메뉴 건너뛰기




Volumn 446, Issue 4, 2014, Pages 901-905

An internal hydrophobic helical domain of Bacillus subtilis enolase is essential but not sufficient as a non-cleavable signal for its secretion

Author keywords

Enolase; Hydrophobic domain; Secretion

Indexed keywords

ENOLASE; HYDROPHOBIC DOMAIN; SECRETION;

EID: 84899486231     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.03.032     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 80053578297 scopus 로고    scopus 로고
    • Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis
    • C.-K. Yang, H. Ewis, X.-Z. Zhang, C.-D. Lu, H.J. Hu, Y. Pan, A.T. Abdelal, and P.-C. Tai Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis J. Bacteriol. 193 20 2011 5607 5615
    • (2011) J. Bacteriol. , vol.193 , Issue.20 , pp. 5607-5615
    • Yang, C.-K.1    Ewis, H.2    Zhang, X.-Z.3    Lu, C.-D.4    Hu, H.J.5    Pan, Y.6    Abdelal, A.T.7    Tai, P.-C.8
  • 2
    • 30344443077 scopus 로고    scopus 로고
    • Non-conventional protein secretion in yeast
    • C. Nombela, C. Gil, and W.L. Chaffin Non-conventional protein secretion in yeast Trends Microbiol. 14 1 2006 15 21
    • (2006) Trends Microbiol. , vol.14 , Issue.1 , pp. 15-21
    • Nombela, C.1    Gil, C.2    Chaffin, W.L.3
  • 3
    • 0042706146 scopus 로고    scopus 로고
    • Moonlighting proteins: Old proteins learning new tricks
    • C.J. Jeffery Moonlighting proteins: old proteins learning new tricks Trends Genet. 19 8 2003 415 417
    • (2003) Trends Genet. , vol.19 , Issue.8 , pp. 415-417
    • Jeffery, C.J.1
  • 6
    • 34247547010 scopus 로고    scopus 로고
    • Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions
    • I. Pal-Bhowmick, H.K. Vora, and G.K. Jarori Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions Malar. J. 6 2007 45
    • (2007) Malar. J. , vol.6 , pp. 45
    • Pal-Bhowmick, I.1    Vora, H.K.2    Jarori, G.K.3
  • 7
    • 20844444771 scopus 로고    scopus 로고
    • Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: Genetic requirements
    • S. Guiral, T.J. Mitchell, B. Martin, and J.P. Claverys Competence-programmed predation of noncompetent cells in the human pathogen Streptococcus pneumoniae: genetic requirements Proc. Natl. Acad. Sci. USA 102 24 2005 8710 8715
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.24 , pp. 8710-8715
    • Guiral, S.1    Mitchell, T.J.2    Martin, B.3    Claverys, J.P.4
  • 9
    • 0027403372 scopus 로고
    • Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells
    • A.K. Dudani, C. Cummings, S. Hashemi, and P.R. Ganz Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells Thromb. Res. 69 2 1993 185 196
    • (1993) Thromb. Res. , vol.69 , Issue.2 , pp. 185-196
    • Dudani, A.K.1    Cummings, C.2    Hashemi, S.3    Ganz, P.R.4
  • 10
    • 0032486286 scopus 로고    scopus 로고
    • Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • V. Pancholi, and V.A. Fischetti Alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci J. Biol. Chem. 273 23 1998 14503 14515
    • (1998) J. Biol. Chem. , vol.273 , Issue.23 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 11
    • 34247854961 scopus 로고    scopus 로고
    • Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis
    • A. Knaust, M.V. Weber, S. Hammerschmidt, S. Bergmann, M. Frosch, and O. Kurzai Cytosolic proteins contribute to surface plasminogen recruitment of Neisseria meningitidis J. Bacteriol. 189 8 2007 3246 3255
    • (2007) J. Bacteriol. , vol.189 , Issue.8 , pp. 3246-3255
    • Knaust, A.1    Weber, M.V.2    Hammerschmidt, S.3    Bergmann, S.4    Frosch, M.5    Kurzai, O.6
  • 14
    • 0041810543 scopus 로고    scopus 로고
    • Crystal structure of Enterococcus hirae enolase at 2.8 A resolution
    • T. Hosaka, T. Meguro, I. Yamato, and Y. Shirakihara Crystal structure of Enterococcus hirae enolase at 2.8 A resolution J. Biochem. 133 6 2003 817 823
    • (2003) J. Biochem. , vol.133 , Issue.6 , pp. 817-823
    • Hosaka, T.1    Meguro, T.2    Yamato, I.3    Shirakihara, Y.4
  • 15
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • K. Arnold, L. Bordoli, J. Kopp, and T. Schwede The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 2 2006 195 201
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 16
    • 34249994314 scopus 로고    scopus 로고
    • To be or not to be: Predicting soluble SecAs as membrane proteins
    • H.-J. Hu, J. Holley, J. He, R.w. Harrison, H. Yang, P.C. Tai, and Y. Pan To be or not to be: predicting soluble SecAs as membrane proteins IEEE Trans. Nanobiosci. 6 2 2007 168 179
    • (2007) IEEE Trans. Nanobiosci. , vol.6 , Issue.2 , pp. 168-179
    • Hu, H.-J.1    Holley, J.2    He, J.3    Yang, H.4    Tai, P.C.5    Pan, Y.6
  • 17
    • 84899476655 scopus 로고    scopus 로고
    • signalP 3.0 server. Accessed on March, 2008
    • signalP 3.0 server [ http://www.cbs.dtu.dk/services/SignalP/ ]. Accessed on March, 2008.
  • 18
    • 79951928644 scopus 로고    scopus 로고
    • CSHProtocols: using deoxycholate and trichloroacetic acid to concentrate proteins and remove interfering substances
    • CSHProtocols: using deoxycholate and trichloroacetic acid to concentrate proteins and remove interfering substances. 2006:doi: http://dx.doi.org/10.1101/ pdb.prot4258.
    • (2006)
  • 19
    • 0035957996 scopus 로고    scopus 로고
    • Mechanisms governing subcellular localization and function of human RGS2
    • S.P. Heximer, H. Lim, J.L. Bernard, and K.J. Blumer Mechanisms governing subcellular localization and function of human RGS2 J. Biol. Chem. 276 17 2001 14195 14203
    • (2001) J. Biol. Chem. , vol.276 , Issue.17 , pp. 14195-14203
    • Heximer, S.P.1    Lim, H.2    Bernard, J.L.3    Blumer, K.J.4
  • 21
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • G. von Heijne Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule J. Mol. Biol. 225 2 1992 487 494
    • (1992) J. Mol. Biol. , vol.225 , Issue.2 , pp. 487-494
    • Von Heijne, G.1
  • 22
    • 0028109251 scopus 로고
    • Effect of alteration of charged residues at the N termini of signal peptides on protein export in Bacillus subtilis
    • M. Chen, and V. Nagarajan Effect of alteration of charged residues at the N termini of signal peptides on protein export in Bacillus subtilis J. Bacteriol. 176 18 1994 5796 5801
    • (1994) J. Bacteriol. , vol.176 , Issue.18 , pp. 5796-5801
    • Chen, M.1    Nagarajan, V.2
  • 23
    • 33645070224 scopus 로고    scopus 로고
    • Release of the type i secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli
    • C. Balsalobre, J.M. Silvan, S. Berglund, Y. Mizunoe, B.E. Uhlin, and S.N. Wai Release of the type I secreted alpha-haemolysin via outer membrane vesicles from Escherichia coli Mol. Microbiol. 59 1 2006 99 112
    • (2006) Mol. Microbiol. , vol.59 , Issue.1 , pp. 99-112
    • Balsalobre, C.1    Silvan, J.M.2    Berglund, S.3    Mizunoe, Y.4    Uhlin, B.E.5    Wai, S.N.6
  • 24
    • 33645473483 scopus 로고    scopus 로고
    • Outer membrane vesicles from group B Neisseria meningitidis gna33 mutant: Proteomic and immunological comparison with detergent-derived outer membrane vesicles
    • G. Ferrari, I. Garaguso, J. Adu-Bobie, F. Doro, A.R. Taddei, A. Biolchi, B. Brunelli, M.M. Giuliani, M. Pizza, and N. Norais et al. Outer membrane vesicles from group B Neisseria meningitidis gna33 mutant: proteomic and immunological comparison with detergent-derived outer membrane vesicles Proteomics 6 6 2006 1856 1866
    • (2006) Proteomics , vol.6 , Issue.6 , pp. 1856-1866
    • Ferrari, G.1    Garaguso, I.2    Adu-Bobie, J.3    Doro, F.4    Taddei, A.R.5    Biolchi, A.6    Brunelli, B.7    Giuliani, M.M.8    Pizza, M.9    Norais, N.10
  • 25
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • D.M. Engelman, T.A. Steitz, and A. Goldman Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins Annu. Rev. Biophys. Biophys. Chem. 15 1986 321 353
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 26
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 27
    • 77952502987 scopus 로고    scopus 로고
    • Reverse vaccinology approach identify an Echinococcus granulosus tegumental membrane protein enolase as vaccine candidate
    • W. Gan, G. Zhao, H. Xu, W. Wu, W. Du, J. Huang, X. Yu, and X. Hu Reverse vaccinology approach identify an Echinococcus granulosus tegumental membrane protein enolase as vaccine candidate Parasitol. Res. 106 4 2010 873 882
    • (2010) Parasitol. Res. , vol.106 , Issue.4 , pp. 873-882
    • Gan, W.1    Zhao, G.2    Xu, H.3    Wu, W.4    Du, W.5    Huang, J.6    Yu, X.7    Hu, X.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.