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Volumn 1, Issue 5, 2006, Pages 2439-2447

Identification of eukaryotic secreted and cell surface proteins using the yeast secretion trap screen

Author keywords

[No Author keywords available]

Indexed keywords

BETA FRUCTOFURANOSIDASE; MEMBRANE PROTEIN;

EID: 34548825632     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.373     Document Type: Article
Times cited : (30)

References (46)
  • 1
    • 0034020622 scopus 로고    scopus 로고
    • Large-scale identification of secreted and membrane-associated gene products using DNA microarrays
    • Diehn, M., Eisen, M.B., Botstein, D. & Brown, P.O. Large-scale identification of secreted and membrane-associated gene products using DNA microarrays. Nat. Genet. 25, 58-62 (2000).
    • (2000) Nat. Genet , vol.25 , pp. 58-62
    • Diehn, M.1    Eisen, M.B.2    Botstein, D.3    Brown, P.O.4
  • 2
    • 10744220468 scopus 로고    scopus 로고
    • The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: A bioinformatics assessment
    • Clark, H.F. et al. The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: A bioinformatics assessment. Genome Res. 13, 2265-2270 (2003).
    • (2003) Genome Res , vol.13 , pp. 2265-2270
    • Clark, H.F.1
  • 4
    • 20544439767 scopus 로고    scopus 로고
    • Features and functions of covalently linked proteins in fungal cell walls
    • De Groot, P.W.J., Ram, A.F. & Klis, F.M. Features and functions of covalently linked proteins in fungal cell walls. Fungal Gen. Biol. 42, 657-675 (2005).
    • (2005) Fungal Gen. Biol , vol.42 , pp. 657-675
    • De Groot, P.W.J.1    Ram, A.F.2    Klis, F.M.3
  • 5
    • 20144363378 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls
    • Yin, Q.Y. et al. Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls. J. Biol Chem. 280, 20894-20901 (2005).
    • (2005) J. Biol Chem , vol.280 , pp. 20894-20901
    • Yin, Q.Y.1
  • 7
    • 0021856417 scopus 로고
    • Signal sequences: The limits of variation
    • von Heijne, G. Signal sequences: The limits of variation. J. Mol. Biol. 184, 99-105 (1985).
    • (1985) J. Mol. Biol , vol.184 , pp. 99-105
    • von Heijne, G.1
  • 8
    • 0032189258 scopus 로고    scopus 로고
    • Signal sequences: More than just greasy peptides
    • Martoglio, B. & Dobbertein, B. Signal sequences: More than just greasy peptides. Trends Cell Biol. 8, 410-415 (1998).
    • (1998) Trends Cell Biol , vol.8 , pp. 410-415
    • Martoglio, B.1    Dobbertein, B.2
  • 9
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath, K., Mothes, W., Wilkinson, B.M., Stirling, C.J. & Rapoport, T.A. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94, 795-807 (1998).
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 10
    • 0033044637 scopus 로고    scopus 로고
    • Machine learning approaches for the prediction of signal peptides and other protein sorting signals
    • Nielsen, H., Brunak, S. & von Heijne, G. Machine learning approaches for the prediction of signal peptides and other protein sorting signals. Protein Eng. 12, 3-9 (1999).
    • (1999) Protein Eng , vol.12 , pp. 3-9
    • Nielsen, H.1    Brunak, S.2    von Heijne, G.3
  • 11
    • 0033953050 scopus 로고    scopus 로고
    • Large-scale predictions of secretory proteins from mammalian genomic and EST sequences
    • Ladunga, I. Large-scale predictions of secretory proteins from mammalian genomic and EST sequences. Curr. Opin. Biotechnol. 11, 13-18 (2000).
    • (2000) Curr. Opin. Biotechnol , vol.11 , pp. 13-18
    • Ladunga, I.1
  • 12
    • 0348143178 scopus 로고    scopus 로고
    • SPEPlip: The detection of signal peptide and lipoprotein cleavage sites
    • Fariselli, P., Finocchiaro, G. & Casadio, R. SPEPlip: The detection of signal peptide and lipoprotein cleavage sites. Bioinformatics 19, 2498-2499 (2003).
    • (2003) Bioinformatics , vol.19 , pp. 2498-2499
    • Fariselli, P.1    Finocchiaro, G.2    Casadio, R.3
  • 14
    • 3242878999 scopus 로고    scopus 로고
    • PrediSi: Prediction of signal peptides and their cleavage positions
    • Hiller, K., Grote, A., Scheer, M., Munch, R. & Jahn, D. PrediSi: prediction of signal peptides and their cleavage positions. Nucleic Acids Res. 32, W375-W379 (2004).
    • (2004) Nucleic Acids Res , vol.32
    • Hiller, K.1    Grote, A.2    Scheer, M.3    Munch, R.4    Jahn, D.5
  • 15
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Kall, L., Krogh, A. & Sonnhammer, E.L.L. A combined transmembrane topology and signal peptide prediction method. J. Mol. Biol. 338, 1027-1036 (2004).
    • (2004) J. Mol. Biol , vol.338 , pp. 1027-1036
    • Kall, L.1    Krogh, A.2    Sonnhammer, E.L.L.3
  • 16
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • Small, I., Peeters, N., Legeai, F. & Lurin, C. Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences. Proteomics 4, 1581-1590 (2004).
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 17
    • 22044433038 scopus 로고    scopus 로고
    • Endoplasmic reticulum: One continuous network compartmentalized by extrinsic cues
    • Levine, T. & Rabouille, C. Endoplasmic reticulum: One continuous network compartmentalized by extrinsic cues. Curr. Opin. Cell Biol. 17 362-368 (2005).
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 362-368
    • Levine, T.1    Rabouille, C.2
  • 18
    • 21844450852 scopus 로고    scopus 로고
    • Protein sorting to the storage vacuoles of plants: A critical appraisal
    • Robinson, D.G., Oliviusson, P. & Hinz, G. Protein sorting to the storage vacuoles of plants: A critical appraisal. Traffic 6, 615-625 (2005).
    • (2005) Traffic , vol.6 , pp. 615-625
    • Robinson, D.G.1    Oliviusson, P.2    Hinz, G.3
  • 19
    • 21844468743 scopus 로고    scopus 로고
    • Unconventional secretory routes: Direct protein export across the plasma membrane of mammalian cells
    • Nickel, W. Unconventional secretory routes: Direct protein export across the plasma membrane of mammalian cells. Traffic 6, 607-614 (2005).
    • (2005) Traffic , vol.6 , pp. 607-614
    • Nickel, W.1
  • 20
    • 30344443077 scopus 로고    scopus 로고
    • Non-conventional protein secretion in yeast
    • Nombela, C., Gil, C. & Chaffin, W.L. Non-conventional protein secretion in yeast. Trends Microbiol. 14, 15-21 (2006).
    • (2006) Trends Microbiol , vol.14 , pp. 15-21
    • Nombela, C.1    Gil, C.2    Chaffin, W.L.3
  • 22
    • 0027165675 scopus 로고
    • Signal sequence trap: A cloning strategy for secreted proteins and type I membrane proteins
    • Tashiro, K. et al. Signal sequence trap: A cloning strategy for secreted proteins and type I membrane proteins. Science 261, 600-603 (1993).
    • (1993) Science , vol.261 , pp. 600-603
    • Tashiro, K.1
  • 23
    • 0029816103 scopus 로고    scopus 로고
    • Molecular cloning of a novel T cell-directed CC chemokine expressed in thymus by signal sequence trap using Epstein-Barr virus vector
    • Imai, T. et al. Molecular cloning of a novel T cell-directed CC chemokine expressed in thymus by signal sequence trap using Epstein-Barr virus vector. J. Biol. Chem. 271, 21514-21521 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 21514-21521
    • Imai, T.1
  • 24
    • 0029023713 scopus 로고
    • Capturing genes encoding membrane and secreted proteins important for mouse development
    • Skarnes, W.C., Moss, J.E., Hurtley, S.M. & Beddington, R.S.P. Capturing genes encoding membrane and secreted proteins important for mouse development. Proc. Natl. Acad. Sci. USA 92, 6592-6596 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6592-6596
    • Skarnes, W.C.1    Moss, J.E.2    Hurtley, S.M.3    Beddington, R.S.P.4
  • 25
    • 0011864425 scopus 로고
    • Fusions of secreted proteins to alkaline phosphatase: An approach for studying protein secretion
    • Hoffman, C.S. & Wright, A. Fusions of secreted proteins to alkaline phosphatase: An approach for studying protein secretion. Proc. Natl. Acad. Sci. USA 82, 5107-5111 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5107-5111
    • Hoffman, C.S.1    Wright, A.2
  • 26
    • 0033557140 scopus 로고    scopus 로고
    • A new signal sequence trap using alkaline phosphatase as a reporter
    • Chen, H. & Leder, P. A new signal sequence trap using alkaline phosphatase as a reporter. Nucleic Acids Res. 27, 1219-1222 (1999).
    • (1999) Nucleic Acids Res , vol.27 , pp. 1219-1222
    • Chen, H.1    Leder, P.2
  • 27
    • 0032936135 scopus 로고    scopus 로고
    • A signal sequence trap based on a constitutively active cytokine receptor
    • Kojima, T. & Kitamura, T. A signal sequence trap based on a constitutively active cytokine receptor. Nat. Biotechnol. 17 487-490 (1999).
    • (1999) Nat. Biotechnol , vol.17 , pp. 487-490
    • Kojima, T.1    Kitamura, T.2
  • 28
  • 29
    • 0030716915 scopus 로고    scopus 로고
    • A genetic selection for isolating cDNAs encoding secreted proteins
    • Jacobs, K.A. et al. A genetic selection for isolating cDNAs encoding secreted proteins. Gene 198, 289-296 (1997).
    • (1997) Gene , vol.198 , pp. 289-296
    • Jacobs, K.A.1
  • 30
    • 0030561540 scopus 로고    scopus 로고
    • Signal sequence trap to clone cDNAs encoding secreted or membrane-associated plant proteins
    • Kristoffersen, P., Teichmann, T., Stracke, R. & Palme, K. Signal sequence trap to clone cDNAs encoding secreted or membrane-associated plant proteins. Anal. Biochem. 243, 127-132 (1996).
    • (1996) Anal. Biochem , vol.243 , pp. 127-132
    • Kristoffersen, P.1    Teichmann, T.2    Stracke, R.3    Palme, K.4
  • 31
    • 0345148433 scopus 로고    scopus 로고
    • Selection of Arabidopsis genes encoding secreted and plasma membrane proteins
    • Goo, J.H., Park, A.R., Park, W.J. & Park, O.K. Selection of Arabidopsis genes encoding secreted and plasma membrane proteins. Plant Mol. Biol. 41, 415-423 (1999).
    • (1999) Plant Mol. Biol , vol.41 , pp. 415-423
    • Goo, J.H.1    Park, A.R.2    Park, W.J.3    Park, O.K.4
  • 32
    • 0242286654 scopus 로고    scopus 로고
    • A signal peptide secretion screen in Fucus distichus embryos reveals expression of glucanase, EGF domain-containing, and LRR receptor kinase-like polypeptides during asymmetric cell growth
    • Belanger, K.D., Wyman, A.J., Sudol, M.N., Singla-Pareek, S.L. & Quatrano, R.S. A signal peptide secretion screen in Fucus distichus embryos reveals expression of glucanase, EGF domain-containing, and LRR receptor kinase-like polypeptides during asymmetric cell growth. Planta 217, 931-950 (2003).
    • (2003) Planta , vol.217 , pp. 931-950
    • Belanger, K.D.1    Wyman, A.J.2    Sudol, M.N.3    Singla-Pareek, S.L.4    Quatrano, R.S.5
  • 33
    • 1342287271 scopus 로고    scopus 로고
    • Coordinated regulation of genes for secretion in tobacco at late developmental stages: Association with resistance against oomycetes
    • Hugot, K. et al. Coordinated regulation of genes for secretion in tobacco at late developmental stages: Association with resistance against oomycetes. Plant Physiol. 134, 1-13 (2004).
    • (2004) Plant Physiol , vol.134 , pp. 1-13
    • Hugot, K.1
  • 34
    • 24944480447 scopus 로고    scopus 로고
    • A coupled yeast signal sequence trap and transient plant expression strategy to identify genes encoding secreted proteins from peach pistils
    • Yamane, H., Lee, S.-J., Kim, B.-D., Tao, R. & Rose, J.K.C. A coupled yeast signal sequence trap and transient plant expression strategy to identify genes encoding secreted proteins from peach pistils. J. Exp. Bot. 56, 2229-2238 (2005).
    • (2005) J. Exp. Bot , vol.56 , pp. 2229-2238
    • Yamane, H.1    Lee, S.-J.2    Kim, B.-D.3    Tao, R.4    Rose, J.K.C.5
  • 36
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K. & Kimura, A. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168 (1983).
    • (1983) J. Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 37
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by the LiAc/SS carrier DNA/PEG method
    • Gietz, R.D. & Woods, R.A. Transformation of yeast by the LiAc/SS carrier DNA/PEG method. Methods Enzymol. 350, 87-96 (2002).
    • (2002) Methods Enzymol , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 38
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman, C.S. & Winston, F. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene. 57, 267-272 (1987).
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 39
    • 0034128691 scopus 로고    scopus 로고
    • DNA extraction method for screening yeast clones by PCR
    • Akada, R., Murakane, T. & Nishizawa, Y. DNA extraction method for screening yeast clones by PCR. BioTechniques 28, 668-674 (2000).
    • (2000) BioTechniques , vol.28 , pp. 668-674
    • Akada, R.1    Murakane, T.2    Nishizawa, Y.3
  • 40
    • 0035476026 scopus 로고    scopus 로고
    • Signal-sequence trap in mammalian and yeast cells: A comparison
    • Galliciotti, G. et al. Signal-sequence trap in mammalian and yeast cells: A comparison. J. Membr. Biol. 183, 175-182 (2001).
    • (2001) J. Membr. Biol , vol.183 , pp. 175-182
    • Galliciotti, G.1
  • 41
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood, J.L., Tonti-Filippini, J., Verboom, R.E. & Millar, A.H. Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol. 139, 598-609 (2005).
    • (2005) Plant Physiol , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 43
    • 33746065295 scopus 로고    scopus 로고
    • Transforming omics data into context: Bioinformatics on genomics and proteomics raw data
    • Perco, P., Rapberger, R., Siehs, C., Lukas, A., Oberbauer, R., Mayer, G. & Mayer, B. Transforming omics data into context: Bioinformatics on genomics and proteomics raw data. Electrophoresis 27, 2659-2675 (2006).
    • (2006) Electrophoresis , vol.27 , pp. 2659-2675
    • Perco, P.1    Rapberger, R.2    Siehs, C.3    Lukas, A.4    Oberbauer, R.5    Mayer, G.6    Mayer, B.7
  • 44
    • 0004270170 scopus 로고    scopus 로고
    • Ausubel, F.M. et al, eds, John Wiley & Sons, Hoboken, New Jersey, USA
    • Ausubel, F.M. et al. (eds.) Current Protocols in Molecular Biology (John Wiley & Sons, Hoboken, New Jersey, USA, 2006).
    • (2006) Current Protocols in Molecular Biology
  • 45
    • 0029199530 scopus 로고
    • Escherichia coli electrotransformation
    • Miller, E.M. & Nickoloff, J.A. Escherichia coli electrotransformation. Methods Mol. Biol. 47, 105-114 (1995).
    • (1995) Methods Mol. Biol , vol.47 , pp. 105-114
    • Miller, E.M.1    Nickoloff, J.A.2


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