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Volumn 88, Issue 6, 2013, Pages 1164-1175

Haloferax volcanii archaeosortase is required for motility, mating, and C-terminal processing of the S-layer glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEOSORTASE A; GLYCOPROTEIN; SORTASE; UNCLASSIFIED DRUG;

EID: 84879018029     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12248     Document Type: Article
Times cited : (48)

References (40)
  • 1
    • 2342625231 scopus 로고    scopus 로고
    • Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes
    • Allers, T., Ngo, H.P., Mevarech, M., and Lloyd, R.G. (2004) Development of additional selectable markers for the halophilic archaeon Haloferax volcanii based on the leuB and trpA genes. Appl Environ Microbiol 70: 943-953.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 943-953
    • Allers, T.1    Ngo, H.P.2    Mevarech, M.3    Lloyd, R.G.4
  • 2
    • 77749304005 scopus 로고    scopus 로고
    • Improved strains and plasmid vectors for conditional overexpression of His-tagged proteins in Haloferax volcanii
    • Allers, T., Barak, S., Liddell, S., Wardell, K., and Mevarech, M. (2010) Improved strains and plasmid vectors for conditional overexpression of His-tagged proteins in Haloferax volcanii. Appl Environ Microbiol 76: 1759-1769.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 1759-1769
    • Allers, T.1    Barak, S.2    Liddell, S.3    Wardell, K.4    Mevarech, M.5
  • 4
    • 84861778995 scopus 로고    scopus 로고
    • Thinking outside the cell: how cadherins drive adhesion
    • Brasch, J., Harrison, O.J., Honig, B., and Shapiro, L. (2012) Thinking outside the cell: how cadherins drive adhesion. Trends Cell Biol 22: 299-310.
    • (2012) Trends Cell Biol , vol.22 , pp. 299-310
    • Brasch, J.1    Harrison, O.J.2    Honig, B.3    Shapiro, L.4
  • 5
    • 84867640103 scopus 로고    scopus 로고
    • Bacterial adhesion to animal tissues: protein determinants for recognition of extracellular matrix components
    • Chagnot, C., Listrat, A., Astruc, T., and Desvaux, M. (2012) Bacterial adhesion to animal tissues: protein determinants for recognition of extracellular matrix components. Cell Microbiol 14: 1687-1696.
    • (2012) Cell Microbiol , vol.14 , pp. 1687-1696
    • Chagnot, C.1    Listrat, A.2    Astruc, T.3    Desvaux, M.4
  • 6
    • 2142808787 scopus 로고    scopus 로고
    • A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria
    • Comfort, D., and Clubb, R.T. (2004) A comparative genome analysis identifies distinct sorting pathways in gram-positive bacteria. Infect Immun 72: 2710-2722.
    • (2004) Infect Immun , vol.72 , pp. 2710-2722
    • Comfort, D.1    Clubb, R.T.2
  • 7
    • 84879025779 scopus 로고    scopus 로고
    • The halohandbook - protocols for haloarchaeal genetics. [WWW document].
    • Dyall-Smith, M. (2004) The halohandbook - protocols for haloarchaeal genetics. [WWW document]. URL http://www.haloarchaea.com.
    • (2004)
    • Dyall-Smith, M.1
  • 8
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J.E., and Gygi, S.P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4: 207-214.
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 9
    • 0000857494 scopus 로고
    • Approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J.K., McCormack, A.L., and Yates, J.R. (1994) Approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5: 976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 11
    • 79551473399 scopus 로고    scopus 로고
    • Assembly and function of the archaeal flagellum
    • Ghosh, A., and Albers, S.V. (2011) Assembly and function of the archaeal flagellum. Biochem Soc Trans 39: 64-69.
    • (2011) Biochem Soc Trans , vol.39 , pp. 64-69
    • Ghosh, A.1    Albers, S.V.2
  • 12
    • 33748882527 scopus 로고    scopus 로고
    • Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic
    • Haft, D.H., Paulsen, I.T., Ward, N., and Selengut, J.D. (2006) Exopolysaccharide-associated protein sorting in environmental organisms: the PEP-CTERM/EpsH system. Application of a novel phylogenetic profiling heuristic. BMC Biol 4: 29.
    • (2006) BMC Biol , vol.4 , pp. 29
    • Haft, D.H.1    Paulsen, I.T.2    Ward, N.3    Selengut, J.D.4
  • 13
    • 84855870250 scopus 로고    scopus 로고
    • Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification
    • Haft, D.H., Payne, S.H., and Selengut, J.D. (2012) Archaeosortases and exosortases are widely distributed systems linking membrane transit with posttranslational modification. J Bacteriol 194: 36-48.
    • (2012) J Bacteriol , vol.194 , pp. 36-48
    • Haft, D.H.1    Payne, S.H.2    Selengut, J.D.3
  • 17
    • 43849084346 scopus 로고    scopus 로고
    • The surprisingly diverse ways that prokaryotes move
    • Jarrell, K.F., and McBride, M.J. (2008) The surprisingly diverse ways that prokaryotes move. Nat Rev Microbiol 6: 466-476.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 466-476
    • Jarrell, K.F.1    McBride, M.J.2
  • 18
    • 84871985639 scopus 로고    scopus 로고
    • Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations
    • Kandiba, L., Guan, Z., and Eichler, J. (2012) Lipid modification gives rise to two distinct Haloferax volcanii S-layer glycoprotein populations. Biochim Biophys Acta 1828: 938-943.
    • (2012) Biochim Biophys Acta , vol.1828 , pp. 938-943
    • Kandiba, L.1    Guan, Z.2    Eichler, J.3
  • 19
    • 0033580929 scopus 로고    scopus 로고
    • Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium
    • Kikuchi, A., Sagami, H., and Ogura, K. (1999) Evidence for covalent attachment of diphytanylglyceryl phosphate to the cell-surface glycoprotein of Halobacterium halobium. J Biol Chem 274: 18011-18016.
    • (1999) J Biol Chem , vol.274 , pp. 18011-18016
    • Kikuchi, A.1    Sagami, H.2    Ogura, K.3
  • 20
    • 50149117169 scopus 로고    scopus 로고
    • Spectral probabilities and generating functions of tandem mass spectra: a strike against decoy databases
    • Kim, S., Gupta, N., and Pevzner, P.A. (2008) Spectral probabilities and generating functions of tandem mass spectra: a strike against decoy databases. J Proteome Res 7: 3354-3363.
    • (2008) J Proteome Res , vol.7 , pp. 3354-3363
    • Kim, S.1    Gupta, N.2    Pevzner, P.A.3
  • 21
    • 65549129105 scopus 로고    scopus 로고
    • Mechanism for sortase localization and the role of sortase localization in efficient pilus assembly in Enterococcus faecalis
    • Kline, K.A., Kau, A.L., Chen, S.L., Lim, A., Pinkner, J.S., Rosch, J., etal. (2009) Mechanism for sortase localization and the role of sortase localization in efficient pilus assembly in Enterococcus faecalis. J Bacteriol 191: 3237-3247.
    • (2009) J Bacteriol , vol.191 , pp. 3237-3247
    • Kline, K.A.1    Kau, A.L.2    Chen, S.L.3    Lim, A.4    Pinkner, J.S.5    Rosch, J.6
  • 22
    • 0037106458 scopus 로고    scopus 로고
    • Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation
    • Konrad, Z., and Eichler, J. (2002) Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation. Biochem J 366: 959-964.
    • (2002) Biochem J , vol.366 , pp. 959-964
    • Konrad, Z.1    Eichler, J.2
  • 23
    • 41149134523 scopus 로고    scopus 로고
    • Fully automated four-column capillary LC-MS system for maximizing throughput in proteomic analyses
    • Livesay, E.A., Tang, K., Taylor, B.K., Buschbach, M.A., Hopkins, D.F., LaMarche, B.L., etal. (2008) Fully automated four-column capillary LC-MS system for maximizing throughput in proteomic analyses. Anal Chem 80: 294-302.
    • (2008) Anal Chem , vol.80 , pp. 294-302
    • Livesay, E.A.1    Tang, K.2    Taylor, B.K.3    Buschbach, M.A.4    Hopkins, D.F.5    LaMarche, B.L.6
  • 24
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S.K., Liu, G., Ton-That, H., and Schneewind, O. (1999) Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285: 760-763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 25
    • 0022003836 scopus 로고
    • Genetic transfer in Halobacterium volcanii
    • Mevarech, M., and Werczberger, R. (1985) Genetic transfer in Halobacterium volcanii. J Bacteriol 162: 461-462.
    • (1985) J Bacteriol , vol.162 , pp. 461-462
    • Mevarech, M.1    Werczberger, R.2
  • 26
    • 6344280371 scopus 로고    scopus 로고
    • Proteomic analyses using an accurate mass and time tag strategy
    • 626-633, 636 passim.
    • Pasa-Tolic, L., Masselon, C., Barry, R.C., Shen, Y., and Smith, R.D. (2004) Proteomic analyses using an accurate mass and time tag strategy. Biotechniques 37: 621-624, 626-633, 636 passim.
    • (2004) Biotechniques , vol.37 , pp. 621-624
    • Pasa-Tolic, L.1    Masselon, C.2    Barry, R.C.3    Shen, Y.4    Smith, R.D.5
  • 27
    • 0037013286 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring
    • Perry, A.M., Ton-That, H., Mazmanian, S.K., and Schneewind, O. (2002) Anchoring of surface proteins to the cell wall of Staphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring. J Biol Chem 277: 16241-16248.
    • (2002) J Biol Chem , vol.277 , pp. 16241-16248
    • Perry, A.M.1    Ton-That, H.2    Mazmanian, S.K.3    Schneewind, O.4
  • 28
    • 0024447751 scopus 로고
    • The mechanism of DNA transfer in the mating system of an archaebacterium
    • Rosenshine, I., Tchelet, R., and Mevarech, M. (1989) The mechanism of DNA transfer in the mating system of an archaebacterium. Science 245: 1387-1389.
    • (1989) Science , vol.245 , pp. 1387-1389
    • Rosenshine, I.1    Tchelet, R.2    Mevarech, M.3
  • 29
    • 84858222518 scopus 로고    scopus 로고
    • Protein secretion and surface display in Gram-positive bacteria
    • Schneewind, O., and Missiakas, D.M. (2012) Protein secretion and surface display in Gram-positive bacteria. Philos Trans R Soc Lond B Biol Sci 367: 1123-1139.
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 1123-1139
    • Schneewind, O.1    Missiakas, D.M.2
  • 30
    • 54349083037 scopus 로고    scopus 로고
    • De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins
    • Shen, Y., Tolić, N., Hixson, K.K., Purvine, S.O., Anderson, G.A., and Smith, R.D. (2008) De novo sequencing of unique sequence tags for discovery of post-translational modifications of proteins. Anal Chem 80: 7742-7754.
    • (2008) Anal Chem , vol.80 , pp. 7742-7754
    • Shen, Y.1    Tolić, N.2    Hixson, K.K.3    Purvine, S.O.4    Anderson, G.A.5    Smith, R.D.6
  • 31
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 1: 2856-2860.
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 32
    • 0036253914 scopus 로고    scopus 로고
    • An Accurate mass tag strategy for quantitative and high throughput proteome measurements
    • Smith, R.D., Anderson, G.A., Lipton, M.S., Paša-Tolic, L., Shen, Y., Conrads, T.P., etal. (2002) An Accurate mass tag strategy for quantitative and high throughput proteome measurements. Proteomics 2: 513-523.
    • (2002) Proteomics , vol.2 , pp. 513-523
    • Smith, R.D.1    Anderson, G.A.2    Lipton, M.S.3    Paša-Tolic, L.4    Shen, Y.5    Conrads, T.P.6
  • 33
    • 82155168216 scopus 로고    scopus 로고
    • Sortase enzymes in Gram-positive bacteria
    • Spirig, T., Weiner, E.M., and Clubb, R.T. (2011) Sortase enzymes in Gram-positive bacteria. Mol Microbiol 82: 1044-1059.
    • (2011) Mol Microbiol , vol.82 , pp. 1044-1059
    • Spirig, T.1    Weiner, E.M.2    Clubb, R.T.3
  • 34
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper, M. (1987) Halobacterial glycoprotein biosynthesis. Biochim Biophys Acta 906: 69-79.
    • (1987) Biochim Biophys Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 35
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper, M., Berg, E., Mengele, R., and Strobel, I. (1990) Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J Bacteriol 172: 7111-7118.
    • (1990) J Bacteriol , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4
  • 36
    • 84875766625 scopus 로고    scopus 로고
    • Diversity and subcellular distribution of archaeal secreted proteins
    • Szabo, Z., and Pohlschroder, M. (2012) Diversity and subcellular distribution of archaeal secreted proteins. Front Microbiol 3: 207.
    • (2012) Front Microbiol , vol.3 , pp. 207
    • Szabo, Z.1    Pohlschroder, M.2
  • 37
    • 0033588339 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction
    • Ton-That, H., and Schneewind, O. (1999) Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction. J Biol Chem 274: 24316-24320.
    • (1999) J Biol Chem , vol.274 , pp. 24316-24320
    • Ton-That, H.1    Schneewind, O.2
  • 38
    • 0033607265 scopus 로고    scopus 로고
    • Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
    • Ton-That, H., Liu, G., Mazmanian, S.K., Faull, K.F., and Schneewind, O. (1999) Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif. Proc Natl Acad Sci USA 96: 12424-12429.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12424-12429
    • Ton-That, H.1    Liu, G.2    Mazmanian, S.K.3    Faull, K.F.4    Schneewind, O.5
  • 39
    • 77953975121 scopus 로고    scopus 로고
    • Haloferax volcanii flagella are required for motility but are not involved in PibD-dependent surface adhesion
    • Tripepi, M., Imam, S., and Pohlschroder, M. (2010) Haloferax volcanii flagella are required for motility but are not involved in PibD-dependent surface adhesion. J Bacteriol 192: 3093-3102.
    • (2010) J Bacteriol , vol.192 , pp. 3093-3102
    • Tripepi, M.1    Imam, S.2    Pohlschroder, M.3
  • 40
    • 0037291906 scopus 로고    scopus 로고
    • Genes involved in the synthesis of the exopolysaccharide methanolan by the obligate methylotroph Methylobacillus sp strain 12S
    • Yoshida, T., Ayabe, Y., Yasunaga, M., Usami, Y., Habe, H., Nojiri, H., and Omori, T. (2003) Genes involved in the synthesis of the exopolysaccharide methanolan by the obligate methylotroph Methylobacillus sp strain 12S. Microbiology 149: 431-444.
    • (2003) Microbiology , vol.149 , pp. 431-444
    • Yoshida, T.1    Ayabe, Y.2    Yasunaga, M.3    Usami, Y.4    Habe, H.5    Nojiri, H.6    Omori, T.7


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