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Volumn 114, Issue 1, 1997, Pages 345-352

A defective signal peptide tethers the floury-2 zein to the endoplasmic reticulum membrane

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EID: 0031131581     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.114.1.345     Document Type: Article
Times cited : (65)

References (34)
  • 2
    • 0015356037 scopus 로고
    • Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose
    • Aviv H, Leder P (1972) Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci USA 69: 1408-1412
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 1408-1412
    • Aviv, H.1    Leder, P.2
  • 3
    • 0001847422 scopus 로고
    • Buffer systems and transfer parameters for semidry electroblotting with a horizontal apparatus
    • MJ Dunn, ed, VCH Publishers, Deerfield Beach, FL
    • Bjerrum OJ, Schafer-Nielsen C (1986) Buffer systems and transfer parameters for semidry electroblotting with a horizontal apparatus. In MJ Dunn, ed, Electrophoresis '86. VCH Publishers, Deerfield Beach, FL, pp 315-327
    • (1986) Electrophoresis '86 , pp. 315-327
    • Bjerrum, O.J.1    Schafer-Nielsen, C.2
  • 4
    • 0019603017 scopus 로고
    • In vitro uptake and processing of prezein and other maize preproteins by maize membranes
    • Burr FA, Burr B (1981) In vitro uptake and processing of prezein and other maize preproteins by maize membranes. J Cell Biol 90: 427-434
    • (1981) J Cell Biol , vol.90 , pp. 427-434
    • Burr, F.A.1    Burr, B.2
  • 5
    • 0019987193 scopus 로고
    • Three mutations in Zea mays affecting zein accumulation: A comparison of zein polypeptides, in vitro synthesis and processing, mRNA levels, and genome organization
    • Burr FA, Burr B (1982) Three mutations in Zea mays affecting zein accumulation: a comparison of zein polypeptides, in vitro synthesis and processing, mRNA levels, and genome organization. J Cell Biol 94: 201-206
    • (1982) J Cell Biol , vol.94 , pp. 201-206
    • Burr, F.A.1    Burr, B.2
  • 7
    • 0001034120 scopus 로고
    • Separation of alcohol-soluble proteins (zeins) from maize into three fractions by differential solubility
    • Esen A (1986) Separation of alcohol-soluble proteins (zeins) from maize into three fractions by differential solubility. Plant Physiol 80: 623-627
    • (1986) Plant Physiol , vol.80 , pp. 623-627
    • Esen, A.1
  • 9
    • 0029438086 scopus 로고
    • Synthesis of plant proteins in heterologous systems: Xenopus laevis oocytes
    • Galili G, Altschuler Y, Ceriotti A (1995) Synthesis of plant proteins in heterologous systems: Xenopus laevis oocytes. Methods Cell Biol 50B: 497-517
    • (1995) Methods Cell Biol , vol.50 B , pp. 497-517
    • Galili, G.1    Altschuler, Y.2    Ceriotti, A.3
  • 10
    • 0027507052 scopus 로고
    • Studies of the zein-like a-prolamins based on an analysis of amino acid sequences: Implications for their evolution and three-dimensional structure
    • Garratt R, Oliva G, Caracelli I, Leite A, Arruda P (1993) Studies of the zein-like a-prolamins based on an analysis of amino acid sequences: implications for their evolution and three-dimensional structure. Proteins 15: 88-99
    • (1993) Proteins , vol.15 , pp. 88-99
    • Garratt, R.1    Oliva, G.2    Caracelli, I.3    Leite, A.4    Arruda, P.5
  • 11
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355: 33-15
    • (1992) Nature , vol.355 , pp. 33-115
    • Gething, M.J.1    Sambrook, J.2
  • 12
    • 0023676995 scopus 로고
    • Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining
    • Hochstrasser DF, Patchornik A, Merril CR (1988) Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining. Anal Biochem 173: 412-423
    • (1988) Anal Biochem , vol.173 , pp. 412-423
    • Hochstrasser, D.F.1    Patchornik, A.2    Merril, C.R.3
  • 13
    • 0004009325 scopus 로고
    • Translation in Xenopus oocytes of mRNAs transcribed in vitro
    • SB Gelvin, RA Schilperoort, eds, Kluwer Academic, Dordrecht, The Netherlands
    • Kawata EE, Galili G, Smith LD, Larkins BA (1988) Translation in Xenopus oocytes of mRNAs transcribed in vitro. In SB Gelvin, RA Schilperoort, eds, Plant Molecular Biology Manual, Vol B7. Kluwer Academic, Dordrecht, The Netherlands, pp 1-22
    • (1988) Plant Molecular Biology Manual , vol.B7 , pp. 1-22
    • Kawata, E.E.1    Galili, G.2    Smith, L.D.3    Larkins, B.A.4
  • 14
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA (1995) Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J 14: 217-223
    • (1995) EMBO J , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteríophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of the bacteríophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0000430975 scopus 로고
    • Synthesis and deposition of zein protein bodies in maize endosperm
    • Larkins BA, Hurkman WJ (1978) Synthesis and deposition of zein protein bodies in maize endosperm. Plant Physiol 62: 256-263
    • (1978) Plant Physiol , vol.62 , pp. 256-263
    • Larkins, B.A.1    Hurkman, W.J.2
  • 18
    • 0002057478 scopus 로고
    • Structure of maize protein bodies and immunocytochemical localization of zeins
    • Lending CR, Kriz AL, Larkins BA, Bracker CE (1988) Structure of maize protein bodies and immunocytochemical localization of zeins. Protoplasma 143: 51-62
    • (1988) Protoplasma , vol.143 , pp. 51-62
    • Lending, C.R.1    Kriz, A.L.2    Larkins, B.A.3    Bracker, C.E.4
  • 19
    • 0024740149 scopus 로고
    • Changes in the zein composition of protein bodies during maize endosperm development
    • Lending CR, Larkins BA (1989) Changes in the zein composition of protein bodies during maize endosperm development. Plant Cell 1: 1011-1023
    • (1989) Plant Cell , vol.1 , pp. 1011-1023
    • Lending, C.R.1    Larkins, B.A.2
  • 20
    • 0000080041 scopus 로고
    • Effect of the floury-2 locus on protein body formation during maize endosperm development
    • Lending CR, Larkins BA (1992) Effect of the floury-2 locus on protein body formation during maize endosperm development. Protoplasma 171: 123-133
    • (1992) Protoplasma , vol.171 , pp. 123-133
    • Lending, C.R.1    Larkins, B.A.2
  • 21
    • 0030099075 scopus 로고    scopus 로고
    • Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant
    • Li CP, Larkins BA (1996) Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant. Plant Mol Biol 30: 873-882
    • (1996) Plant Mol Biol , vol.30 , pp. 873-882
    • Li, C.P.1    Larkins, B.A.2
  • 22
    • 0028173387 scopus 로고
    • Synthesis of an unusual α-zein protein is correlated with the phenotypic effects of the floury 2 mutation in maize
    • Lopes MA, Coleman CE, Kodrzycki R, Lending CR, Larkins BA (1994) Synthesis of an unusual α-zein protein is correlated with the phenotypic effects of the floury 2 mutation in maize. Mol Gen Genet 245: 537-547
    • (1994) Mol Gen Genet , vol.245 , pp. 537-547
    • Lopes, M.A.1    Coleman, C.E.2    Kodrzycki, R.3    Lending, C.R.4    Larkins, B.A.5
  • 23
    • 0020479477 scopus 로고
    • Analysis of sequence microheterogeneity among zein messenger RNAs
    • Marks MD, Larkins BA (1982) Analysis of sequence microheterogeneity among zein messenger RNAs. J Biol Chem 257: 9976-9983
    • (1982) J Biol Chem , vol.257 , pp. 9976-9983
    • Marks, M.D.1    Larkins, B.A.2
  • 24
    • 0026151429 scopus 로고
    • Three high-lysine mutations control the level of ATP-binding hsp70-like proteins in the maize endosperm
    • Marocco A, Santucci A, Cerioli S, Motto M, DiFonzo N, Thompson R, Salamini F (1991 ) Three high-lysine mutations control the level of ATP-binding hsp70-like proteins in the maize endosperm. Plant Cell 3: 507-515
    • (1991) Plant Cell , vol.3 , pp. 507-515
    • Marocco, A.1    Santucci, A.2    Cerioli, S.3    Motto, M.4    DiFonzo, N.5    Thompson, R.6    Salamini, F.7
  • 25
    • 0001645004 scopus 로고
    • Second mutant gene affecting the amino acid pattern of maize endosperm proteins
    • Nelson OE, Mertz ET, Bates L (1965) Second mutant gene affecting the amino acid pattern of maize endosperm proteins. Science 150: 1469-1470
    • (1965) Science , vol.150 , pp. 1469-1470
    • Nelson, O.E.1    Mertz, E.T.2    Bates, L.3
  • 26
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 27
    • 0014024517 scopus 로고
    • Reagents which reduce interactions between ribosomal RNA and rapidly labelled RNA from rat liver
    • Parish JH, Kirby KS (1966) Reagents which reduce interactions between ribosomal RNA and rapidly labelled RNA from rat liver. Biochim Biophys Acta 129: 554-562
    • (1966) Biochim Biophys Acta , vol.129 , pp. 554-562
    • Parish, J.H.1    Kirby, K.S.2
  • 28
    • 0017191401 scopus 로고
    • An efficient m RNA-de pendent translation system from reticulocyte lysates
    • Pelham HRB, Jackson RJ (1976) An efficient m RNA-de pendent translation system from reticulocyte lysates. Eur J Biochem 67: 247-256
    • (1976) Eur J Biochem , vol.67 , pp. 247-256
    • Pelham, H.R.B.1    Jackson, R.J.2
  • 30
    • 0021909517 scopus 로고
    • Invertase signal and mature sequence substitutions that delay intercompartmental transport of active enzyme
    • Schauer I, Emr S, Gross C, Schekman R (1985) Invertase signal and mature sequence substitutions that delay intercompartmental transport of active enzyme. J Cell Biol 100: 1664-1675
    • (1985) J Cell Biol , vol.100 , pp. 1664-1675
    • Schauer, I.1    Emr, S.2    Gross, C.3    Schekman, R.4
  • 31
    • 0025776271 scopus 로고
    • A zein signal sequence functions as a signal-anchor when fused to maize alcohol dehydrogenase
    • Shatters R, Miernyk J (1991) A zein signal sequence functions as a signal-anchor when fused to maize alcohol dehydrogenase. Biochim Biophys Acta 1068: 179-188
    • (1991) Biochim Biophys Acta , vol.1068 , pp. 179-188
    • Shatters, R.1    Miernyk, J.2
  • 32
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne G (1983) Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133: 17-21
    • (1983) Eur J Biochem , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 33
    • 0021770334 scopus 로고
    • How signal sequences maintain cleavage specificity
    • von Heijne G (1984) How signal sequences maintain cleavage specificity. J Mol Biol 173: 243-251
    • (1984) J Mol Biol , vol.173 , pp. 243-251
    • Von Heijne, G.1
  • 34
    • 0000031926 scopus 로고
    • Increases in binding protein (BiP) accompany changes in protein body morphology in three high-lysine mutants of maize
    • Zhang F, Boston RS (1992) Increases in binding protein (BiP) accompany changes in protein body morphology in three high-lysine mutants of maize. Protoplasma 171: 142-152
    • (1992) Protoplasma , vol.171 , pp. 142-152
    • Zhang, F.1    Boston, R.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.