메뉴 건너뛰기




Volumn 198, Issue 2 JAN, 1997, Pages 289-296

A genetic selection for isolating cDNAs encoding secreted proteins

Author keywords

Chemokine; G protein coupled receptor; Invertase; Protein secretion; Signal sequence

Indexed keywords

BETA FRUCTOFURANOSIDASE; CHEMOKINE; COMPLEMENTARY DNA; CYTOKINE; GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; RAFFINOSE; RECEPTOR; SIGNAL PEPTIDE; SUCROSE;

EID: 0030716915     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0378-1119(97)00330-2     Document Type: Article
Times cited : (248)

References (38)
  • 1
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of ura3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., Cao, L., Kleckner, N., 1987. A method for gene disruption that allows repeated use of ura3 selection in the construction of multiply disrupted yeast strains. Genetics 116, 541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 4
    • 0027288333 scopus 로고
    • Functional substitution of the signal recognition particle 54-kDa subunit by its E. coli homolog
    • Bernstein, H.D., Zopf, D., Freymann, D.M., Walter, P., 1993. Functional substitution of the signal recognition particle 54-kDa subunit by its E. coli homolog. Proc. Natl. Acad. Sci. USA 90, 5229-5233.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5229-5233
    • Bernstein, H.D.1    Zopf, D.2    Freymann, D.M.3    Walter, P.4
  • 5
    • 0028105217 scopus 로고
    • High-throughput rapid yeast DNA extraction. Application to yeast artificial chromosomes as polymerase chain reaction templates
    • Blanchard, M.M., Nowotny, V., 1994. High-throughput rapid yeast DNA extraction. Application to yeast artificial chromosomes as Polymerase Chain Reaction templates. GATA 11, 7-11.
    • (1994) GATA , vol.11 , pp. 7-11
    • Blanchard, M.M.1    Nowotny, V.2
  • 6
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma
    • Blobel, G., Dobberstein, B., 1975. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835-851.
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 7
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J.D., Trueheart, J., Natosulis, G., Fink, G.R., 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154, 164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natosulis, G.3    Fink, G.R.4
  • 8
    • 0020681321 scopus 로고
    • The secreted form of invertase in Saccharomyces cerevisiae is synthesized from mRNA encoding a signal sequence
    • Carlson, M., Taussig, R., Kustu, S., Botstein, D., 1983. The secreted form of invertase in Saccharomyces cerevisiae is synthesized from mRNA encoding a signal sequence. Mol. Cell. Biol. 3, 439-447.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 439-447
    • Carlson, M.1    Taussig, R.2    Kustu, S.3    Botstein, D.4
  • 9
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., Sacchi, N., 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 10
    • 0022590783 scopus 로고
    • The amino terminus of the yeast F1-ATPase ß-subunit precursor functions as a mitochondrial import signal
    • Emr, S.D., Vassarotti, A., Garrett, J., Geller, B.L., Takeda, M., Douglas, M.G., 1986. The amino terminus of the yeast F1-ATPase ß-subunit precursor functions as a mitochondrial import signal. J. Cell. Biol. 102, 523-533.
    • (1986) J. Cell. Biol. , vol.102 , pp. 523-533
    • Emr, S.D.1    Vassarotti, A.2    Garrett, J.3    Geller, B.L.4    Takeda, M.5    Douglas, M.G.6
  • 11
    • 0027437850 scopus 로고
    • Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2
    • Gyuris, J., Golemis, E., Chertkov, H., Brent, R., 1993. Cdil, a human G1 and S phase protein phosphatase that associates with Cdk2. Cell 75, 791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 12
    • 0027958547 scopus 로고
    • Evolutionary conversation of components of the protein translocation complex
    • Hartmann, E., Sommer, T., Prehn, S., Görlich, D., Jentsch, S., Rapoport, T.A., 1994. Evolutionary conversation of components of the protein translocation complex. Nature 367, 654-700.
    • (1994) Nature , vol.367 , pp. 654-700
    • Hartmann, E.1    Sommer, T.2    Prehn, S.3    Görlich, D.4    Jentsch, S.5    Rapoport, T.A.6
  • 14
    • 0023088363 scopus 로고
    • Many random sequences functionally replace the secretion signal sequence of yeast invertase
    • Kaiser, C.A., Preuss, D., Grisafi, P., Botstein, D., 1987. Many random sequences functionally replace the secretion signal sequence of yeast invertase. Science 235, 312-317.
    • (1987) Science , vol.235 , pp. 312-317
    • Kaiser, C.A.1    Preuss, D.2    Grisafi, P.3    Botstein, D.4
  • 16
    • 0024006019 scopus 로고
    • Intracellular sorting and processing of a yeast vacuolar hydrolase: Proteinase A propeptide contains vacuolar targeting information
    • Klionsky, D.J., Banta, L.M., Emr, S.D., 1988. Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information. Mol. Cell. Biol. 8, 2105-2116.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2105-2116
    • Klionsky, D.J.1    Banta, L.M.2    Emr, S.D.3
  • 17
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M., 1989. The scanning model for translation: an update. J. Cell Biol. 108, 229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 19
    • 0025051883 scopus 로고
    • Translational control of prokaryotic gene expression
    • McCarthy, J.E.G., Gualerzi, C., 1990. Translational control of prokaryotic gene expression. Trends Genet. 6, 78-85.
    • (1990) Trends Genet. , vol.6 , pp. 78-85
    • McCarthy, J.E.G.1    Gualerzi, C.2
  • 20
    • 0024321694 scopus 로고
    • Cassette mutagenic analysis of the yeast invertase signal peptide: Effects on protein translocation
    • Ngsee, J.K., Hansen, W., Walter, P., Smith, M., 1989. Cassette mutagenic analysis of the yeast invertase signal peptide: effects on protein translocation. Mol. Cell. Biol. 9, 3400-3410.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3400-3410
    • Ngsee, J.K.1    Hansen, W.2    Walter, P.3    Smith, M.4
  • 21
    • 0029863754 scopus 로고    scopus 로고
    • Differential effects of changes in the length of a signal/anchor domain on membrane insertion, subunit assembly, and intracellular transport of a type II integral membrane protein
    • Parks, G.D., 1996. Differential effects of changes in the length of a signal/anchor domain on membrane insertion, subunit assembly, and intracellular transport of a type II integral membrane protein. J. Biochem. 271, 7187-7195.
    • (1996) J. Biochem. , vol.271 , pp. 7187-7195
    • Parks, G.D.1
  • 22
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FastP and FastA
    • Pearson, W.R., Lipman, D.J., 1988. Rapid and sensitive sequence comparison with FastP and FastA. Methods Enzymol. 183, 63-98.
    • (1988) Methods Enzymol. , vol.183 , pp. 63-98
    • Pearson, W.R.1    Lipman, D.J.2
  • 23
    • 0022478894 scopus 로고
    • Mutations affecting the signal sequence alter synthesis and secretion of yeast invertase
    • Perlman, D., Raney, P., Halvorson, H.O., 1986. Mutations affecting the signal sequence alter synthesis and secretion of yeast invertase. Proc. Natl. Acad. Sci. USA 83, 5033-5037.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5033-5037
    • Perlman, D.1    Raney, P.2    Halvorson, H.O.3
  • 24
    • 0003648101 scopus 로고
    • August, Genetics Computer Group, 575 Science Drive, Madison, WI 53711. Program Manual for the EGCG Package, Peter Rice, The Sanger Centre, Hinxton Hall, Cambridge, CB10 1RQ, UK
    • Program Manual for the Wisconsin Package, version 8, (August, 1994) Genetics Computer Group, 575 Science Drive, Madison, WI 53711. Program Manual for the EGCG Package, Peter Rice, The Sanger Centre, Hinxton Hall, Cambridge, CB10 1RQ, UK.
    • (1994) Program Manual for the Wisconsin Package, Version 8
  • 25
    • 0010136245 scopus 로고    scopus 로고
    • Characterization of ß-R1, a gene that is selectively induced by interferon (IFN-ß) compared with IFN-α
    • Rani, M.R.S., Foster, G.R., Leung, S., Leaman, D., Stark, G.R., Ransohoff, R.M., 1996. Characterization of ß-R1, a gene that is selectively induced by interferon (IFN-ß) compared with IFN-α. J. Biol. Chem. 271, 22878-22884.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22878-22884
    • Rani, M.R.S.1    Foster, G.R.2    Leung, S.3    Leaman, D.4    Stark, G.R.5    Ransohoff, R.M.6
  • 26
    • 0029952518 scopus 로고    scopus 로고
    • Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes
    • Rapoport, T.A., Jungnickel, B., Kutay, U., 1996. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Ann. Rev. Biochem. 65, 271-303.
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 271-303
    • Rapoport, T.A.1    Jungnickel, B.2    Kutay, U.3
  • 27
    • 0025752784 scopus 로고
    • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. 3
    • Redding, K., Holcomb, C., Fuller, R.S., 1991. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. 3. Cell Biol. 113, 527-538.
    • (1991) Cell Biol. , vol.113 , pp. 527-538
    • Redding, K.1    Holcomb, C.2    Fuller, R.S.3
  • 28
    • 0026193157 scopus 로고
    • Different legumin protein domains act as vacuolar targeting signals
    • Saalbach, G., Jung, R., Kunze, G., Saalbach, I., Adler, K., Muntz, K., 1991. Different legumin protein domains act as vacuolar targeting signals. Plant Cell 3, 695-708.
    • (1991) Plant Cell , vol.3 , pp. 695-708
    • Saalbach, G.1    Jung, R.2    Kunze, G.3    Saalbach, I.4    Adler, K.5    Muntz, K.6
  • 31
    • 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., 1995. Capturing genes encoding membrane and secreted proteins important for mouse development. Proc. Natl. Acad. Sci. USA 92, 6592-6596.
    • (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
  • 32
    • 0025443923 scopus 로고
    • A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole
    • Tague, B.W., Dickinson, C.D., Chrispeels, M.J., 1990. A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole. Plant Cell 2, 533-546.
    • (1990) Plant Cell , vol.2 , pp. 533-546
    • Tague, B.W.1    Dickinson, C.D.2    Chrispeels, M.J.3
  • 33
    • 0027165675 scopus 로고
    • Signal sequence trap: A cloning strategy for secreted proteins and type I membrane proteins
    • Tashiro, K., Tada, H., Heilker, R., Shirozu, M., Nakano, T., Honjo, T., 1993. Signal sequence trap: a cloning strategy for secreted proteins and type I membrane proteins. Science 261, 600-603.
    • (1993) Science , vol.261 , pp. 600-603
    • Tashiro, K.1    Tada, H.2    Heilker, R.3    Shirozu, M.4    Nakano, T.5    Honjo, T.6
  • 34
    • 0021856417 scopus 로고
    • Signal sequences. the limits of variation
    • von Heijne, G., 1985. Signal sequences. The limits of variation. J. Mol. Biol. 184, 99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Von Heijne, G.1
  • 35
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter, P., Johnson, A.E., 1994. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10, 87-119.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 36
    • 0025934445 scopus 로고
    • Characterization of a human cDNA that encodes a functional receptor for platelet activating factor
    • Ye, R.D., Prossnitz, E.R., Zou, A.H., Cochrane, C.G., 1991. Characterization of a human cDNA that encodes a functional receptor for platelet activating factor. Biochem. Biophys. Res. Commun. 180, 105-111.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 105-111
    • Ye, R.D.1    Prossnitz, E.R.2    Zou, A.H.3    Cochrane, C.G.4
  • 37
    • 0028843648 scopus 로고
    • A signal sequence detection system using secreted protease activity as an indicator
    • Yokoyama-Kobayashi, M., Sugano, S., Kato, T., Kato, S., 1995. A signal sequence detection system using secreted protease activity as an indicator. Gene 163, 193-196.
    • (1995) Gene , vol.163 , pp. 193-196
    • Yokoyama-Kobayashi, M.1    Sugano, S.2    Kato, T.3    Kato, S.4
  • 38
    • 0026664440 scopus 로고
    • Control of translation initiation in Saccharomyces cerevisiae
    • Yoon, H., Donahue, T.F., 1992. Control of translation initiation in Saccharomyces cerevisiae. Mol. Microbiol. 6, 1413-1419.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1413-1419
    • Yoon, H.1    Donahue, T.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.