The Expression of the Gene for the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase in Maize

1978 ◽  
pp. 349-362 ◽  
Author(s):  
Gerhard Link ◽  
John R. Bedbrook ◽  
Lawrence Bogorad ◽  
Donald M. Coen ◽  
Alexander Rich
Keyword(s):  
Large Subunit ◽  
Bisphosphate Carboxylase

scholarly journals Characterization of the gene and mRNA of the large subunit of ribulose-1,5-bisphosphate carboxylase in pea plants.

1983 ◽  
Vol 3 (4) ◽  
pp. 587-595 ◽  
Author(s):  
K K Oishi ◽  
K K Tewari
Keyword(s):  
Immunoglobulin G ◽  
Large Subunit ◽  
Rrna Genes ◽  
Mapping Technique ◽  
Affinity Column ◽  
Bisphosphate Carboxylase ◽  
Bamhi Fragment ◽  
Dna Fragment

mRNA coding for the large subunit (LS) of ribulose-1,5-bisphosphate carboxylase was obtained by fractionating chloroplast polysomes on an affinity column, using anti-ribulose-1,5-bisphosphate carboxylase immunoglobulin G. Approximately 20% of the polysomal RNA specifically bound to the affinity column. LS mRNA was also isolated by fractionating chloroplast polysomal RNA on sucrose gradients. The LS mRNA fraction was identified by translation in vitro followed by immunoprecipitation with anti-ribulose-1,5-bisphosphate carboxylase immunoglobulin G. Labeled LS mRNA was hybridized to a genomic digests of pea chloroplast DNA. The LS gene was localized on a 3.55-kilobase pair BamHI fragment in SalI-SmaI DNA fragment 4. The BamHI fragment containing the LS gene was cloned, and a restriction endonuclease map was constructed. The LS gene was localized on a 1.9-kbp KpnI-EcoRI fragment. The LS gene was analyzed by electron microscopy, using the R loop mapping technique. LS mRNA was colinear with the gene, and its size was 1.35 +/- 0.2 kilobase pairs. When the LS mRNA was analyzed on methylmercury agarose gels, it comigrated with the 16S rRNA. The direction of transcription of the LS gene was in the same direction as that of the rRNA genes.

Synthesis of the large subunit of ribulose-1,5-bisphosphate carboxylase in anin vitro partially definedE. coli system

1983 ◽  
Vol 2 (5) ◽  
pp. 279-290 ◽  
Author(s):  
Jack L. Erion ◽  
Joseph Tarnowski ◽  
Susan Peacock ◽  
Paul Caldwell ◽  
Betty Redfield ◽  
...  
Keyword(s):  
Large Subunit ◽  
Bisphosphate Carboxylase

scholarly journals Protein degradation rate as affected by plant proteases among fresh samples of perennial ryegrass cultivars (Lolium perenne L.) / Einfluss pflanzlicher Proteasen auf den Proteinabbau bei unterschiedlichen Englischen Raigrass Sorten (Lolium perenne L.)

2016 ◽  
Vol 67 (2) ◽  
pp. 61-68
Author(s):  
Martin Gierus ◽  
Marc Loesche ◽  
Heba Salama ◽  
Antje Herrmann ◽  
Friedhelm Taube
Keyword(s):  
Protein Degradation ◽  
Protein Content ◽  
Lolium Perenne ◽  
Perennial Ryegrass ◽  
Incubation Time ◽  
Large Subunit ◽  
Ethanol Solution ◽  
Bisphosphate Carboxylase ◽  
Lolium Perenne L ◽  
Degradation Rates

Summary The objective of this study was to quantify the proteolytic activity of a set of 10 diploid early intermediate heading cultivars of Lolium perenne under rumenlike conditions. A field experiment was conducted in Northern Germany, where the perennial ryegrass cultivars were grown during two growing seasons. Leaves of the first and second cut were sampled in the field, sterilized with 800 ml. l−1 ethanol solution and incubated for 0, 6, and 24 h under rumenlike conditions (darkness, 39°C, pH 6.5) without the presence of rumen microbes. Results revealed that the leaf protein content declined with increasing incubation time, confirming the involvement of plant-mediated proteolysis in the degradation process. Gel electrophoresis illustrated that the decrease in protein content is probably mainly caused by the loss of the large subunit of Rubisco (ribulose-1, 5-bisphosphate carboxylase/oxygenase), which was entirely degraded during the incubation time. Although differences among harvests and years were evident, genetic variation among the 10 diploid perennial grass samples concerning protein degradation rates and degradation characteristics was not detected.

scholarly journals Molecular insights into the functional role of nitric oxide (NO) as a signal for plant responses in chickpea

2018 ◽  
Vol 45 (2) ◽  
pp. 267 ◽  
Author(s):  
Parankusam Santisree ◽  
Pooja Bhatnagar-Mathur ◽  
Kiran K. Sharma
Keyword(s):  
Nitric Oxide ◽  
Large Scale ◽  
Molecular Mechanisms ◽  
Lipid Transfer Protein ◽  
Positive Impact ◽  
Large Subunit ◽  
Plant Responses ◽  
Acid Oxidase ◽  
No Donor ◽  
Bisphosphate Carboxylase

The molecular mechanisms and targets of nitric oxide (NO) are not fully known in plants. Our study reports the first large-scale quantitative proteomic analysis of NO donor responsive proteins in chickpea. Dose response studies carried out using NO donors, sodium nitroprusside (SNP), diethylamine NONOate (DETA) and S-nitrosoglutathione (GSNO) in chickpea genotype ICCV1882, revealed a dose dependent positive impact on seed germination and seedling growth. SNP at 0.1 mM concentration proved to be most appropriate following confirmation using four different chickpea genotypes. while SNP treatment enhanced the percentage of germination, chlorophyll and nitrogen contents in chickpea, addition of NO scavenger, cPTIO reverted its impact under abiotic stresses. Proteome profiling revealed 172 downregulated and 76 upregulated proteins, of which majority were involved in metabolic processes (118) by virtue of their catalytic (145) and binding (106) activity. A few crucial proteins such as S-adenosylmethionine synthase, dehydroascorbate reductase, pyruvate kinase fragment, 1-aminocyclopropane-1-carboxylic acid oxidase, 1-pyrroline-5-carboxylate synthetase were less abundant whereas Bowman-Birk type protease inhibitor, non-specific lipid transfer protein, chalcone synthase, ribulose-1-5-bisphosphate carboxylase oxygenase large subunit, PSII D2 protein were highly abundant in SNP treated samples. This study highlights the protein networks for a better understanding of possible NO induced regulatory mechanisms in plants.

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