The effect of cycloheximide and cycloheximide analogues on protein, asparagine, and glutamine synthesis in corn root tips

1978 ◽  
Vol 56 (22) ◽  
pp. 2873-2877 ◽  
Author(s):  
W. George Wheatley ◽  
Ann Oaks
Keyword(s):  
Protein Synthesis ◽  
Basic Amino Acid ◽  
Hydroxyl Group ◽  
Root Tips ◽  
Inhibit Protein Synthesis ◽  
Corn Root ◽  
Structural Analogues ◽  
Ketone Carbonyl ◽  
Glutamine Synthesis ◽  
Organic Acids And Sugars

Cycloheximide treatment (3.6 × 10−6 M) inhibits the incorporation of [2-14C]acetate into protein, asparagine, and the organic acids and sugars fraction. At the same time, it enhances the release of 14CO2 and the incorporation of carbon into glutamine and the neutral and basic amino acid fraction. Eight structural analogues of cycloheximide were tested for their effects on protein, asparagine, and glutamine formation in corn root tips. Two analogues, cycloheximide acetate and streptovitacin A (at a concentration of 1.8 × 10−5 M), acted in a manner similar to cycloheximide. Their effect was to inhibit protein and asparagine synthesis and to enhance glutamine formation. Six other analogues (1.8 × 10−5 M) had no marked effect on these fractions. The results of this investigation indicate that the structural analogues which inhibit asparagine formation in corn root tips also inhibit protein synthesis. The results suggest that the hydroxyl group of the hydroxyethylglutarimide portion of the cycloheximide molecule and the ketone-carbonyl group of the cyclohexanone ring are important for their action on protein synthesis in corn root tips.

The effect of cycloheximide on amide formation in maize roots

1973 ◽  
Vol 51 (1) ◽  
pp. 91-95 ◽  
Author(s):  
Ann Oaks ◽  
F. J. Johnson
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Root Tip ◽  
Minor Effect ◽  
Root Tips ◽  
Corn Root ◽  
Basic Amino Acids ◽  
Maize Roots ◽  
A Minor ◽  
Mature Root

Cycloheximide inhibits the incorporation of acetate-2-14C into protein and into asparagine in corn root tips. It also causes an accumulation of glutamine and, over a concentration range of 0.4 to 5.0 μg/ml, a transient accumulation of the neutral and basic amino acids. In mature sections, cycloheximide inhibits protein synthesis but causes an increase in the incorporation of radioactivity into both glutamine and asparagine. Azaserine, a glutamine analogue, also inhibits the formation of asparagine in root-tip sections but has only a minor effect on protein synthesis. In mature root sections, there is an accumulation of glutamine but no effect on asparagine formation when azaserine is used. Glutamine additions to root tips or mature root sections affect neither asparagine formation nor protein synthesis. We conclude that cycloheximide is behaving as a glutamine analogue in its effect on asparagine biosynthesis, and that its effect as a glutamine analogue is lost as cells mature.

Protein synthesis in trifluralin-treated corn root tips

1989 ◽  
Vol 8 (3) ◽  
pp. 205-214 ◽  
Author(s):  
N. D. Camper ◽  
K. L. Ellers
Keyword(s):  
Protein Synthesis ◽  
Root Tips ◽  
Corn Root

INHIBITION OF THYROGLOBULIN BIOSYNTHESIS AND DEGRADATION BY EXCESS IODIDE. SYNERGISM WITH LITHIUM

1976 ◽  
Vol 81 (2) ◽  
pp. 495-506 ◽  
Author(s):  
A. Radvila ◽  
R. Roost ◽  
H. Bürgi ◽  
H. Kohler ◽  
H. Studer
Keyword(s):  
Protein Synthesis ◽  
Thyroid Gland ◽  
Inhibitory Action ◽  
Inhibit Protein Synthesis ◽  
Thyrotrophic Hormone ◽  
Thyroid Glands ◽  
Pre Treatment ◽  
Excess Iodide ◽  
Kidney Liver

ABSTRACT Lithium and excess iodide inhibit the release of thyroid hormone from preformed stores. We thus tested the hypothesis that this was due to an inhibition of thyroglobulin breakdown. Rats were pre-treated with propylthiouracil (PTU) for 3 weeks in order to deplete their thyroids of thyroglobulin. While the PTU was continued, lithium chloride (0.25 mEq./100 g weight) or potassium iodide (3 mg per rat) were injected every 12 h for 3 days. Thereafter the thyroglobulin content in thyroid gland homogenates was measured. PTU pre-treatment lowered the thyroglobulin content from 4.21 to 0.22 mg/100 mg gland. Lithium caused a marked re-accumulation of thyroglobulin to 0.60 mg/100 mg within 3 days. While iodide alone had only a borderline effect, it markedly potentiated the action of lithium and a combination of the two drugs increased the thyroglobulin content to 1.04 mg/100 mg. Thyroxine was injected into similarly pre-treated animals to suppress secretion of thyrotrophic hormone. This markedly inhibited the proteolysis of thyroglobulin and 1.3 mg/100 mg gland accumulated after 3 days. Excess iodide, given in addition to thyroxine, decreased the amount of thyroglobulin accumulated to 0.75 mg/100 mg gland. To study whether this could be explained by an inhibitory action of iodide on thyroglobulin biosynthesis, thyroid glands from animals treated with excess iodide were incubated in vitro in the presence of 0.2 mm iodide for 3 h. Iodide decreased the incorporation of radioactive leucine into total thyroidal protein and into thyroglobulin by 25 and 35 % respectively. Iodide did not inhibit protein synthesis in the kidney, liver or muscle tissue. Thus, large doses of iodide selectively inhibit thyroglobulin biosynthesis.

The effects of D- and L-threo-chloramphenicol on the early development of the chick embryo

Development ◽  
1965 ◽  
Vol 13 (3) ◽  
pp. 341-356
Author(s):  
F. S. Billett ◽  
Rosalba Collini ◽  
Louie Hamilton
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Chick Embryo ◽  
Messenger Rna ◽  
Mammalian Cells ◽  
Animal Cells ◽  
Inhibit Protein Synthesis ◽  
Acid Complex ◽  
Amino Acid Complex ◽  
Bacterial Systems

In many bacterial systems chloramphenicol has been shown to inhibit protein synthesis (Hahn & Wisseman, 1951; Gale & Folkes, 1953). The precise mechanism of this inhibition is not clear, although the evidence suggests that the interaction of the soluble RNA-amino acid complex with the ribosomes is prevented because the attachment of the messenger RNA to the ribosomes is itself impaired (Lacks & Gros, 1959; Nathans & Lipman, 1961; Jardetsky & Julian, 1964; Julian & Jardetsky, 1964). In contrast to its effect on bacterial systems, chloramphenicol has been reported to have little or no action on the protein synthesis by cell-free extracts of mammalian cells (Rendi, 1959; Ehrenstein & Lipmann, 1961). A basis for this resistance has been proposed by Vazquez (1964), who finds that whereas bacterial ribosomes bind chloramphenicol, ribosomes from other organisms do not. Nevertheless, it cannot be stated with any confidence that chloramphenicol has no effect on the protein synthesis of animal cells.

Proteomic Analyses of Soybean Root Tips During Germination

2014 ◽  
Vol 21 (12) ◽  
pp. 1308-1319
Author(s):  
Setsuko Komatsu ◽  
Myeong W. Oh ◽  
Hee Y. Jang ◽  
Soo J. Kwon ◽  
Hye R. Kim ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Proteomic Analysis ◽  
Plant Root ◽  
Root Tip ◽  
Root Tips ◽  
Form Complex ◽  
Molecular Weights ◽  
Soybean Seedlings ◽  
2D Gel ◽  
Proteomic Techniques

Plant root systems form complex networks with the surrounding soil environment and are controlled by both internal and external factors. To better understand the function of root tips of soybean during germination, three proteomic techniques were used to analyze the protein profiles of root tip cells. Proteins were extracted from the root tips of 4-dayold soybean seedlings and analyzed using two-dimensional (2D) gel electrophoresis-based proteomics, SDS-gel based proteomics, and gel-free proteomics techniques. A total of 121, 862, and 341 proteins were identified in root tips using the 2D gel-based, SDS gel-based, and gel-free proteomic techniques, respectively. The proteins identified by 2D gel-based proteomic analysis were predominantly localized in the cytoplasm, whereas nuclear-localized proteins were most commonly identified by the SDS gel-based and gel-free proteomics techniques. Of the 862 proteins identified in the SDS gelbased proteomic analysis, 190 were protein synthesis-related proteins. Furthermore, 24 proteins identified using the 2Dgel based proteomic technique shifted between acidic and basic isoelectric points, and 2 proteins, heat shock protein 70.2 and AAA-type ATPase, displayed two different molecular weights at the same isoelectric point. Taken together, these results suggest that a number of proteins related to protein synthesis and modification are activated in the root tips of soybean seedlings during germination.

The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER

1979 ◽  
Vol 35 (1) ◽  
pp. 253-266
Author(s):  
S.P. Gibbs
Keyword(s):  
Protein Synthesis ◽  
Nuclear Envelope ◽  
Outer Membrane ◽  
Chloroplast Envelope ◽  
Inhibit Protein Synthesis ◽  
Ochromonas Danica ◽  
Plastid Proteins ◽  
Regular Network ◽  
Cytoplasmic Ribosomes ◽  
Plastid Ribosomes

In 8 classes of algae, namely the Cryptophyceae, Raphidophyceae, Haptophyceae, Chrysophyceae, Bacillariophyceae, Xanthophyceae, Eustigmatophyceae and Phaeophyceae, the chloroplasts, in addition to being surrounded by a double-membraned chloroplast envelope, are also enclosed by a cisterna of endoplasmic reticulum called the chloroplast ER. Often this ER cisterna is continuous with the outher membrane of the nuclear envelope in such a manner that the nuclear envelope forms a part of the ER sac enclosing the chloroplast. In all these classes of algae except the Cryptophyceae, a regular network of tubules and vesicles, named the periplastidal reticulum, is present at a specific location between the chloroplast envelope and the chloroplast ER. In the Cryptophyceae, scattered vesicles are found between the chloroplast envelope and the chloroplast ER. Ribosomes which have been shown to be arranged to polysomes are found on the outer membrane of the chloroplast ER. It is proposed that nuclear-coded proteins which are destined for the chloroplast are synthesized on these polysomes, passing during synthesis into the lumen of the ER cisterna. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles then fuse with the outer membrane of the chloroplast envelope thereby delivering their contents to the lumen of the chloroplast envelope. Proteins then cross the inner membrane of the chloroplast envelope in an as yet unknown manner. Experimental evidence for this hypothesis comes from studies on Ochromonas danica using chloramphenicol and spectinomycin, which inhibit protein synthesis on plastid ribosomes, and cycloheximide, which inhibits protein synthesis on cytoplasmic ribosomes. In cells of Ochromonas exposed to chloramphenicol or spectinomycin, the periplastidal reticulum proliferates markedly becoming several layers thick. Presumably this build up of periplastidal reticulum occurs because the transport of cytoplasmically synthesized plastid proteins is slowed down when protein synthesis in the chloroplast is inhibited. Conversely, when cells of Ochromonas are treated with cycloheximide, there is a reduction in the amount of periplastidal reticulum presumably because there are no cytoplasmically synthesized proteins to be transported into the chloroplast.

scholarly journals ISG56/IFIT1 is primarily responsible for interferon-induced changes to patterns of parainfluenza virus type 5 transcription and protein synthesis

2013 ◽  
Vol 94 (1) ◽  
pp. 59-68 ◽  
Author(s):  
J. Andrejeva ◽  
H. Norsted ◽  
M. Habjan ◽  
V. Thiel ◽  
S. Goodbourn ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Virus Type ◽  
Cellular Protein ◽  
Parainfluenza Virus ◽  
Hydroxyl Group ◽  
Virus Protein ◽  
Viral Mrnas ◽  
Tetratricopeptide Repeats ◽  
Virus Transcription

Interferon (IFN) induces an antiviral state in cells that results in alterations of the patterns and levels of parainfluenza virus type 5 (PIV5) transcripts and proteins. This study reports that IFN-stimulated gene 56/IFN-induced protein with tetratricopeptide repeats 1 (ISG56/IFIT1) is primarily responsible for these effects of IFN. It was shown that treating cells with IFN after infection resulted in an increase in virus transcription but an overall decrease in virus protein synthesis. As there was no obvious decrease in the overall levels of cellular protein synthesis in infected cells treated with IFN, these results suggested that ISG56/IFIT1 selectively inhibits the translation of viral mRNAs. This conclusion was supported by in vitro translation studies. Previous work has shown that ISG56/IFIT1 can restrict the replication of viruses lacking a 2′-O-methyltransferase activity, an enzyme that methylates the 2′-hydroxyl group of ribose sugars in the 5′-cap structures of mRNA. However, the data in the current study strongly suggested that PIV5 mRNAs are methylated at the 2′-hydroxyl group and thus that ISG56/IFIT1 selectively inhibits the translation of PIV5 mRNA by some as yet unrecognized mechanism. It was also shown that ISG56/IFIT1 is primarily responsible for the IFN-induced inhibition of PIV5.

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