Plastid gene expression in a yellow-green leaf mutant of Petunia hybrida View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1983-04

AUTHORS

C. M. Colijn, J. N. M. Mol, A. J. Kool, H. J. J. Nijkamp

ABSTRACT

We have analyzed the morphology and gene expression in plastids of a yellow-green leaf mutant of Petunia hybrida (E 5059). Under normal light intensities (20,000 lx), yellow-green leaves develop with a typical proplastid morphology (few membranes, incomplete stacking). When such plants are grown under low light intensities (3,000 lx), the newly formed leaves are green. The plastids in these green leaves have a wild-type like chloroplast morphology (thylakoids and grana structure). Pre-existing green leaves remain green in 20,000 lx, indicating that chlorophyll is not degraded. An analysis of polypeptides synthesized in isolated plastids from the yellow-green and green leaves of this mutant plant shows several differences. In the yellow-green leaf plastids only a very small amount of the large subunit of ribulose-1,5-bisphosphate carboxylase (RuBPCase) is present, while in green plastids this polypeptide is present in much higher amounts. Hybridization experiments indicated that in plastids from the yellow-green leaves the mRNA coding for the large subunit polypeptide is present in much lower amounts than in plastids from the 3,000 lx green leaves of this mutant or in chloroplasts from wild type plants. These results indicate regulation at the mRNA level. Furthermore, in yellow-green leaf plastids eleven polypeptides are present with high molecular wieght (higher than 67,000 d). Five of them are synthesized by the yellow-green leaf plastid itself. Such high molecular weight polypeptides are also synthesized by proplastids isolated from white petunia cell suspension cultures, but are not synthesized by 3,000 lx green leaf plastids, or by isolated normal leaf chloroplasts. These results indicate that the synthesis of these polypeptides is specific for the proplastid stage of chloroplast biogenesis. More... »

PAGES

209-217

References to SciGraph publications

Journal

TITLE

Planta

ISSUE

3

VOLUME

157

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00405184

DOI

http://dx.doi.org/10.1007/bf00405184

DIMENSIONS

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PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24264149


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37 schema:description We have analyzed the morphology and gene expression in plastids of a yellow-green leaf mutant of Petunia hybrida (E 5059). Under normal light intensities (20,000 lx), yellow-green leaves develop with a typical proplastid morphology (few membranes, incomplete stacking). When such plants are grown under low light intensities (3,000 lx), the newly formed leaves are green. The plastids in these green leaves have a wild-type like chloroplast morphology (thylakoids and grana structure). Pre-existing green leaves remain green in 20,000 lx, indicating that chlorophyll is not degraded. An analysis of polypeptides synthesized in isolated plastids from the yellow-green and green leaves of this mutant plant shows several differences. In the yellow-green leaf plastids only a very small amount of the large subunit of ribulose-1,5-bisphosphate carboxylase (RuBPCase) is present, while in green plastids this polypeptide is present in much higher amounts. Hybridization experiments indicated that in plastids from the yellow-green leaves the mRNA coding for the large subunit polypeptide is present in much lower amounts than in plastids from the 3,000 lx green leaves of this mutant or in chloroplasts from wild type plants. These results indicate regulation at the mRNA level. Furthermore, in yellow-green leaf plastids eleven polypeptides are present with high molecular wieght (higher than 67,000 d). Five of them are synthesized by the yellow-green leaf plastid itself. Such high molecular weight polypeptides are also synthesized by proplastids isolated from white petunia cell suspension cultures, but are not synthesized by 3,000 lx green leaf plastids, or by isolated normal leaf chloroplasts. These results indicate that the synthesis of these polypeptides is specific for the proplastid stage of chloroplast biogenesis.
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