Ultrastructural detection of ribulose-1,5-bisphosphate carboxylase protein and its subunit mRNAs in wild-type and holoenzyme-deficient Nicotiana using immuno-gold and in-situ-hybridization techniques View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-02

AUTHORS

J. Brangeon, A. Nato, A. Forchioni

ABSTRACT

In-situ-localization techniques have been adapted to the ultrastructural detection of the holoenzyme ribulose-1,5-bisphosphate carboxylase (RuBPCase) and its composite large- and smallsubunit mRNAs in wild-type and mutant RuBPCase deficient plantlets of Nicotiana tabacum L. Immuno-gold techniques which show the distribution of target proteins have confirmed visually the presence of the holoenzyme in the wild-type plastids and its total absence in the enzyme-less mutant. Using in-situ hybridization coupled with electron microscopy and biotinylated probes for the two subunits, we have directly visualized specific small-subunit mRNAs located in the cytoplasm and large-subunit mRNAs confined to plastids in the enzyme-deficient mutant, and with apparent distributions comparable to those visualized in the wild-type counterpart. These results show that (i) gene products can be visualized in situ by electronmicroscopy techniques under conditions where the respective cellular compartments are readily recognizable and (ii) that an accumulation of mRNAs corresponding to the composite subunits can occur without translation and-or assembly of the protein. More... »

PAGES

151-159

Journal

TITLE

Planta

ISSUE

2

VOLUME

177

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00392803

DOI

http://dx.doi.org/10.1007/bf00392803

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1004784869

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24212337


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