메뉴 건너뛰기




Volumn 162, Issue 2, 2011, Pages 180-190

Multimerization-defective variants of dodecameric secretin PulD

Author keywords

In vitro synthesis; Mutations; Oligomerization; Outer membrane protein; Secretion

Indexed keywords

BACTERIAL DNA; PROTEIN PULD; PULLULANASE; SECRETIN; UNCLASSIFIED DRUG;

EID: 79952105841     PISSN: 09232508     EISSN: 17697123     Source Type: Journal    
DOI: 10.1016/j.resmic.2011.01.006     Document Type: Article
Times cited : (23)

References (32)
  • 2
  • 3
    • 0030028530 scopus 로고    scopus 로고
    • XcpD, an outer membrane protein required for protein secretion by Xanthomonas campestris pv. campestris, forms a multimer
    • Chen L.-Y., Chen D.-Y., Miaw J., Hu N.-T. XcpD, an outer membrane protein required for protein secretion by Xanthomonas campestris pv. campestris, forms a multimer. J. Biol. Chem. 1996, 271:2703-2708.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2703-2708
    • Chen, L.-Y.1    Chen, D.-Y.2    Miaw, J.3    Hu, N.-T.4
  • 5
    • 34249825232 scopus 로고    scopus 로고
    • YaeT-independent multimerization and outer membrane association of secretin PulD
    • Collin S., Guilvout I., Chami M., Pugsley A.P. YaeT-independent multimerization and outer membrane association of secretin PulD. Mol. Microbiol. 2007, 64:1350-1357.
    • (2007) Mol. Microbiol. , vol.64 , pp. 1350-1357
    • Collin, S.1    Guilvout, I.2    Chami, M.3    Pugsley, A.P.4
  • 7
    • 33750892424 scopus 로고    scopus 로고
    • Wza, the translocon for E. coli capsular polysaccharides, defines a new class of membrane proteins
    • Dong C., Beis K., Nesper J., Brunkan-LaMontague A., Clarke B., Whitfield C., Naismith J. Wza, the translocon for E. coli capsular polysaccharides, defines a new class of membrane proteins. Nature 2006, 444:226-229.
    • (2006) Nature , vol.444 , pp. 226-229
    • Dong, C.1    Beis, K.2    Nesper, J.3    Brunkan-LaMontague, A.4    Clarke, B.5    Whitfield, C.6    Naismith, J.7
  • 8
  • 9
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • Guilvout I., Chami M., Engel A., Pugsley A.P., Bayan N. Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. EMBO J. 2006, 25:5241-5249.
    • (2006) EMBO J. , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 10
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity?
    • Guilvout I., Hardie K.R., Sauvonnet N., Pugsley A.P. Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity?. J. Bacteriol. 1999, 181:7212-7220.
    • (1999) J. Bacteriol. , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 11
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie K.R., Lory S., Pugsley A.P. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 1996, 15:978-988.
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 12
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions
    • Hardie K.R., Seydel A., Guilvout I., Pugsley A.P. The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol. Microbiol. 1996, 22:967-976.
    • (1996) Mol. Microbiol. , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, I.3    Pugsley, A.P.4
  • 13
    • 34247850883 scopus 로고    scopus 로고
    • PilQ missense mutations have diverse effects on PilQ multimer formation, piliation, and pilus function in Neisseria gonorrhoeae
    • Helm R.A., Barnhart M.M., Seifert H.S. pilQ missense mutations have diverse effects on PilQ multimer formation, piliation, and pilus function in Neisseria gonorrhoeae. J Bacteriol. 2007, 189:3198-3207.
    • (2007) J Bacteriol. , vol.189 , pp. 3198-3207
    • Helm, R.A.1    Barnhart, M.M.2    Seifert, H.S.3
  • 14
    • 0031747016 scopus 로고    scopus 로고
    • Insertion mutagenesis of XpsD, an outer-membrane protein involved in extracellular protein secretion in Xanthomonas campestris pv. campestris
    • Hu N.-T., Hung M.N., Chanhan Chen D., Tsai R.-T. Insertion mutagenesis of XpsD, an outer-membrane protein involved in extracellular protein secretion in Xanthomonas campestris pv. campestris. Microbiology 1998, 144:1479-1486.
    • (1998) Microbiology , vol.144 , pp. 1479-1486
    • Hu, N.-T.1    Hung, M.N.2    Chanhan Chen, D.3    Tsai, R.-T.4
  • 15
    • 0010461565 scopus 로고    scopus 로고
    • The assembly pathway of outer membrane protein PhoE of Escherichia coli
    • Jansen C., Heutink M., Tommassen J., de Cock H. The assembly pathway of outer membrane protein PhoE of Escherichia coli. Eur. J. Biochem 2000, 267:3792-3800.
    • (2000) Eur. J. Biochem , vol.267 , pp. 3792-3800
    • Jansen, C.1    Heutink, M.2    Tommassen, J.3    de Cock, H.4
  • 16
    • 0028363816 scopus 로고
    • PIV, a filamentous phage protein that mediates phage export across the bacterial cell envelope, forms a multimer
    • Kazmierczak B.I., Mielke D.L., Russel M., Model P. pIV, a filamentous phage protein that mediates phage export across the bacterial cell envelope, forms a multimer. J. Mol. Biol. 1994, 238:187-198.
    • (1994) J. Mol. Biol. , vol.238 , pp. 187-198
    • Kazmierczak, B.I.1    Mielke, D.L.2    Russel, M.3    Model, P.4
  • 17
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov K.V., Pardon E., Steyaert J., Hol W.G. Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 2009, 17:255-265.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 18
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T.A., Roberts J.D., Zakour R.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 1987, 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 19
  • 20
    • 0033612142 scopus 로고    scopus 로고
    • An aqueous channel for filamentous phage export
    • Marciano D.K., Russel M., Simon S.M. An aqueous channel for filamentous phage export. Science 1999, 284:1516-1519.
    • (1999) Science , vol.284 , pp. 1516-1519
    • Marciano, D.K.1    Russel, M.2    Simon, S.M.3
  • 21
    • 0028143313 scopus 로고
    • Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins
    • Meerman H.J., Georgiou G. Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins. Biotechnology (NY) 1994, 12:1107-1110.
    • (1994) Biotechnology (NY) , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgiou, G.2
  • 22
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis S., Chapon C., d'Enfert C., Pugsley A.P., Schwartz M. Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae. J. Bacteriol. 1985, 164:633-638.
    • (1985) J. Bacteriol. , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    d'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 23
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USA
    • Miller J.H. Experiments in Molecular Genetics 1972, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, USA.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 25
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen N., Stahlberg H., Pugsley A.P., Engel A. Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy. EMBO J. 2000, 19:2229-2236.
    • (2000) EMBO J. , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahlberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 26
    • 0024278694 scopus 로고
    • Targeting of porin to the outer membrane of Escherichia coli. Rate of trimer assembly and identification of a dimer intermediate
    • Reid J., Fung H., Gehring K., Klebba P.E., Nikaido H. Targeting of porin to the outer membrane of Escherichia coli. Rate of trimer assembly and identification of a dimer intermediate. J Biol. Chem. 1988, 263:7753-7759.
    • (1988) J Biol. Chem. , vol.263 , pp. 7753-7759
    • Reid, J.1    Fung, H.2    Gehring, K.3    Klebba, P.E.4    Nikaido, H.5
  • 27
    • 31344479308 scopus 로고    scopus 로고
    • Advances in understanding bacterial outer-membrane biogenesis
    • Ruiz N., Kahne D., Silhavy T.J. Advances in understanding bacterial outer-membrane biogenesis. Nat. Rev. Microbiol. 2006, 4:57-66.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 57-66
    • Ruiz, N.1    Kahne, D.2    Silhavy, T.J.3
  • 28
    • 0027986656 scopus 로고
    • Mutants at conserved positions in gene IV, a gene required for assembly and secretion of filamentous phages
    • Russel M. Mutants at conserved positions in gene IV, a gene required for assembly and secretion of filamentous phages. Mol. Microbiol. 1994, 14:357-369.
    • (1994) Mol. Microbiol. , vol.14 , pp. 357-369
    • Russel, M.1
  • 29
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik V.E., Robert-Badouy J., Condemine G. Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J. 1997, 16:3007-3016.
    • (1997) EMBO J. , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Badouy, J.2    Condemine, G.3
  • 30
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • Sklar J.G., Wu T., Kahne D., Silhavy T.J. Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev. 2007, 21:2473-2484.
    • (2007) Genes Dev. , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 32
    • 13844318282 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda H., Matsuyama S. Sorting of lipoproteins to the outer membrane in E. coli. Biochim. Biophys. Acta 2004, 1694:1-9.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 1-9
    • Tokuda, H.1    Matsuyama, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.