen, G., Youn, B., Postle, K., and Kang, C. (2004) Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 Åresolution. Mol. Microbiol. 51, 711-720 (Pubitemid 38233938)
    • (2004) Molecular Microbiology , vol.51 , Issue.3 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 32
    • 0025280089 scopus 로고
    • Colicin M is only bactericidal when provided from outside the cell
    • Harkness, R. E., and Braun, V. (1990) ColicinMis only bactericidal when provided from outside the cell. Mol. Gen. Genet. 222, 37-40 (Pubitemid 20219856)
    • (1990) Molecular and General Genetics , vol.222 , Issue.1 , pp. 37-40
    • Harkness, R.E.1    Braun, V.2
  • 33
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 35
    • 0027730754 scopus 로고
    • A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme
    • Kuroki, R., Weaver, L. H., and Matthews, B. W. (1993)Acovalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme. Science 262, 2030-2033 (Pubitemid 24041881)
    • (1993) Science , vol.262 , Issue.5142 , pp. 2030-2033
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 37
    • 65249096720 scopus 로고    scopus 로고
    • Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain
    • Arnold, T., Zeth, K., and Linke, D. (2009) Structure and function of colicin S4, a colicin with a duplicated receptor-binding domain. J. Biol. Chem. 284, 6403-6413
    • (2009) J. Biol. Chem. , vol.284 , pp. 6403-6413
    • Arnold, T.1    Zeth, K.2    Linke, D.3
  • 38
    • 0024385856 scopus 로고
    • Assembly of colicin genes from a few DNA fragments. Nucleotide sequence of colicin D
    • Roos, U., Harkness, R. E., and Braun, V. (1989) Assembly of colicin genes from a few DNA fragments. Nucleotide sequence of colicin D. Mol. Microbiol. 3, 891-902 (Pubitemid 19214077)
    • (1989) Molecular Microbiology , vol.3 , Issue.7 , pp. 891-902
    • Roos, U.1    Harkness, R.E.2    Braun, V.3
  • 39
    • 0036589206 scopus 로고    scopus 로고
    • Bacteriocin diversity: Ecological and evolutionary perspectives
    • DOI 10.1016/S0300-9084(02)01421-9, PII S0300908402014219
    • Riley, M. A., and Wertz, J. E. (2002) Bacteriocin diversity. Ecological and evolutionary perspectives. Biochimie 84, 357-364 (Pubitemid 35350866)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 357-364
    • Riley, M.A.1    Wertz, J.E.2
  • 40
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • DOI 10.1016/S0300-9084(02)01427-X, PII S030090840201427X
    • Braun, V., Patzer, S. I., and Hantke, K. (2002) Ton-dependent colicins and microcins. Modular design and evolution. Biochimie 84, 365-380 (Pubitemid 35350867)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 41
    • 0018759646 scopus 로고
    • Mode of action of pesticin: N-acetylglucosaminidase activity
    • Ferber, D. M., and Brubaker, R. R. (1979) Mode of action of pesticin. N-Acetylglucosaminidase activity. J. Bacteriol. 139, 495-501 (Pubitemid 9225583)
    • (1979) Journal of Bacteriology , vol.139 , Issue.2 , pp. 495-501
    • Ferber, D.M.1    Brubaker, R.R.2
  • 42
    • 3042855401 scopus 로고    scopus 로고
    • Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells
    • DOI 10.1128/JB.186.14.4520-4527.2004
    • Penfold, C. N., Healy, B., Housden, N. G., Boetzel, R., Vankemmelbeke, M., Moore, G. R., Kleanthous, C., and James, R. (2004) Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells. J. Bacteriol. 186, 4520-4527 (Pubitemid 38891015)
    • (2004) Journal of Bacteriology , vol.186 , Issue.14 , pp. 4520-4527
    • Penfold, C.N.1    Healy, B.2    Housden, N.G.3    Boetzel, R.4    Vankemmelbeke, M.5    Moore, G.R.6    Kleanthous, C.7    James, R.8
  • 43
    • 0027938907 scopus 로고
    • Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering
    • Duché, D., Baty, D., Chartier, M., and Letellier, L. (1994) Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering. J. Biol. Chem. 269, 24820-24825 (Pubitemid 24311742)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.40 , pp. 24820-24825
    • Duche, D.1    Baty, D.2    Chartier, M.3    Letellier, L.4
  • 44
    • 44949113393 scopus 로고    scopus 로고
    • Investigating early events in receptor binding and translocation of colicin E9 using synchronized cell killing and proteolytic cleavage
    • DOI 10.1128/JB.00047-08
    • Zhang, Y., Vankemmelbeke, M. N., Holland, L. E., Walker, D. C., James, R., and Penfold, C. N. (2008) Investigating early events in receptor binding and translocation of colicin E9 using synchronized cell killing and proteolytic cleavage. J. Bacteriol. 190, 4342-4350 (Pubitemid 351812882)
    • (2008) Journal of Bacteriology , vol.190 , Issue.12 , pp. 4342-4350
    • Zhang, Y.1    Vankemmelbeke, M.N.2    Holland, L.E.3    Walker, D.C.4    James, R.5    Penfold, C.N.6
  • 45
    • 57049103480 scopus 로고    scopus 로고
    • Primary events in the colicin translocon. FRET analysis of colicin unfolding initiated by binding to BtuB and OmpF
    • Zakharov, S. D., Sharma, O., Zhalnina, M. V., and Cramer, W. A. (2008) Primary events in the colicin translocon. FRET analysis of colicin unfolding initiated by binding to BtuB and OmpF. Biochemistry 47, 12802-12809
    • (2008) Biochemistry , vol.47 , pp. 12802-12809
    • Zakharov, S.D.1    Sharma, O.2    Zhalnina, M.V.3    Cramer, W.A.4
  • 46
    • 34249792101 scopus 로고    scopus 로고
    • Colicin E2 is still in contact with its receptor and import machinery when its nuclease domain enters the cytoplasm
    • Duché, D. (2007) Colicin E2 is still in contact with its receptor and import machinery when its nuclease domain enters the cytoplasm. J. Bacteriol. 189, 4217-4222
    • (2007) J. Bacteriol. , vol.189 , pp. 4217-4222
    • Duché, D.1
  • 47
    • 80051681504 scopus 로고    scopus 로고
    • FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm
    • Chauleau, M., Mora, L., Serba, J., and de Zamaroczy, M. (2011) FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm. J. Biol. Chem. 286, 29397-29407
    • (2011) J. Biol. Chem. , vol.286 , pp. 29397-29407
    • Chauleau, M.1    Mora, L.2    Serba, J.3    De Zamaroczy, M.4
  • 48
    • 78449293752 scopus 로고    scopus 로고
    • Swimming against the tide. Progress and challenges in our understanding of colicin translocation
    • Kleanthous, C. (2010) Swimming against the tide. Progress and challenges in our understanding of colicin translocation. Nat. Rev. Microbiol. 8, 843-848
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 843-848
    • Kleanthous, C.1
  • 49
    • 0019467025 scopus 로고
    • Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: Implications for the mechanism of catalysis
    • DOI 10.1016/0022-2836(81)90398-3
    • Anderson, W. F., Grütter, M. G., Remington, S. J., Weaver, L. H., and Matthews, B. W. (1981) Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme. Implications for the mechanism of catalysis. J. Mol. Biol. 147, 523-543 (Pubitemid 11082558)
    • (1981) Journal of Molecular Biology , vol.147 , Issue.4 , pp. 523-543
    • Anderson, W.F.1    Grutter, M.G.2    Remington, S.J.3
  • 50
    • 77956944538 scopus 로고
    • (Boyer, P. D., ed) 3rd Ed., Academic Press, New York
    • Tsugita, A. (1971) in The Enzymes (Boyer, P. D., ed) 3rd Ed., pp. 343-411, Academic Press, New York
    • (1971) The Enzymes , pp. 343-411
    • Tsugita, A.1
  • 51
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high level expression of cloned genes
    • Studier, F. W., and Moffatt, B. A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high level expression of cloned genes. J. Mol. Biol. 189, 113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 52
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • DOI 10.1006/jmbi.1996.0399
    • Miroux, B., and Walker, J. E. (1996) Overproduction of proteins in Escherichia coli. Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298 (Pubitemid 26254109)
    • (1996) Journal of Molecular Biology , vol.260 , Issue.3 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 53
    • 0028291473 scopus 로고
    • The pesticin receptor of Yersinia enterocolitica: A novel virulence factor with dual function
    • DOI 10.1111/j.1365-2958.1994.tb00420.x
    • Rakin, A., Saken, E., Harmsen, D., and Heesemann, J. (1994) The pesticin receptor of Yersinia enterocolitica. A novel virulence factor with dual function. Mol. Microbiol. 13, 253-263 (Pubitemid 24225497)
    • (1994) Molecular Microbiology , vol.13 , Issue.2 , pp. 253-263
    • Rakin, A.1    Saken, E.2    Harmsen, D.3    Heesemann, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.