scholarly journals Changes in chloroplastic and cytoplasmic ribosomal protein after GA3-treatment of Zea mays leaves

2015 ◽  
Vol 27 (1) ◽  
pp. 81-84 ◽  
Author(s):  
P. Masłowski ◽  
M. Komoszyński ◽  
A. Śliwak
Keyword(s):  
Zea Mays ◽  
Gibberellic Acid ◽  
Ribosomal Protein ◽  
Polyacrylamide Gel ◽  
Qualitative Composition ◽  
Maize Leaves ◽  
Additional Protein ◽  
Cytoplasmic Ribosomes

Protein was isolated from chioroplastic and cytoplasmic ribosomes of 14-day-old maize leaves subjected to the action of gibberellic acid. The proteins were separated electrophoretically on polyacrylamide gel. Fourteen fractions of ribosomal protein were obtained exhibiting wide electrophoretic differences. Qualitative differences were found between the chloroplastic and cytoplasmic ribosomes. Gibberellic acid caused the appearance of an additional protein Traction in cytoplasmic ribosomes. It did not, however, affect the qualitative composition of ribosome proteins from chloroplasts.

Growth-Related Changes in Subcellular Ion Patterns in Maize Leaves (Zea mays L.) under Salt Stress

2011 ◽  
Vol 198 (1) ◽  
pp. 46-56 ◽  
Author(s):  
M. Shahzad ◽  
K. Witzel ◽  
C. Zörb ◽  
K. H. Mühling
Keyword(s):  
Zea Mays ◽  
Salt Stress ◽  
Zea Mays L ◽  
Maize Leaves

scholarly journals Profiling of BABA-induced differentially expressed genes of Zea mays using suppression subtractive hybridization

RSC Advances ◽  
2017 ◽  
Vol 7 (69) ◽  
pp. 43849-43865 ◽  
Author(s):  
Arun K. Shaw ◽  
Pardeep K. Bhardwaj ◽  
Supriya Ghosh ◽  
Ikbal Azahar ◽  
Sinchan Adhikari ◽  
...  
Keyword(s):  
Zea Mays ◽  
Differentially Expressed Genes ◽  
Suppression Subtractive Hybridization ◽  
Defense Mechanisms ◽  
Subtractive Hybridization ◽  
Differentially Expressed ◽  
Maize Leaves

This study aims to identify differentially expressed transcripts in BABA-primed maize leaves using suppression subtractive hybridization (SSH) strategy. Findings shed new light on the BABA potentiated defense mechanisms in plants.

scholarly journals Halobacterium cutirubrum ribosomes. Properties of the ribosomal proteins and ribonucleic acid

1972 ◽  
Vol 130 (1) ◽  
pp. 103-110 ◽  
Author(s):  
L. P. Visentin ◽  
C. Chow ◽  
A. T. Matheson ◽  
M. Yaguchi ◽  
F. Rollin
Keyword(s):  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Soluble Fraction ◽  
Ribosomal Subunit ◽  
23S Rrna ◽  
Core Particle ◽  
Fractionation Procedure ◽  
Additional Protein ◽  
70S Ribosome ◽  
Low Ionic Strength

1. The 30S ribosomal subunit of the extreme halophile Halobacterium cutirubrum is unstable and loses 75% of its ribosomal protein when the 70S ribosome is dissociated into the two subunits. A stable 30S subunit is obtained if the dissociation of the 70S particle is carried out in the presence of the soluble fraction. 2. A fractionation procedure was developed for the selective removal of groups of proteins from the 30S and 50S subunits. When the ribosomes, which are stable in 4m-K+ and 0.1m-Mg2+, were extracted with low-ionic-strength buffer 75–80% of the 30S proteins and 60–65% of the 50S proteins as well as the 5S rRNA were released. The proteins in this fraction are the most acidic of the H. cutirubrum ribosomal proteins. Further extraction with Li+–EDTA releases additional protein, leaving a core particle containing either 16S rRNA or 23S rRNA and about 5% of the total ribosomal protein. The amino acid composition, mobility on polyacrylamide gels at pH4.5 and 8.7, and the molecular-weight distribution of the various protein fractions were determined. 3. The s values of the rRNA are 5S, 16S and 23S. The C+G contents of the 16S and 23S rRNA were 56.1 and 58.8% respectively and these are higher than C+G contents of the corresponding Escherichia coli rRNA (53.8 and 54.1%).

The role of gibberellic acid in the hydrolysis of endosperm reserves in Zea mays

Planta ◽  
1974 ◽  
Vol 121 (1) ◽  
pp. 67-74 ◽  
Author(s):  
B. M. R. Harvey ◽  
Ann Oaks
Keyword(s):  
Zea Mays ◽  
Gibberellic Acid ◽  
Hydrolysis Of

Regulation of Phosphoenolpyruvate Carboxylase in Zea mays by Protein Phosphorylation and Metabolites and Their Roles in Photosynthesis

1996 ◽  
Vol 23 (1) ◽  
pp. 25 ◽  
Author(s):  
Y Gao ◽  
KC Woo
Keyword(s):  
Zea Mays ◽  
Enzyme Activity ◽  
Protein Phosphorylation ◽  
Photosynthetic Rate ◽  
Phosphoenolpyruvate Carboxylase ◽  
Strong Inhibitor ◽  
Physiological Concentration ◽  
Crude Extracts ◽  
Maize Leaves

The effects of metabolites, protein phosphorylation and malate inhibition on phosphoenolpyruvate carboxylase (PEPC) activity were investigated at pH 7.0 in partially purified enzyme from maize leaves. Glycine, glucose 6-phosphate or alanine stimulated the activity two- to three-fold. Glycine and glucose 6-phosphate increased the affinity for PEP by factors of eight and four respectively. These metabolites changed the response of the enzyme activity to pH. Activity increased between pH 6.8 and 8.0 by 10-fold in the absence and 26% in the presence of these metabolites. In vitro phosphorylation of PEPC increased the activity two-fold in the absence but not in the presence of these metabolites. Malate was a strong inhibitor of PEPC, the KI value being 0.25-0.5 mM. Protein phosphorylation and the above metabolites increased the Ki value by factors of three and 12 respectively, but they synergistically increased the Ki 50-fold, thus providing maximal protection against malate inhibition. In the crude extracts from light- and dark-adapted leaves in the presence of a physiological concentration of malate (20 mM), PEPC activity comparable to the photosynthetic rate was obtained only from the light-adapted leaves in the presence of metabolites indicating that both light-induced protein phosphorylation and metabolic activators were essential for PEPC activation during photosynthesis. We propose that both these factors act synergistically to modulate PEPC during photosynthesis in maize.

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