Literature DB >> 16664403

Correct targeting of the bean storage protein phaseolin in the seeds of transformed tobacco.

J S Greenwood1, M J Chrispeels.   

Abstract

The storage protein phaseolin accumulates during seed development in protein bodies in cotyledons of the common bean Phaseolus vulgaris. Hall et al. (In L Van Vloten-Doting, TC Hall, eds, Molecular Form and Function of the Plant Genome, 1985 Plenum Press, In press) recently reported the expression of a gene coding for phaseolin and the accumulation of phaseolin protein in developing seeds of tobacco plants regenerated from transformed callus cells. The protein did not accumulate in other organs of the plants. Mature seeds from normal and transformed tobacco plants were obtained and the subcellular distribution of phaseolin in the seeds was examined using both light and electron microscopic immunocytochemical methods. Phaseolin was found in six of seven transformed tobacco embryos examined, but was present in only one endosperm of five. When present, phaseolin was located exclusively in the protein bodies of the embryonic and endospermic cells. Furthermore, phaseolin was restricted solely to the amorphous matrix of the protein bodies and was excluded from the globoid and proteinaceous crystalloid components of these organelles. The subcellular location of phaseolin in seeds from transformed tobacco plants is similar to that seen in mature seeds of the common bean indicating that in the transformed cells the protein is targeted to the right subcellular compartment.

Entities:  

Year:  1985        PMID: 16664403      PMCID: PMC1074829          DOI: 10.1104/pp.79.1.65

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  16 in total

1.  Immunofluorescent localization of pea storage proteins in glycol methacrylate embedded tissue.

Authors:  S Craig; D J Goodchild; A Millerd
Journal:  J Histochem Cytochem       Date:  1979-10       Impact factor: 2.479

2.  Conjugates of immunoglobulin G with different fluorochromes. I. Characterization by anionic-exchange chromatography.

Authors:  P Brandtzaeg
Journal:  Scand J Immunol       Date:  1973       Impact factor: 3.487

3.  Ultrastructural localization of antigenic sites on osmium-fixed tissues applying the protein A-gold technique.

Authors:  M Bendayan; M Zollinger
Journal:  J Histochem Cytochem       Date:  1983-01       Impact factor: 2.479

4.  An improved procedure for immunoelectron microscopy: ultrathin plastic embedding of immunolabeled ultrathin frozen sections.

Authors:  G A Keller; K T Tokuyasu; A H Dutton; S J Singer
Journal:  Proc Natl Acad Sci U S A       Date:  1984-09       Impact factor: 11.205

5.  LR white resin and improved on-grid immunogold detection of vicilin, a pea seed storage protein.

Authors:  S Craig; C Miller
Journal:  Cell Biol Int Rep       Date:  1984-10

6.  Dictyosomes participate in the intracellular pathway of storage proteins in developing Vicia faba cotyledons.

Authors:  U zur Nieden; R Manteuffel; E Weber; D Neumann
Journal:  Eur J Cell Biol       Date:  1984-05       Impact factor: 4.492

7.  Post-embedding immunolabelling. Some effects of tissue preparation on the antigenicity of plant proteins.

Authors:  S Craig; D J Goodchild
Journal:  Eur J Cell Biol       Date:  1982-10       Impact factor: 4.492

8.  Localization of lectins in legume cotyledons.

Authors:  A E Clarke; R B Knox; M A Jermyn
Journal:  J Cell Sci       Date:  1975-10       Impact factor: 5.285

9.  In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum: evidence for two glycosylation steps.

Authors:  R Bollini; A Vitale; M J Chrispeels
Journal:  J Cell Biol       Date:  1983-04       Impact factor: 10.539

10.  Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy.

Authors:  B Baumgartner; K T Tokuyasu; M J Chrispeels
Journal:  J Cell Biol       Date:  1978-10       Impact factor: 10.539

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  37 in total

1.  Developmentally regulated expression of a sunflower 11S seed protein gene in transgenic tobacco.

Authors:  M A Bogue; R A Vonder Haar; M L Nuccio; L R Griffing; T L Thomas
Journal:  Mol Gen Genet       Date:  1990-06

2.  Tonoplast and Soluble Vacuolar Proteins Are Targeted by Different Mechanisms.

Authors:  L. Gomez; M. J. Chrispeels
Journal:  Plant Cell       Date:  1993-09       Impact factor: 11.277

3.  Upstream sequences regulating legumin gene expression in heterologous transgenic plants.

Authors:  H Bäumlein; W Boerjan; I Nagy; R Panitz; D Inzé; U Wobus
Journal:  Mol Gen Genet       Date:  1991-01

4.  Sorting of proteins in the secretory system of plant cells.

Authors:  M J Chrispeels; A von Schaewen
Journal:  Antonie Van Leeuwenhoek       Date:  1992-02       Impact factor: 2.271

5.  Cellular localization of soybean storage protein mRNA in transformed tobacco seeds.

Authors:  S J Barker; J J Harada; R B Goldberg
Journal:  Proc Natl Acad Sci U S A       Date:  1988-01       Impact factor: 11.205

6.  The synthesis of a 19 kilodalton zein protein in transgenic petunia plants.

Authors:  J D Williamson; G Galili; B A Larkins; S B Gelvin
Journal:  Plant Physiol       Date:  1988-12       Impact factor: 8.340

7.  Protein trafficking in plant cells.

Authors:  G Della-Cioppa; G M Kishore; R N Beachy; R T Fraley
Journal:  Plant Physiol       Date:  1987-08       Impact factor: 8.340

8.  Immunocytochemical localization of patatin, the major glycoprotein in potato (Solanum tuberosum L.) tubers.

Authors:  U Sonnewald; D Studer; M Rocha-Sosa; L Willmitzer
Journal:  Planta       Date:  1989-05       Impact factor: 4.116

9.  Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole.

Authors:  J J Pueyo; M J Chrispeels; E M Herman
Journal:  Planta       Date:  1995       Impact factor: 4.116

10.  Different legumin protein domains act as vacuolar targeting signals.

Authors:  G Saalbach; R Jung; G Kunze; I Saalbach; K Adler; K Müntz
Journal:  Plant Cell       Date:  1991-07       Impact factor: 11.277

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