A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-11

AUTHORS

Leslie M. Hoffman, Debra D. Donaldson, Eliot M. Herman

ABSTRACT

In vitro mutagenesis was used to supplement the sulfur amino acid codon content of a gene encoding β-phaseolin, a Phaseolus vulgaris storage protein. The number of methionine codons in the phaseolin gene was increased from three to nine by insertion of a 45 base pair (bp) synthetic duplex. Either modified or normal phaseolin genes were integrated into the genome of tobacco plants through Agrobacterium tumefaciens-mediated transformation. Although similar levels of phaseolin RNA are detected in seeds of plants transformed with either the normal or modified (himet) gene, the quantity of himet protein is consistently much lower than normal β-phaseolin. Himet phaseolin is expressed in a temporal- and organ-specific fashion, and is N-glycosylated and assembled into trimers in the manner of normal phaseolin. After germination, both types of phaseolin are hydrolyzed, but the himet protein is more quickly degraded. Electron microscopic immunocytochemical observations of developing seeds indicate that the himet protein is primarily localized in the endoplasmic reticulum (ER) and in Golgi apparatus secretion vesicles. Himet phaseolin is absent from protein storage vacuoles, termed protein bodies, where normal phaseolin is deposited in transgenic tobacco. We interpret the immunocytochemical data to indicate that himet phasolin is transported through the ER and Golgi apparatus and is then degraded in Golgi secretion vesicles or the protein bodies. More... »

PAGES

717-729

References to SciGraph publications

Journal

TITLE

Plant Molecular Biology

ISSUE

6

VOLUME

11

Author Affiliations

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf00019513

    DOI

    http://dx.doi.org/10.1007/bf00019513

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1033347973

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/24272623


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    41 schema:description In vitro mutagenesis was used to supplement the sulfur amino acid codon content of a gene encoding β-phaseolin, a Phaseolus vulgaris storage protein. The number of methionine codons in the phaseolin gene was increased from three to nine by insertion of a 45 base pair (bp) synthetic duplex. Either modified or normal phaseolin genes were integrated into the genome of tobacco plants through Agrobacterium tumefaciens-mediated transformation. Although similar levels of phaseolin RNA are detected in seeds of plants transformed with either the normal or modified (himet) gene, the quantity of himet protein is consistently much lower than normal β-phaseolin. Himet phaseolin is expressed in a temporal- and organ-specific fashion, and is N-glycosylated and assembled into trimers in the manner of normal phaseolin. After germination, both types of phaseolin are hydrolyzed, but the himet protein is more quickly degraded. Electron microscopic immunocytochemical observations of developing seeds indicate that the himet protein is primarily localized in the endoplasmic reticulum (ER) and in Golgi apparatus secretion vesicles. Himet phaseolin is absent from protein storage vacuoles, termed protein bodies, where normal phaseolin is deposited in transgenic tobacco. We interpret the immunocytochemical data to indicate that himet phasolin is transported through the ER and Golgi apparatus and is then degraded in Golgi secretion vesicles or the protein bodies.
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