메뉴 건너뛰기




Volumn 50, Issue 2, 2006, Pages 179-184

Expression, purification, and characterization of Pseudomonas aeruginosa SecA

Author keywords

ATPase; SecA

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANTIBODY; BACTERIAL PROTEIN; CARRIER PROTEIN; LIPOSOME; RECOMBINANT PROTEIN; SECA PROTEIN, BACTERIA;

EID: 33750903901     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.06.023     Document Type: Article
Times cited : (6)

References (26)
  • 1
    • 0026352441 scopus 로고
    • Characterization of membrane-associated and soluble states of SecA protein from wild-type and secA51(ts) mutant strains of Escherichia coli
    • Cabelli R.J., Dolan K.M., Qian L.P., and Oliver D.B. Characterization of membrane-associated and soluble states of SecA protein from wild-type and secA51(ts) mutant strains of Escherichia coli. J. Biol. Chem. 266 (1991) 24420-24427
    • (1991) J. Biol. Chem. , vol.266 , pp. 24420-24427
    • Cabelli, R.J.1    Dolan, K.M.2    Qian, L.P.3    Oliver, D.B.4
  • 2
    • 0034721917 scopus 로고    scopus 로고
    • Two independent mechanisms down-regulate the intrinsic SecA ATPase activity
    • Nakatogawa H., Mori H., and Ito K. Two independent mechanisms down-regulate the intrinsic SecA ATPase activity. J. Biol. Chem. 275 (2000) 33209-33212
    • (2000) J. Biol. Chem. , vol.275 , pp. 33209-33212
    • Nakatogawa, H.1    Mori, H.2    Ito, K.3
  • 3
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure
    • Durand E., Bernadac A., Ball G., Lazdunski A., Sturgis J.N., and Filloux A. Type II protein secretion in Pseudomonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure. J. Bacteriol. 185 (2003) 2749-2758
    • (2003) J. Bacteriol. , vol.185 , pp. 2749-2758
    • Durand, E.1    Bernadac, A.2    Ball, G.3    Lazdunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 4
    • 0037615052 scopus 로고    scopus 로고
    • Secretins of Pseudomonas aeruginosa: Large holes in the outer membrane
    • Bitter W. Secretins of Pseudomonas aeruginosa: Large holes in the outer membrane. Arch. Microbiol. 179 (2003) 307-314
    • (2003) Arch. Microbiol. , vol.179 , pp. 307-314
    • Bitter, W.1
  • 5
    • 0345196631 scopus 로고    scopus 로고
    • The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex
    • Meyer T.H., Menetret J.F., Breitling R., Miller K.R., Akey C.W., and Rapoport T.A. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex. J. Mol. Biol. 285 (1999) 1789-1800
    • (1999) J. Mol. Biol. , vol.285 , pp. 1789-1800
    • Meyer, T.H.1    Menetret, J.F.2    Breitling, R.3    Miller, K.R.4    Akey, C.W.5    Rapoport, T.A.6
  • 8
    • 0024291341 scopus 로고
    • SecA protein is required for secretory protein translocation into E. colimembrane vesicles
    • Cabelli R.J., Chen L., Tai P.C., and Oliver D.B. SecA protein is required for secretory protein translocation into E. colimembrane vesicles. Cell 55 (1988) 683-692
    • (1988) Cell , vol.55 , pp. 683-692
    • Cabelli, R.J.1    Chen, L.2    Tai, P.C.3    Oliver, D.B.4
  • 9
    • 0027488666 scopus 로고
    • Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase
    • Mitchell C., and Oliver D. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol. Microbiol. 10 (1993) 483-497
    • (1993) Mol. Microbiol. , vol.10 , pp. 483-497
    • Mitchell, C.1    Oliver, D.2
  • 10
    • 2342463112 scopus 로고
    • Streptomycin causes misreading of natural messenger by interacting with ribosomes after initiation
    • Tai P.C., Wallace B.J., and Davis B.D. Streptomycin causes misreading of natural messenger by interacting with ribosomes after initiation. Proc. Natl. Acad. Sci. USA. 75 (1978) 275-279
    • (1978) Proc. Natl. Acad. Sci. USA. , vol.75 , pp. 275-279
    • Tai, P.C.1    Wallace, B.J.2    Davis, B.D.3
  • 13
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 14
    • 23244445215 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of heterogeneous protein-protein interactions: Sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory
    • Dam J., and Schuck P. Sedimentation velocity analysis of heterogeneous protein-protein interactions: Sedimentation coefficient distributions c(s) and asymptotic boundary profiles from Gilbert-Jenkins theory. Biophys. J. 89 (2005) 651-666
    • (2005) Biophys. J. , vol.89 , pp. 651-666
    • Dam, J.1    Schuck, P.2
  • 15
    • 20444380585 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s)
    • Dam J., Velikovsky C.A., Mariuzza R.A., Urbanke C., and Schuck P. Sedimentation velocity analysis of heterogeneous protein-protein interactions: Lamm equation modeling and sedimentation coefficient distributions c(s). Biophys. J. 89 (2005) 619-634
    • (2005) Biophys. J. , vol.89 , pp. 619-634
    • Dam, J.1    Velikovsky, C.A.2    Mariuzza, R.A.3    Urbanke, C.4    Schuck, P.5
  • 16
    • 0025019705 scopus 로고
    • The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
    • Lill R., Dowhan W., and Wickner W. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell 60 (1990) 271-280
    • (1990) Cell , vol.60 , pp. 271-280
    • Lill, R.1    Dowhan, W.2    Wickner, W.3
  • 17
    • 0028642345 scopus 로고
    • Rapid purification of native SecA from Escherichia coli: development of a new affinity chromatography procedure
    • Kiser K.B., Arnaud P., and Schmidt M.G. Rapid purification of native SecA from Escherichia coli: development of a new affinity chromatography procedure. Curr. Microbiol. 29 (1994) 323-329
    • (1994) Curr. Microbiol. , vol.29 , pp. 323-329
    • Kiser, K.B.1    Arnaud, P.2    Schmidt, M.G.3
  • 18
    • 0036129188 scopus 로고    scopus 로고
    • Complex behavior in solution of homodimeric SecA
    • Woodbury R.L., Hardy S.J., and Randall L.L. Complex behavior in solution of homodimeric SecA. Protein Sci. 11 (2002) 875-882
    • (2002) Protein Sci. , vol.11 , pp. 875-882
    • Woodbury, R.L.1    Hardy, S.J.2    Randall, L.L.3
  • 20
    • 0015102782 scopus 로고
    • Pressure-induced dissociation of sedimenting ribosomes: effect on sedimentation patterns
    • Infante A.A., and Baierlein R. Pressure-induced dissociation of sedimenting ribosomes: effect on sedimentation patterns. Proc. Natl. Acad. Sci. USA 68 (1971) 1780-1785
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1780-1785
    • Infante, A.A.1    Baierlein, R.2
  • 21
    • 0027476802 scopus 로고
    • Characterization of a Bacillus subtilis SecA mutant protein deficient in translocation ATPase and release from the membrane
    • van der Wolk J., Klose M., Breukink E., Demel R.A., de Kruijff B., Freudl R., and Driessen A.J. Characterization of a Bacillus subtilis SecA mutant protein deficient in translocation ATPase and release from the membrane. Mol. Microbiol. 8 (1993) 31-42
    • (1993) Mol. Microbiol. , vol.8 , pp. 31-42
    • van der Wolk, J.1    Klose, M.2    Breukink, E.3    Demel, R.A.4    de Kruijff, B.5    Freudl, R.6    Driessen, A.J.7
  • 22
    • 0027513153 scopus 로고
    • Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli SecA mutants in vivo
    • Klose M., Schimz K.L., van der Wolk J., Driessen A.J., and Freudl R. Lysine 106 of the putative catalytic ATP-binding site of the Bacillus subtilis SecA protein is required for functional complementation of Escherichia coli SecA mutants in vivo. J. Biol. Chem. 268 (1993) 4504-4510
    • (1993) J. Biol. Chem. , vol.268 , pp. 4504-4510
    • Klose, M.1    Schimz, K.L.2    van der Wolk, J.3    Driessen, A.J.4    Freudl, R.5
  • 23
    • 0031936275 scopus 로고    scopus 로고
    • Identification and characterization of protease-resistant SecA fragments: SecA has two membrane-integral forms
    • Chen X., Brown T., and Tai P.C. Identification and characterization of protease-resistant SecA fragments: SecA has two membrane-integral forms. J. Bacteriol. 180 (1998) 527-537
    • (1998) J. Bacteriol. , vol.180 , pp. 527-537
    • Chen, X.1    Brown, T.2    Tai, P.C.3
  • 24
    • 0037144467 scopus 로고    scopus 로고
    • Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA
    • Hunt J.F., Weinkauf S., Henry L., Fak J.J., McNicholas P., Oliver D.B., and Deisenhofer J. Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA. Science 297 (2002) 2018-2026
    • (2002) Science , vol.297 , pp. 2018-2026
    • Hunt, J.F.1    Weinkauf, S.2    Henry, L.3    Fak, J.J.4    McNicholas, P.5    Oliver, D.B.6    Deisenhofer, J.7
  • 26
    • 0026441161 scopus 로고
    • Electron-microscopy of thin-sectioned 3-dimensional crystals of SecA protein from Escherichi coli structure in projection at 40-angstrom resolution
    • Weaver A.J., Mcdowall A.W., Oliver D.B., and Deisenhofer J. Electron-microscopy of thin-sectioned 3-dimensional crystals of SecA protein from Escherichi coli structure in projection at 40-angstrom resolution. J. Struct. Biol. 109 (1992) 87-96
    • (1992) J. Struct. Biol. , vol.109 , pp. 87-96
    • Weaver, A.J.1    Mcdowall, A.W.2    Oliver, D.B.3    Deisenhofer, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.