Culture of soybean fruit explants: growth conditions and efficiency of nitrogen sources for reserve protein synthesis

1991 ◽  
Vol 27 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Paulo R. Mosquim ◽  
Ladasiav Sodek
Keyword(s):  
Protein Synthesis ◽  
Nitrogen Sources ◽  
Growth Conditions ◽  
Reserve Protein ◽  
Fruit Explants

scholarly journals Carbon and Nitrogen Sources Have No Impact on the Organization and Composition of Ustilago maydis Respiratory Supercomplexes

2021 ◽  
Vol 7 (1) ◽  
pp. 42
Author(s):  
Deyamira Matuz-Mares ◽  
Oscar Flores-Herrera ◽  
Guadalupe Guerra-Sánchez ◽  
Lucero Romero-Aguilar ◽  
Héctor Vázquez-Meza ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Atp Synthesis ◽  
Nitrogen Sources ◽  
Growth Conditions ◽  
Energy Conditions ◽  
Respiratory Complexes ◽  
Respiratory Supercomplexes ◽  
Nadh Dehydrogenases ◽  
Reduced Nicotinamide Adenine Dinucleotide

Respiratory supercomplexes are found in mitochondria of eukaryotic cells and some bacteria. A hypothetical role of these supercomplexes is electron channeling, which in principle should increase the respiratory chain efficiency and ATP synthesis. In addition to the four classic respiratory complexes and the ATP synthase, U. maydis mitochondria contain three type II NADH dehydrogenases (NADH for reduced nicotinamide adenine dinucleotide) and the alternative oxidase. Changes in the composition of the respiratory supercomplexes due to energy requirements have been reported in certain organisms. In this study, we addressed the organization of the mitochondrial respiratory complexes in U. maydis under diverse energy conditions. Supercomplexes were obtained by solubilization of U. maydis mitochondria with digitonin and separated by blue native polyacrylamide gel electrophoresis (BN-PAGE). The molecular mass of supercomplexes and their probable stoichiometries were 1200 kDa (I1:IV1), 1400 kDa (I1:III2), 1600 kDa (I1:III2:IV1), and 1800 kDa (I1:III2:IV2). Concerning the ATP synthase, approximately half of the protein is present as a dimer and half as a monomer. The distribution of respiratory supercomplexes was the same in all growth conditions. We did not find evidence for the association of complex II and the alternative NADH dehydrogenases with other respiratory complexes.

Growth Conditions of a Thermophilic Geobacillus sp. as an Enhanced Oil Recovery Material

2012 ◽  
Vol 496 ◽  
pp. 457-460
Author(s):  
Xiang Ping Kong
Keyword(s):  
Enhanced Oil Recovery ◽  
Bacterial Growth ◽  
Oil Recovery ◽  
Nitrogen Sources ◽  
Growth Conditions ◽  
Good Growth ◽  
Strictly Aerobic ◽  
Aerobic Bacterium ◽  
Carbon And Nitrogen Sources ◽  
Carbon And Nitrogen

The growth conditions of a Geobacillus sp. were investigated by single-factor experiments. The strain was strictly aerobic bacterium, and could grow on hydrocarbons as the sole carbon source. The optimum carbon and nitrogen sources were 3.0% sucrose and 0.20% KNO3, respectively. The range of temperature, salinity and pH for the bacterial growth was 35-70 °C, 0-10% NaCl and 5.5-9.5, and good growth was obtained at 35-65 °C, 0.5-8% NaCl and 6.0-9.0, respectively. Particularly, the optimum temperature for the bacterial growth was between 50 °C and 60 °C. The strain had wide adaptability to the extreme conditions, and may be potentially applied to microbial enhanced oil recovery and oil-waste bioremediation technology.

Polysomal organization in growing and resting cultures and its relation to protein synthesis in Tetrahymena

1983 ◽  
Vol 59 (1) ◽  
pp. 121-131
Author(s):  
P. Isberner ◽  
G. Cleffmann
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Growth Conditions ◽  
The Other ◽  
Protein Accumulation ◽  
Resting Cells ◽  
Amino Acid Incorporation ◽  
Total Rna ◽  
Acid Incorporation ◽  
Other Hand

Cytosol from Tetrahymena cells growing at different rates was isolated and separated by centrifugation into polysomal and non-polysomal fractions. The RNAs of either fraction were separated chromatographically into poly(A)+ RNA and poly(A)-RNA. It was found that in resting cultures the total RNA per cell is only about half of that of rapidly growing cultures. All fractions of RNA were reduced proportionally. Thus, the percentage of polysomally bound total RNA (70% of cytosol RNA) and polysomally bound poly(A)+ RNA (72% of cytosol poly(A)+ RNA) is the same in growing and resting cultures. Differences, however, were found in the polysomal structure. Polysomes from resting cultures contained significantly fewer ribosomes. The amounts of RNA bound to polysomes were related to the rate of protein synthesis under different growth conditions. The decrease in cellular RNA corresponded well with the reduction in amino acid incorporation in resting cells. The rate of protein accumulation in resting cells, on the other hand, was considerably less, suggesting that polypeptides in resting cultures are less stable.

Growth morphology of Streptomyces akiyoshiensis in submerged culture: influence of pH, inoculum, and nutrients

1992 ◽  
Vol 38 (2) ◽  
pp. 98-103 ◽  
Author(s):  
M. A. Glazebrook ◽  
L. C. Vining ◽  
R. L. White
Keyword(s):  
Nitrogen Sources ◽  
Growth Conditions ◽  
Culture Conditions ◽  
Inoculum Size ◽  
Clear Correlation ◽  
Growth Morphology ◽  
Physiological Control ◽  
Submerged Cultures ◽  
Pellet Formation ◽  
Culture Influence

Most media in which the growth of shaken submerged cultures of Streptomyces akiyoshiensis was examined did not support the formation of well-dispersed mycelial suspensions. Investigation of the culture conditions promoting dispersed growth showed the pH of the culture medium to be of critical importance; an initial value of 5.5 minimized aggregation of the mycelium while supporting adequate biomass production. In cultures started at this pH, spore inocula gave better mycelial dispersal than did vegetative inocula; with spore inocula, growth morphology was also less affected by inoculum size. The composition of the nutrient solution influenced the extent of mycelial dispersal; slow growth was often associated with clumping but no clear correlation was observed between pellet formation and the ability of carbon or nitrogen sources to support rapid growth. Increasing the phosphate concentration from 0.5 to 15 mM caused a modest decrease in mycelial aggregation. Conditions promoting a well-dispersed mycelium suitable for studying the physiological control of secondary metabolism also supported the formation of 5-hydroxy-4-oxonorvaline by S. akiyoshiensis. Key words: Streptomyces akiyoshiensis, mycelial aggregation, growth conditions.

scholarly journals Functional Analysis of the ATG8 Homologue Aoatg8 and Role of Autophagy in Differentiation and Germination in Aspergillus oryzae

2006 ◽  
Vol 5 (8) ◽  
pp. 1328-1336 ◽  
Author(s):  
Takashi Kikuma ◽  
Mamoru Ohneda ◽  
Manabu Arioka ◽  
Katsuhiko Kitamoto
Keyword(s):  
Aspergillus Oryzae ◽  
Fusion Proteins ◽  
Fluorescent Protein ◽  
Normal Growth ◽  
Nitrogen Sources ◽  
Growth Conditions ◽  
Conidial Germination ◽  
Aerial Hyphae ◽  
Green Fluorescent ◽  
Starvation Conditions

ABSTRACT Autophagy is a well-known degradation system, induced by nutrient starvation, in which cytoplasmic components and organelles are digested via vacuoles/lysosomes. Recently, it was reported that autophagy is involved in the turnover of cellular components, development, differentiation, immune responses, protection against pathogens, and cell death. In this study, we isolated the ATG8 gene homologue Aoatg8 from the filamentous fungus Aspergillus oryzae and visualized autophagy by the expression of DsRed2-AoAtg8 and enhanced green fluorescent protein-AoAtg8 fusion proteins in this fungus. While the fusion proteins were localized in dot structures which are preautophagosomal structure-like structures under normal growth conditions, starvation or rapamycin treatment caused their accumulation in vacuoles. DsRed2 expressed in the cytoplasm was also taken up into vacuoles under starvation conditions or during the differentiation of conidiophores and conidial germination. Deletion mutants of Aoatg8 did not form aerial hyphae and conidia, and DsRed2 was not localized in vacuoles under starvation conditions, indicating that Aoatg8 is essential for autophagy. Furthermore, Aoatg8 conditional mutants showed delayed conidial germination in the absence of nitrogen sources. These results suggest that autophagy functions in both the differentiation of aerial hyphae and in conidial germination in A. oryzae.

scholarly journals Borrelia burgdorferi Alters Its Gene Expression and Antigenic Profile in Response to CO2 Levels

2006 ◽  
Vol 189 (2) ◽  
pp. 437-445 ◽  
Author(s):  
Jenny A. Hyde ◽  
Jerome P. Trzeciakowski ◽  
Jonathan T. Skare
Keyword(s):  
Gene Expression ◽  
Protein Synthesis ◽  
Borrelia Burgdorferi ◽  
Growth Conditions ◽  
Etiologic Agent ◽  
Complex Life Cycle ◽  
Mammalian Host ◽  
Transcriptional Level ◽  
Virulence Determinants

ABSTRACT The etiologic agent of Lyme disease, Borrelia burgdorferi, must adapt to the distinct environments of its arthropod vector and mammalian host during its complex life cycle. B. burgdorferi alters gene expression and protein synthesis in response to temperature, pH, and other uncharacterized environmental factors. The hypothesis tested in this study is that dissolved gases, including CO2, serve as a signal for B. burgdorferi to alter protein production and gene expression. In this study we focused on characterization of in vitro anaerobic (5% CO2, 3% H2, 0.087 ppm O2) and microaerophilic (1% CO2, 3.48 ppm O2) growth conditions and how they modulate protein synthesis and gene expression in B. burgdorferi. Higher levels of several immunoreactive proteins, including BosR, NapA, DbpA, OspC, BBK32, and RpoS, were synthesized under anaerobic conditions. Previous studies demonstrated that lower levels of NapA were produced when microaerophilic cultures were purged with nitrogen gas to displace oxygen and CO2. In this study we identified CO2 as a factor contributing to the observed change in NapA synthesis. Specifically, a reduction in the level of dissolved CO2, independent of O2 levels, resulted in reduced NapA synthesis. BosR, DbpA, OspC, and RpoS synthesis was also decreased with the displacement of CO2. Quantitative reverse transcription-PCR indicated that the levels of the dbpA, ospC, and BBK32 transcripts are increased in the presence of CO2, indicating that these putative borrelial virulence determinants are regulated at the transcriptional level. Thus, dissolved CO2 may be an additional cue for borrelial host adaptation and gene regulation.

scholarly journals Glucose repression of the yeast ADH2 gene occurs through multiple mechanisms, including control of the protein synthesis of its transcriptional activator, ADR1.

1992 ◽  
Vol 12 (4) ◽  
pp. 1663-1673 ◽  
Author(s):  
R C Vallari ◽  
W J Cook ◽  
D C Audino ◽  
M J Morgan ◽  
D E Jensen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Glucose Repression ◽  
Regulatory Protein ◽  
Transcriptional Activator ◽  
Protein Translation ◽  
Growth Conditions ◽  
Mrna Levels ◽  
Coding Region ◽  
Glucose Depletion

The rate of ADH2 transcription increases dramatically when Saccharomyces cerevisiae cells are shifted from glucose to ethanol growth conditions. Since ADH2 expression under glucose growth conditions is strictly dependent on the dosage of the transcriptional activator ADR1, we investigated the possibility that regulation of the rate of ADR1 protein synthesis plays a role in controlling ADR1 activation of ADH2 transcription. We found that the rate of ADR1 protein synthesis increased 10- to 16-fold within 40 to 60 min after glucose depletion, coterminous with initiation of ADH2 transcription. Changes in ADR1 mRNA levels contributed only a twofold effect on ADR1 protein synthetic differences. The 510-nt untranslated ADR1 mRNA leader sequence was found to have no involvement in regulating the rate of ADR1 protein synthesis. In contrast, sequences internal to ADR1 coding region were determined to be necessary for controlling ADR1 translation. The ADR1c mutations which enhance ADR1 activity under glucose growth conditions did not affect ADR1 protein translation. ADR1 was also shown to be multiply phosphorylated in vivo under both ethanol and glucose growth conditions. Our results indicate that derepression of ADH2 occurs through multiple mechanisms involving the ADR1 regulatory protein.

scholarly journals Production of cellulase by Mucor ramanniacus using submerged fermentation and its applications in biodegradation of agro-industrial waste

2021 ◽  
Author(s):  
Taiwo Dorcas Ibukunoluwa ◽  
Ademakinwa Adedeji Nelson ◽  
Zainab Adenike Ayinla ◽  
Femi Kayode Agboola
Keyword(s):  
Specific Activity ◽  
Protein A ◽  
Nitrogen Sources ◽  
Tween 80 ◽  
Growth Conditions ◽  
Cellulase Production ◽  
Industrial Applications ◽  
Inoculum Size ◽  
Industrial Wastes ◽  
Triton X

Abstract This study was undertaken to isolate and identify a novel cellulase-producing strain from a waste site (7°28’11’’N 4°31’24’’E), optimise the growth conditions, partially purify and biochemically characterise the enzyme. The potentials of the purified cellulase to hydrolyse the lignocellulosic component of some agro-industrial wastes (e.g. orange peels etc.) was also investigated. The best cellulase-producing fungus was identified as Mucor ramanniacus and the optimum conditions for cellulase production were pH (4.5), inoculum size (12 mm), carbon and nitrogen sources were carboxymethyl cellulose and sodium nitrate respectively resulting in a specific activity of 1423 Units/mg protein. A purification fold of 1.56 and 45.37 % yield were obtained after purification. The optimum pH and temperature were at 9.0 and 40°C respectively. The kinetic parameters were 0.63 ± 0.495 mg/ml, 20.21 ± 11.28 U/ml, 1001.4s− 1 for Km and Vmax and kcat respectively. Na+, K+, Ca+, Cysteine, β-mercaptoethanol and SDS were activators while Tween 80, Triton X-100 EDTA, Hg2+ and Ba2+ inhibited the enzyme. M. ramanniacus cellulase hydrolysed all agro-industrial wastes used. The partially purified M. ramanniacus cellulase showed great potential in biodegradation of various lignocellulosic substrates and the biochemical characteristics exhibited makes it suitable in industrial applications.

The mitospecific domain of Mrp7 (bL27) supports mitochondrial translation during fermentation and is required for effective adaptation to respiration

2021 ◽  
Author(s):  
Jessica M. Anderson ◽  
Jodie M. Box ◽  
Rosemary A. Stuart
Keyword(s):  
Protein Synthesis ◽  
Mitochondrial Protein ◽  
Growth Conditions ◽  
Mitochondrial Protein Synthesis ◽  
Mitochondrial Translation ◽  
Glucose Fermentation ◽  
Binding Partner ◽  
Oxphos Complex ◽  
Mitochondrial Signaling ◽  
Metabolic Conditions

We demonstrate here that mitoribosomal protein synthesis, responsible for the synthesis of oxidative phosphorylation (OXPHOS) subunits encoded by mitochondrial genome, occurs at high levels during glycolysis fermentation and in a manner uncoupled from OXPHOS complex assembly regulation. Furthermore, we provide evidence that the mitospecific domain of Mrp7 (bL27), a mitoribosomal component, is required to maintain mitochondrial protein synthesis during fermentation, but is not required under respiration growth conditions. Maintaining mitotranslation under high glucose fermentation conditions also involves Mam33 (p32/gC1qR homolog), a binding partner of Mrp7’s mitospecific domain, and together they confer a competitive advantage for a cell's ability to adapt to respiration-based metabolism when glucose becomes limiting. Furthermore, our findings support that the mitoribosome, and specifically the central protuberance (CP) region, may be differentially regulated and/or assembled, under the different metabolic conditions of fermentation and respiration. Based on our findings, we propose the purpose of mitotranslation is not limited to the assembly of OXPHOS complexes, but also plays a role in mitochondrial signaling critical for switching cellular metabolism from a glycolysis- to a respiratory-based state.

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