메뉴 건너뛰기




Volumn 6, Issue 7, 2007, Pages 2420-2434

Proteins in different Synechocystis compartments have distinguishing N-terminal features: A combined proteomics and multivariate sequence analysis

Author keywords

Cyanobacteria; Leader peptidase; Multivariate sequence analysis; Signal peptide

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; HYDROPHOBICITY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; PROTEOMICS; SEQUENCE ANALYSIS; SYNECHOCYSTIS;

EID: 34547183476     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr0605973     Document Type: Article
Times cited : (28)

References (101)
  • 1
    • 0002578627 scopus 로고
    • Supramolecular membrane organization
    • Bryant, D. A, Ed, Kluwer: Dordrecht
    • Gantt, E. Supramolecular membrane organization. In The Molecular Biology of Cyanobacteria; Bryant, D. A., Ed.; Kluwer: Dordrecht, 1994; pp 119-138.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 119-138
    • Gantt, E.1
  • 2
    • 29144514372 scopus 로고    scopus 로고
    • The three-dimensional structure of the cyanobacterium Synechocystis sp. PCC 6803
    • van de Meene, A. M.; Hohmann-Marriott, M. F.; Vermaas, W. F.; Roberson, R. W. The three-dimensional structure of the cyanobacterium Synechocystis sp. PCC 6803. Arch. Microbiol. 2006, 184 (5), 259-270.
    • (2006) Arch. Microbiol , vol.184 , Issue.5 , pp. 259-270
    • van de Meene, A.M.1    Hohmann-Marriott, M.F.2    Vermaas, W.F.3    Roberson, R.W.4
  • 3
    • 33744500753 scopus 로고    scopus 로고
    • Liberton, M.; Howard, Berg, R.; Heuser, J.; Roth, R.; Pakrasi, H. B. infrastructure, of the membrane systems in the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. Protoplasma 2006, 227 (2-4), 129-138.
    • Liberton, M.; Howard, Berg, R.; Heuser, J.; Roth, R.; Pakrasi, H. B. infrastructure, of the membrane systems in the unicellular cyanobacterium Synechocystis sp. strain PCC 6803. Protoplasma 2006, 227 (2-4), 129-138.
  • 4
    • 33947105612 scopus 로고    scopus 로고
    • Thylakoid membrane perforations and connectivity enable intracellular traffic in cyanobacteria
    • Nevo, R.; Charuvi, D.; Shimoni, E.; Schwarz, R.; Kaplan, A.; Ohad, I.; Reich, Z. Thylakoid membrane perforations and connectivity enable intracellular traffic in cyanobacteria. EMBO J. 2007, 26 (5), 1467-1473.
    • (2007) EMBO J , vol.26 , Issue.5 , pp. 1467-1473
    • Nevo, R.1    Charuvi, D.2    Shimoni, E.3    Schwarz, R.4    Kaplan, A.5    Ohad, I.6    Reich, Z.7
  • 5
    • 0038236448 scopus 로고    scopus 로고
    • Membrane-specific targeting of green fluorescent protein by the Tat pathway in the cyanobacterium Synechocystis PCC6803
    • Spence, E.; Sarcina, M.; Ray, N.; Moller, S. G.; Mullineaux, C. W.; Robinson, C. Membrane-specific targeting of green fluorescent protein by the Tat pathway in the cyanobacterium Synechocystis PCC6803. Mol. Microbiol. 2003, 48 (6), 1481-1489.
    • (2003) Mol. Microbiol , vol.48 , Issue.6 , pp. 1481-1489
    • Spence, E.1    Sarcina, M.2    Ray, N.3    Moller, S.G.4    Mullineaux, C.W.5    Robinson, C.6
  • 8
    • 0033967631 scopus 로고    scopus 로고
    • The Tat protein export pathway
    • Berks, B. C.; Sargent, F.; Palmer, T. The Tat protein export pathway. Mol. Microbiol. 2000, 35 (2), 260-274.
    • (2000) Mol. Microbiol , vol.35 , Issue.2 , pp. 260-274
    • Berks, B.C.1    Sargent, F.2    Palmer, T.3
  • 9
    • 10744228022 scopus 로고    scopus 로고
    • Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli
    • Alami, M.; Luke, I.; Deitermann, S.; Eisner, G.; Koch, H. G.; Brunner, J.; Muller, M. Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli. Mol. Cell. Proteomics 2003, 12 (4), 937-946.
    • (2003) Mol. Cell. Proteomics , vol.12 , Issue.4 , pp. 937-946
    • Alami, M.1    Luke, I.2    Deitermann, S.3    Eisner, G.4    Koch, H.G.5    Brunner, J.6    Muller, M.7
  • 11
    • 0034832014 scopus 로고    scopus 로고
    • Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
    • Sargent, F.; Gohlke, U.; De Leeuw, E.; Stanley, N. R.; Palmer, T.; Saibil, H. R.; Berks, B. C. Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure. Eur. J. Biochem. 2001, 268 (12), 3361-3367.
    • (2001) Eur. J. Biochem , vol.268 , Issue.12 , pp. 3361-3367
    • Sargent, F.1    Gohlke, U.2    De Leeuw, E.3    Stanley, N.R.4    Palmer, T.5    Saibil, H.R.6    Berks, B.C.7
  • 12
    • 0035827675 scopus 로고    scopus 로고
    • TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli
    • Bolhuis, A.; Mathers, J. E.; Thomas, J. D.; Barrett, C. M.; Robinson, C. TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli. J. Biol. Chem. 2001, 276 (23), 20213-2019.
    • (2001) J. Biol. Chem , vol.276 , Issue.23 , pp. 20213-22019
    • Bolhuis, A.1    Mathers, J.E.2    Thomas, J.D.3    Barrett, C.M.4    Robinson, C.5
  • 14
  • 15
    • 8144225875 scopus 로고    scopus 로고
    • Coordinating assembly and export of complex bacterial proteins
    • Jack, R. L.; Buchanan, G.; Dubini, A.; Hatzixanthis, K.; Palmer, T.; Sargent, F. Coordinating assembly and export of complex bacterial proteins. EMBO J. 2004, 23 (20), 3962-3972.
    • (2004) EMBO J , vol.23 , Issue.20 , pp. 3962-3972
    • Jack, R.L.1    Buchanan, G.2    Dubini, A.3    Hatzixanthis, K.4    Palmer, T.5    Sargent, F.6
  • 16
    • 3042589734 scopus 로고    scopus 로고
    • Localization of the Tat translocon components in Escherichia coli
    • Berthelmann, F.; Bruser, T. Localization of the Tat translocon components in Escherichia coli. FEBS Lett. 2004, 569 (1-3), 82-88.
    • (2004) FEBS Lett , vol.569 , Issue.1-3 , pp. 82-88
    • Berthelmann, F.1    Bruser, T.2
  • 17
    • 0026453267 scopus 로고
    • Signal peptidases in prokaryotes and eukaryotes - a new protease family
    • Dalbey, R. E.; Von Heijne, G. Signal peptidases in prokaryotes and eukaryotes - a new protease family. Trends Biochem. Sci. 1992, 17 (11), 474-478.
    • (1992) Trends Biochem. Sci , vol.17 , Issue.11 , pp. 474-478
    • Dalbey, R.E.1    Von Heijne, G.2
  • 18
    • 0025340734 scopus 로고
    • Lipoproteins in bacteria
    • Hayashi, S.; Wu, H. C. Lipoproteins in bacteria. J. Bioenerg. Biomembr. 1990, 22 (3), 451-471.
    • (1990) J. Bioenerg. Biomembr , vol.22 , Issue.3 , pp. 451-471
    • Hayashi, S.1    Wu, H.C.2
  • 20
    • 4544384204 scopus 로고    scopus 로고
    • Lipoprotein trafficking in Escherichia coli
    • Narita, S.; Matsuyama, S.; Tokuda, H. Lipoprotein trafficking in Escherichia coli. Arch. Microbiol. 2004, 182 (1), 1-6.
    • (2004) Arch. Microbiol , vol.182 , Issue.1 , pp. 1-6
    • Narita, S.1    Matsuyama, S.2    Tokuda, H.3
  • 21
    • 0033797930 scopus 로고    scopus 로고
    • Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic proteins in cells grown at low and high salt concentrations
    • Fulda, S.; Huang, F.; Nilsson, F.; Hagemann, M.; Norling, B. Proteomics of Synechocystis sp. strain PCC 6803. Identification of periplasmic proteins in cells grown at low and high salt concentrations. Eur. J. Biochem. 2000, 267 (19), 5900-5907.
    • (2000) Eur. J. Biochem , vol.267 , Issue.19 , pp. 5900-5907
    • Fulda, S.1    Huang, F.2    Nilsson, F.3    Hagemann, M.4    Norling, B.5
  • 22
    • 32944467003 scopus 로고    scopus 로고
    • Proteomic screening of salt-stress-induced changes in plasma membranes of Synechocystis sp. strain PCC 6803
    • Huang, F.; Fulda, S.; Hagemann, M.; Norling, B. Proteomic screening of salt-stress-induced changes in plasma membranes of Synechocystis sp. strain PCC 6803. Proteomics 2006, 6 (3), 910-920.
    • (2006) Proteomics , vol.6 , Issue.3 , pp. 910-920
    • Huang, F.1    Fulda, S.2    Hagemann, M.3    Norling, B.4
  • 24
    • 3042733909 scopus 로고    scopus 로고
    • Isolation of outer membrane of Synechocystis sp. PCC 6803 and its proteomic characterization
    • Huang, F.; Hedman, E.; Funk, C.; Kieselbach, T.; Schroder, W. P.; Norling, B. Isolation of outer membrane of Synechocystis sp. PCC 6803 and its proteomic characterization. Mol. Cell. Proteomics 2004, 3 (6), 586-595.
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.6 , pp. 586-595
    • Huang, F.1    Hedman, E.2    Funk, C.3    Kieselbach, T.4    Schroder, W.P.5    Norling, B.6
  • 25
    • 29544451629 scopus 로고    scopus 로고
    • Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC 6803
    • Srivastava, R.; Pisareva, T.; Norling, B. Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC 6803. Proteomics 2005, 5 (18), 4905-4916.
    • (2005) Proteomics , vol.5 , Issue.18 , pp. 4905-4916
    • Srivastava, R.1    Pisareva, T.2    Norling, B.3
  • 26
    • 0037427963 scopus 로고    scopus 로고
    • The general protein secretory pathway: Phylogenetic analyses leading to evolutionary conclusions
    • Cao, T. B.; Saier, M. H., Jr. The general protein secretory pathway: phylogenetic analyses leading to evolutionary conclusions. Biochim. Biophys. Acta 2003, 1609 (1), 115-125.
    • (2003) Biochim. Biophys. Acta , vol.1609 , Issue.1 , pp. 115-125
    • Cao, T.B.1    Saier Jr., M.H.2
  • 27
    • 0028178852 scopus 로고
    • Identification and characterization of the sec-A protein homologue in the cyanobacterium Synechococcus PCC7942
    • Nakai, M.; Nohara, T.; Sugita, D.; Endo, T. Identification and characterization of the sec-A protein homologue in the cyanobacterium Synechococcus PCC7942. Biochem. Biophys. Res. Commun. 1994, 200 (2), 844-851.
    • (1994) Biochem. Biophys. Res. Commun , vol.200 , Issue.2 , pp. 844-851
    • Nakai, M.1    Nohara, T.2    Sugita, D.3    Endo, T.4
  • 28
    • 0027336391 scopus 로고
    • Sec-Y protein is localized in both the cytoplasmic and thylakoid membranes in the cyanobacterium Synechococcus PCC7942
    • Nakai, M.; Sugita, D.; Omata, T.; Endo, T. Sec-Y protein is localized in both the cytoplasmic and thylakoid membranes in the cyanobacterium Synechococcus PCC7942. Biochem. Biophys. Res. Commun. 1993, 193 (1), 228-234.
    • (1993) Biochem. Biophys. Res. Commun , vol.193 , Issue.1 , pp. 228-234
    • Nakai, M.1    Sugita, D.2    Omata, T.3    Endo, T.4
  • 29
    • 1642555810 scopus 로고    scopus 로고
    • Evidence for polar positional information independent of cell division and nucleoid occlusion
    • Janakiraman, A.; Goldberg, M. B. Evidence for polar positional information independent of cell division and nucleoid occlusion. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (3), 835-840.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.3 , pp. 835-840
    • Janakiraman, A.1    Goldberg, M.B.2
  • 30
    • 2642540881 scopus 로고    scopus 로고
    • A microdomain for protein secretion in Gram-positive bacteria
    • Rosch, J.; Caparon, M. A microdomain for protein secretion in Gram-positive bacteria. Science 2004, 304 (5676), 1513-1515.
    • (2004) Science , vol.304 , Issue.5676 , pp. 1513-1515
    • Rosch, J.1    Caparon, M.2
  • 32
    • 4644262108 scopus 로고    scopus 로고
    • Traffic spotting: Poles apart
    • Pugsley, A. P.; Buddelmeijer, N. Traffic spotting: poles apart. Mol. Microbiol. 2004, 53 (6), 1559-1562.
    • (2004) Mol. Microbiol , vol.53 , Issue.6 , pp. 1559-1562
    • Pugsley, A.P.1    Buddelmeijer, N.2
  • 33
    • 0031588694 scopus 로고    scopus 로고
    • Relation between amino acid composition and cellular location of proteins
    • Cedano, J.; Aloy, P.; Perez-Pons, J. A.; Querol, E. Relation between amino acid composition and cellular location of proteins. J. Mol. Biol. 1997, 266 (3), 594-600.
    • (1997) J. Mol. Biol , vol.266 , Issue.3 , pp. 594-600
    • Cedano, J.1    Aloy, P.2    Perez-Pons, J.A.3    Querol, E.4
  • 34
    • 0032548904 scopus 로고    scopus 로고
    • Adaptation of protein surfaces to subcellular location
    • Andrade, M. A.; O'Donoghue, S. I.; Rost, B. Adaptation of protein surfaces to subcellular location. J. Mol. Biol. 1998, 276 (2), 517-525.
    • (1998) J. Mol. Biol , vol.276 , Issue.2 , pp. 517-525
    • Andrade, M.A.1    O'Donoghue, S.I.2    Rost, B.3
  • 35
    • 0035876479 scopus 로고    scopus 로고
    • Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria
    • Fukuchi, S.; Nishikawa, K. Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. J. Mol. Biol. 2001, 309 (4), 835-843.
    • (2001) J. Mol. Biol , vol.309 , Issue.4 , pp. 835-843
    • Fukuchi, S.1    Nishikawa, K.2
  • 36
    • 33748937555 scopus 로고    scopus 로고
    • The surprising complexity of signal sequences
    • Hegde, R. S.; Bernstein, H. D. The surprising complexity of signal sequences. Trends Biochem. Sci. 2006, 31 (10), 563-571.
    • (2006) Trends Biochem. Sci , vol.31 , Issue.10 , pp. 563-571
    • Hegde, R.S.1    Bernstein, H.D.2
  • 37
    • 0033135048 scopus 로고    scopus 로고
    • Different sequence patterns in signal peptides from mycoplasmas, other gram-positive bacteria, and Escherichia coli: A multivariate data analysis
    • Edman, M.; Jarhede, T.; Sjostrom, M.; Wieslander, A. Different sequence patterns in signal peptides from mycoplasmas, other gram-positive bacteria, and Escherichia coli: a multivariate data analysis. Proteins 1999, 35 (2), 195-205.
    • (1999) Proteins , vol.35 , Issue.2 , pp. 195-205
    • Edman, M.1    Jarhede, T.2    Sjostrom, M.3    Wieslander, A.4
  • 38
    • 0345735670 scopus 로고    scopus 로고
    • Functional activity of eukaryotic signal sequences in Escherichia coli: The ovalbumin family of serine protease inhibitors
    • Belin, D.; Guzman, L. M.; Bost, S.; Konakova, M.; Silva, F.; Beckwith, J. Functional activity of eukaryotic signal sequences in Escherichia coli: the ovalbumin family of serine protease inhibitors. J. Mol. Biol. 2004, 335 (2), 437-453.
    • (2004) J. Mol. Biol , vol.335 , Issue.2 , pp. 437-453
    • Belin, D.1    Guzman, L.M.2    Bost, S.3    Konakova, M.4    Silva, F.5    Beckwith, J.6
  • 39
    • 0034029906 scopus 로고    scopus 로고
    • The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria
    • Kajava, A. V.; Zolov, S. N.; Kalinin, A. E.; Nesmeyanova, M. A. The net charge of the first 18 residues of the mature sequence affects protein translocation across the cytoplasmic membrane of gram-negative bacteria. J. Bacteriol. 2000, 182 (8), 2163-2169.
    • (2000) J. Bacteriol , vol.182 , Issue.8 , pp. 2163-2169
    • Kajava, A.V.1    Zolov, S.N.2    Kalinin, A.E.3    Nesmeyanova, M.A.4
  • 40
    • 4344660408 scopus 로고    scopus 로고
    • A directed evolution strategy for optimized export of recombinant proteins reveals critical determinants for preprotein discharge
    • Kaderbhai, M. A.; Davey, H. M.; Kaderbbai, N. N. A directed evolution strategy for optimized export of recombinant proteins reveals critical determinants for preprotein discharge. Protein Sci. 2004, 13 (9), 2458-2469.
    • (2004) Protein Sci , vol.13 , Issue.9 , pp. 2458-2469
    • Kaderbhai, M.A.1    Davey, H.M.2    Kaderbbai, N.N.3
  • 41
    • 84984087585 scopus 로고
    • Simple conditions for growth of unicellular blue-green algae on plates
    • Allen, M. M. Simple conditions for growth of unicellular blue-green algae on plates. J. Phycol. 1968, 4 1-4.
    • (1968) J. Phycol , vol.4 , pp. 1-4
    • Allen, M.M.1
  • 42
    • 0033032596 scopus 로고    scopus 로고
    • Isolation of salt-induced periplasmic proteins from Synechocystis sp. strain PCC 6803
    • Fulda, S.; Mikkat, S.; Schroder, W.; Hagemann, M. Isolation of salt-induced periplasmic proteins from Synechocystis sp. strain PCC 6803. Arch. Microbiol. 1999, 171 (3), 214-217.
    • (1999) Arch. Microbiol , vol.171 , Issue.3 , pp. 214-217
    • Fulda, S.1    Mikkat, S.2    Schroder, W.3    Hagemann, M.4
  • 43
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J.; Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 1982, 157 (1), 105-132.
    • (1982) J. Mol. Biol , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 44
    • 11144325691 scopus 로고
    • Partial least-squares regression: A tutorial
    • Geladi, P.; Kowalski, B. R. Partial least-squares regression: A tutorial Anal. Chim. Acta 1986, 185, 1-17.
    • (1986) Anal. Chim. Acta , vol.185 , pp. 1-17
    • Geladi, P.1    Kowalski, B.R.2
  • 45
    • 0003122173 scopus 로고    scopus 로고
    • Partial least squares projections to latent structures (PLS) in chemistry
    • Schleyer, P, Allinger, N. L, Clark, T, Dasteiger, J, Kollman, P. A, Schaefer, H. F, III, Eds, John Wiley & Sons: Chichester, U.K
    • Wold, S.; Eriksson, L.; Sjöström, M. Partial least squares projections to latent structures (PLS) in chemistry. In The Encyclopedia of Computational Chemistry; Schleyer, P., Allinger, N. L., Clark, T., Dasteiger, J., Kollman, P. A., Schaefer, H. F., III, Eds.; John Wiley & Sons: Chichester, U.K., 1998; pp 2006-2021.
    • (1998) The Encyclopedia of Computational Chemistry , pp. 2006-2021
    • Wold, S.1    Eriksson, L.2    Sjöström, M.3
  • 46
    • 0032517828 scopus 로고    scopus 로고
    • Modelling and diagnostics of batch processes and analogous kinetic experiments
    • Wold, S.; Kettaneh, N.; Fridén, H.; Holmberg, A. Modelling and diagnostics of batch processes and analogous kinetic experiments. Chemom. Intell. Lab. Syst. 1998, 33 331-333.
    • (1998) Chemom. Intell. Lab. Syst , vol.33 , pp. 331-333
    • Wold, S.1    Kettaneh, N.2    Fridén, H.3    Holmberg, A.4
  • 48
    • 0023192524 scopus 로고
    • Peptide quantitative structure-activity relationships, a multivariate approach
    • Hellberg, S.; Sjostrom, M.; Skagerberg, B.; Wold, S. Peptide quantitative structure-activity relationships, a multivariate approach. J. Med. Chem. 1987, 30 (7), 1126-1135.
    • (1987) J. Med. Chem , vol.30 , Issue.7 , pp. 1126-1135
    • Hellberg, S.1    Sjostrom, M.2    Skagerberg, B.3    Wold, S.4
  • 49
  • 50
    • 84951601886 scopus 로고
    • Cross-validatory, estimation of the number of components in factor and principal components models
    • Wold, S. Cross-validatory, estimation of the number of components in factor and principal components models. Technometrics 1978, 20, 397-406.
    • (1978) Technometrics , vol.20 , pp. 397-406
    • Wold, S.1
  • 51
    • 4644354102 scopus 로고    scopus 로고
    • Recognition of fold and sugar linkage for glycosyltransferases by multivariate sequence analysis
    • Rosen, M. L.; Edman, M.; Sjostrom, M.; Wieslander, A. Recognition of fold and sugar linkage for glycosyltransferases by multivariate sequence analysis. J. Biol. Chem. 2004, 279 (37), 38683-38692.
    • (2004) J. Biol. Chem , vol.279 , Issue.37 , pp. 38683-38692
    • Rosen, M.L.1    Edman, M.2    Sjostrom, M.3    Wieslander, A.4
  • 52
    • 0032475858 scopus 로고    scopus 로고
    • 2D-isolation of pure plasma and thylakoid membranes from the cyanobacterium Synechocystis sp. PCC 6803
    • Norling, B.; Zak, E.; Andersson, B.; Pakrasi, H. 2D-isolation of pure plasma and thylakoid membranes from the cyanobacterium Synechocystis sp. PCC 6803. FEBS Lett. 1998, 436 (2), 189-192.
    • (1998) FEBS Lett , vol.436 , Issue.2 , pp. 189-192
    • Norling, B.1    Zak, E.2    Andersson, B.3    Pakrasi, H.4
  • 53
    • 0035818524 scopus 로고    scopus 로고
    • The initial steps of biogenesis of cyanobacterial photosystems occur in plasma membranes
    • Zak, E.; Norling, B.; Maitra, R.; Huang, F.; Andersson, B.; Pakrasi, H. B. The initial steps of biogenesis of cyanobacterial photosystems occur in plasma membranes. Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (23), 13443-1348.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , Issue.23 , pp. 13443-11348
    • Zak, E.1    Norling, B.2    Maitra, R.3    Huang, F.4    Andersson, B.5    Pakrasi, H.B.6
  • 54
    • 0037172810 scopus 로고    scopus 로고
    • Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides
    • Kashino, Y.; Lauber, W. M.; Carroll, J. A.; Wang, Q.; Whitmarsh, J.; Satoh, K.; Pakrasi, H. B. Proteomic analysis of a highly active photosystem II preparation from the cyanobacterium Synechocystis sp. PCC 6803 reveals the presence of novel polypeptides. Biochemistry 2002, 41 (25), 8004-8012.
    • (2002) Biochemistry , vol.41 , Issue.25 , pp. 8004-8012
    • Kashino, Y.1    Lauber, W.M.2    Carroll, J.A.3    Wang, Q.4    Whitmarsh, J.5    Satoh, K.6    Pakrasi, H.B.7
  • 56
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen, J. D.; Nielsen, H.; von Heijne, G.; Brunak, S. Improved prediction of signal peptides: SignalP 3.0. J. Mol. Biol. 2004, 340 (4), 783-795.
    • (2004) J. Mol. Biol , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 57
    • 0348044549 scopus 로고    scopus 로고
    • Genome trees constructed using five different approaches suggest new major bacterial clades
    • Wolf, Y. I.; Rogozin, I. B.; Grishin, N. V.; Tatusov, R. L.; Koonin, E. V. Genome trees constructed using five different approaches suggest new major bacterial clades. BMC Evol. Biol. 2001, 1, 8.
    • (2001) BMC Evol. Biol , vol.1 , pp. 8
    • Wolf, Y.I.1    Rogozin, I.B.2    Grishin, N.V.3    Tatusov, R.L.4    Koonin, E.V.5
  • 58
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: A genome-based survey of the secretome
    • Tjalsma, H.; Bolhuis, A.; Jongbloed, J. D.; Bron, S.; van Dijl, J. M. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 2000, 64 (3), 515-547.
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , Issue.3 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    van Dijl, J.M.5
  • 59
    • 0025068060 scopus 로고
    • Visualization of the bacterial polysaccharide capsule
    • Bayer, M. E. Visualization of the bacterial polysaccharide capsule. Curr. Top. Microbiol. Immunol. 1990, 150 129-157.
    • (1990) Curr. Top. Microbiol. Immunol , vol.150 , pp. 129-157
    • Bayer, M.E.1
  • 60
    • 0029810703 scopus 로고    scopus 로고
    • Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: Evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation
    • Mustardy, L.; Los, D. A.; Gombos, Z.; Murata, N. Immunocytochemical localization of acyl-lipid desaturases in cyanobacterial cells: evidence that both thylakoid membranes and cytoplasmic membranes are sites of lipid desaturation. Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (19), 10524-10527.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , Issue.19 , pp. 10524-10527
    • Mustardy, L.1    Los, D.A.2    Gombos, Z.3    Murata, N.4
  • 61
    • 7244255961 scopus 로고    scopus 로고
    • Klinkert, B.; Ossenbuhl, F.; Sikorski, M.; Berry, S.; Eichacker, L.; Nickelsen, J. PratA, a periplasmic tetratricopeptide repeat protein involved in biogenesis of photosystem II in Synechocystis sp. PCC 6803. J. Biol. Chem. 2004, 279 (43), 44639-44644.
    • Klinkert, B.; Ossenbuhl, F.; Sikorski, M.; Berry, S.; Eichacker, L.; Nickelsen, J. PratA, a periplasmic tetratricopeptide repeat protein involved in biogenesis of photosystem II in Synechocystis sp. PCC 6803. J. Biol. Chem. 2004, 279 (43), 44639-44644.
  • 62
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V.; Sharif, A.; Koronakis, E.; Luisi, B.; Hughes, C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 2000, 405 (6789), 914-919.
    • (2000) Nature , vol.405 , Issue.6789 , pp. 914-919
    • Koronakis, V.1    Sharif, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 63
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud, C.; Bissery, V.; Benchetrit, T.; Mornon, J. P. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 1987, 224 (1), 149-155.
    • (1987) FEBS Lett , vol.224 , Issue.1 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 65
    • 1942505330 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions
    • Yu, C. S.; Lin, C. J.; Hwang, J. K. Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions. Protein Sci. 2004, 13 (5), 1402-1406.
    • (2004) Protein Sci , vol.13 , Issue.5 , pp. 1402-1406
    • Yu, C.S.1    Lin, C.J.2    Hwang, J.K.3
  • 66
    • 27744479231 scopus 로고    scopus 로고
    • Combining inducible protein overexpression with NMR-grade triple isotope labeling in the cyanobacterium Anabaena sp. PCC 7120
    • Desplancq, D.; Bernard, C.; Sibler, A. P.; Kieffer, B.; Miguet, L.; Potier, N.; Van Dorsselaer, A.; Weiss, E. Combining inducible protein overexpression with NMR-grade triple isotope labeling in the cyanobacterium Anabaena sp. PCC 7120. BioTechniques 2005, 39 (3), 405-411.
    • (2005) BioTechniques , vol.39 , Issue.3 , pp. 405-411
    • Desplancq, D.1    Bernard, C.2    Sibler, A.P.3    Kieffer, B.4    Miguet, L.5    Potier, N.6    Van Dorsselaer, A.7    Weiss, E.8
  • 67
    • 0028207032 scopus 로고
    • Role of signal peptides in targeting of proteins in cyanobacteria
    • Mackle, M. M.; Zilinskas, B. A. Role of signal peptides in targeting of proteins in cyanobacteria. J. Bacteriol. 1994, 176 (7), 1857-1864.
    • (1994) J. Bacteriol , vol.176 , Issue.7 , pp. 1857-1864
    • Mackle, M.M.1    Zilinskas, B.A.2
  • 68
    • 25444468656 scopus 로고    scopus 로고
    • The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA
    • Chou, Y. T.; Gierasch, L. M. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J. Biol. Chem. 2005, 280 (38), 32753-32760.
    • (2005) J. Biol. Chem , vol.280 , Issue.38 , pp. 32753-32760
    • Chou, Y.T.1    Gierasch, L.M.2
  • 70
    • 24944458963 scopus 로고    scopus 로고
    • Atomic model of the E. coli membrane-bound protein translocation complex SecYEG
    • Bostina, M.; Mohsin, B.; Kuhlbrandt, W.; Collinson, I. Atomic model of the E. coli membrane-bound protein translocation complex SecYEG. J. Mol. Biol. 2005, 352 (5), 1035-1043.
    • (2005) J. Mol. Biol , vol.352 , Issue.5 , pp. 1035-1043
    • Bostina, M.1    Mohsin, B.2    Kuhlbrandt, W.3    Collinson, I.4
  • 71
    • 27144525002 scopus 로고    scopus 로고
    • Investigating the SecY plug movement at the SecYEG translocation channel
    • Tam, P. C.; Maillard, A. P.; Chan, K. K.; Duong, F. Investigating the SecY plug movement at the SecYEG translocation channel. EMBO J. 2005, 24 (19), 3380-3388.
    • (2005) EMBO J , vol.24 , Issue.19 , pp. 3380-3388
    • Tam, P.C.1    Maillard, A.P.2    Chan, K.K.3    Duong, F.4
  • 72
    • 0034723287 scopus 로고    scopus 로고
    • Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase
    • van der Does, C.; Swaving, J.; van Klompenburg, W.; Driessen, A. J. Non-bilayer lipids stimulate the activity of the reconstituted bacterial protein translocase. J. Biol. Chem. 2000, 275 (4), 2472-248.
    • (2000) J. Biol. Chem , vol.275 , Issue.4 , pp. 2472-2248
    • van der Does, C.1    Swaving, J.2    van Klompenburg, W.3    Driessen, A.J.4
  • 73
    • 0001552671 scopus 로고
    • The lipid phase of thylakoid and cytoplasmic membranes from the blue-green algae (Cyanobacteria), Anacystis nidulans and Anabaena variabilis
    • Wada, H.; Hirasawa, R.; Omata, T.; Murata, N. The lipid phase of thylakoid and cytoplasmic membranes from the blue-green algae (Cyanobacteria), Anacystis nidulans and Anabaena variabilis. Plant Cell. Physiol. 1984, 25, 907-912.
    • (1984) Plant Cell. Physiol , vol.25 , pp. 907-912
    • Wada, H.1    Hirasawa, R.2    Omata, T.3    Murata, N.4
  • 75
    • 4644357445 scopus 로고    scopus 로고
    • Signal sequences influence membrane integration of the prion protein
    • Ott, C. M.; Lingappa, V. R. Signal sequences influence membrane integration of the prion protein. Biochemistry 2004, 43 (38), 11973-11982.
    • (2004) Biochemistry , vol.43 , Issue.38 , pp. 11973-11982
    • Ott, C.M.1    Lingappa, V.R.2
  • 76
    • 0035979713 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins: Determinants and dynamics
    • Coder, V.; Spiess, M. Topogenesis of membrane proteins: determinants and dynamics. FEBS Lett. 2001, 504 (3), 87-93.
    • (2001) FEBS Lett , vol.504 , Issue.3 , pp. 87-93
    • Coder, V.1    Spiess, M.2
  • 77
    • 13544259578 scopus 로고    scopus 로고
    • Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum
    • Higy, M.; Gander, S.; Spiess, M. Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum. Biochemistry 2005, 44 (6), 2039-2047.
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2039-2047
    • Higy, M.1    Gander, S.2    Spiess, M.3
  • 78
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy, M.; Junne, T.; Spiess, M. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 2004, 43 (40), 12716-12722.
    • (2004) Biochemistry , vol.43 , Issue.40 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 79
    • 22444450987 scopus 로고    scopus 로고
    • A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
    • Garrison, J. L.; Kunkel, E. J.; Hegde, R. S.; Taunton, J. A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum. Nature 2005, 436 (7048), 285-289.
    • (2005) Nature , vol.436 , Issue.7048 , pp. 285-289
    • Garrison, J.L.1    Kunkel, E.J.2    Hegde, R.S.3    Taunton, J.4
  • 81
    • 1542313960 scopus 로고    scopus 로고
    • Sec61p contributes to signal sequence orientation according to the positive-inside rule
    • Coder, V.; Junne, T.; Spiess, M. Sec61p contributes to signal sequence orientation according to the positive-inside rule. Mol. Biol. Cell 2004, 15 (3), 1470-1478.
    • (2004) Mol. Biol. Cell , vol.15 , Issue.3 , pp. 1470-1478
    • Coder, V.1    Junne, T.2    Spiess, M.3
  • 82
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • Rapoport, T. A.; Goder, V.; Heinrich, S. U.; Matlack, K. E. Membrane-protein integration and the role of the translocation channel. Trends Cell. Biol. 2004, 14 (10), 568-575.
    • (2004) Trends Cell. Biol , vol.14 , Issue.10 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.4
  • 83
    • 4143101547 scopus 로고    scopus 로고
    • The machinery of membrane protein assembly
    • White, S. H.; von Heijne, G. The machinery of membrane protein assembly. Curr. Opin. Struct. Biol. 2004, 14 (4), 397-404.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , Issue.4 , pp. 397-404
    • White, S.H.1    von Heijne, G.2
  • 85
    • 30744464566 scopus 로고    scopus 로고
    • Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established
    • Deutscher, J.; Saier, M. H., Jr. Ser/Thr/Tyr protein phosphorylation in bacteria - for long time neglected, now well established. J. Mol. Microbiol. Biotechnol. 2005, 9 (3-4), 125-131.
    • (2005) J. Mol. Microbiol. Biotechnol , vol.9 , Issue.3-4 , pp. 125-131
    • Deutscher, J.1    Saier Jr., M.H.2
  • 86
    • 33947245585 scopus 로고    scopus 로고
    • Sensing the light: Photoreceptive systems and signal transduction in cyanobacteria
    • Montgomery, B. L. Sensing the light: photoreceptive systems and signal transduction in cyanobacteria. Mol. Microbiol. 2007, 64 (1), 16-27.
    • (2007) Mol. Microbiol , vol.64 , Issue.1 , pp. 16-27
    • Montgomery, B.L.1
  • 87
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: Protein glycosylation in pathogenic bacteria
    • Benz, I.; Schmidt, M. A. Never say never again: protein glycosylation in pathogenic bacteria. Mol. Microbiol. 2002, 45 (2), 267-276.
    • (2002) Mol. Microbiol , vol.45 , Issue.2 , pp. 267-276
    • Benz, I.1    Schmidt, M.A.2
  • 89
    • 0030868265 scopus 로고    scopus 로고
    • Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes
    • Tjalsma, H.; Noback, M. A.; Bron, S.; Venema, G.; Yamane, K.; van Dijl, J. M. Bacillus subtilis contains four closely related type I signal peptidases with overlapping substrate specificities. Constitutive and temporally controlled expression of different sip genes. J. Biol. Chem. 1997, 272 (41), 25983-25992.
    • (1997) J. Biol. Chem , vol.272 , Issue.41 , pp. 25983-25992
    • Tjalsma, H.1    Noback, M.A.2    Bron, S.3    Venema, G.4    Yamane, K.5    van Dijl, J.M.6
  • 93
    • 0038386050 scopus 로고    scopus 로고
    • 3D-Jury: A simple approach to improve protein structure predictions
    • Ginalski, K.; Elofsson, A.; Fischer, D.; Rychlewski, L. 3D-Jury: a simple approach to improve protein structure predictions. Bioinformatics 2003, 19 (8), 1015-1018.
    • (2003) Bioinformatics , vol.19 , Issue.8 , pp. 1015-1018
    • Ginalski, K.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 94
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor
    • Paetzel, M.; Dalbey, R. E.; Strynadka, N. C. Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor. Nature 1998, 396 (6707), 186-190.
    • (1998) Nature , vol.396 , Issue.6707 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.3
  • 95
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305 (3), 567-580.
    • (2001) J. Mol. Biol , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 96
    • 0347988151 scopus 로고    scopus 로고
    • Regulation of signal peptidase by phospholipids in membrane: Characterization of phospholipid bilayer incorporated Escherichia coli signal peptidase
    • Wang, Y.; Bruckner, R.; Stein, R. L. Regulation of signal peptidase by phospholipids in membrane: characterization of phospholipid bilayer incorporated Escherichia coli signal peptidase. Biochemistry 2004, 43 (1), 265-270.
    • (2004) Biochemistry , vol.43 , Issue.1 , pp. 265-270
    • Wang, Y.1    Bruckner, R.2    Stein, R.L.3
  • 97
    • 0347635421 scopus 로고    scopus 로고
    • Geukens, N.; Frederix, F.; Reekmans, G.; Lammertyn, E.; Van, Mellaert, L.; Dehaen, W.; Maes, G.; Anne, J. Analysis of type I signal peptidase affinity and specificity for preprotein substrates. Biochem. Biophys. Res. Commun. 2004, 314 (2), 459-467.
    • Geukens, N.; Frederix, F.; Reekmans, G.; Lammertyn, E.; Van, Mellaert, L.; Dehaen, W.; Maes, G.; Anne, J. Analysis of type I signal peptidase affinity and specificity for preprotein substrates. Biochem. Biophys. Res. Commun. 2004, 314 (2), 459-467.
  • 99
    • 0041528498 scopus 로고    scopus 로고
    • Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen
    • Rutkowski, D. T.; Ott, C. M.; Polansky, J. R.; Lingappa, V. R. Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen. J. Biol. Chem. 2003, 278 (32), 30365-30372.
    • (2003) J. Biol. Chem , vol.278 , Issue.32 , pp. 30365-30372
    • Rutkowski, D.T.1    Ott, C.M.2    Polansky, J.R.3    Lingappa, V.R.4
  • 101
    • 0035957413 scopus 로고    scopus 로고
    • Vipp1 deletion mutant of Synechocystis: A connection between bacterial phage shock and thylakoid biogenesis?
    • Westphal, S.; Heins, L.; Soll, J.; Vothknecht, U. C. Vipp1 deletion mutant of Synechocystis: a connection between bacterial phage shock and thylakoid biogenesis? Proc. Natl. Acad. Sci. U.S.A. 2001, 98 (7), 4243-4248.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , Issue.7 , pp. 4243-4248
    • Westphal, S.1    Heins, L.2    Soll, J.3    Vothknecht, U.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.