scholarly journals The role of ribosomal ribonucleic acid in the structure and function of mammalian brain ribosomes

1974 ◽  
Vol 143 (2) ◽  
pp. 419-426 ◽  
Author(s):  
Barbara Kay Grove ◽  
Terry C. Johnson
Keyword(s):  
Protein Synthesis ◽  
Protein Interactions ◽  
Chemical Properties ◽  
Chain Elongation ◽  
Synthetic Activity ◽  
Mammalian Brain ◽  
28S Rrna ◽  
Diethylaminoethyl Cellulose ◽  
Brain Ribosomes

In order to resolve the functional role of intact rRNA in polypeptide chain elongation mouse brain ribosomes were treated with dilute pancreatic or T1 RNAase (ribonuclease). After RNAase treatment, several physical–chemical properties as well as the functional activity of the ribosomes were measured. RNAase treatment resulted in the extensive hydrolysis of both 18S and 28S rRNA; however, the sedimentation properties of mono-ribosomes were unaltered and more than 90% of the relatively low-molecular-weight RNA fragments remained associated with ribosome particles. Analysis of the ability of RNAase-treated ribosomes to participate in cell-free protein synthesis showed that ribosomes with less than 2% intact rRNA retained more than 85% of their activity in polyphenylalanine incorporation. Proof that the incorporation of phenylalanine by ribosomes with hydrolysed rRNA actually represented active translocation was obtained by the effective inhibition of incorporation by diphtheria toxin. In addition, the oligopeptide products of protein synthesis could be identified by BD (benzoylated diethylaminoethyl)-cellulose column chromatography. Analysis of the size distribution of oligopeptides synthesized by normal and RNAase-treated ribosomes showed no significant differences which indicated that there was no change in the proportion of ribosomes engaged in protein synthesis. Thus strong RNA–protein and protein–protein interactions must serve to maintain the functional integrity of ribosomes even when the rRNA is extensively degraded. The ability of the enzyme-treated ribosomes to efficiently incorporate amino acids clearly demonstrated that ‘intact’ rRNA is not required for protein-synthetic activity.

scholarly journals Key role of l-alanine in the control of hepatic protein synthesis

1987 ◽  
Vol 241 (2) ◽  
pp. 491-498 ◽  
Author(s):  
D Pérez-Sala ◽  
R Parrilla ◽  
M S Ayuso
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Physiological Role ◽  
Chain Elongation ◽  
Liver Protein ◽  
Isolated Liver Cells ◽  
Metabolic Transformation ◽  
Hepatic Protein Synthesis

We investigated the effects of administration of single amino acids to starved rats on the regulation of protein synthesis in the liver. Of all the amino acids tested, only alanine, ornithine and proline promoted statistically significant increases in the extent of hepatic polyribosome aggregation. The most effective of these was alanine, whose effect of promoting polyribosomal aggregation was accompanied by a decrease in the polypeptide-chain elongation time. The following observations indicate that alanine plays an important physiological role in the regulation of hepatic protein synthesis. Alanine was the amino acid showing the largest decrease in hepatic content in the transition from high (fed) to low (starved) rates of protein synthesis. The administration of glucose or pyruvate is also effective in increasing liver protein synthesis in starved rats, and their effects were accompanied by an increased hepatic alanine content. An increase in hepatic ornithine content does not lead to an increased protein synthesis, unless it is accompanied by an increase of alanine. The effect of alanine is observed either in vivo, in rats pretreated with cycloserine to prevent its transamination, or in isolated liver cells under conditions in which its metabolic transformation is fully impeded.

scholarly journals ABERRANT INTRANUCLEOLAR MATURATION OF RIBOSOMAL PRECURSORS IN THE ABSENCE OF PROTEIN SYNTHESIS

1970 ◽  
Vol 45 (3) ◽  
pp. 554-564 ◽  
Author(s):  
Nessly C. Craig ◽  
Robert P. Perry
Keyword(s):  
Protein Synthesis ◽  
Ionic Strength ◽  
Ribosomal Rna ◽  
Buoyant Density ◽  
Protein Composition ◽  
28S Rrna ◽  
Maturation Process ◽  
Variable Response ◽  
Protein Complement

To help elucidate the role of protein in the maturation of ribosomal RNA in cultured L cells, we have studied the effects of cycloheximide upon the maturation process and upon the intranucleolar ribonucleoprotein particles containing the "preribosomal RNA's." Five parameters of these particles were analyzed: (a) extractability, (b) sedimentation characteristics in sucrose gradients, (c) RNA composition, (d) buoyant density in CsCl gradients, and (e) effects of increased ionic strength on the buoyant density. When protein synthesis is inhibited, the rate of conversion of the precursor 45S ribosomal RNA is rapidly diminished, falling to less than 30% of the control rate within 1 hr. Nevertheless, in terms of the first three parameters there is no difference between control and cycloheximide nucleolar particles. However, the cycloheximide particles have a lower and more heterogeneous buoyant density and a more variable response to increased ionic strength. The results imply that the protein composition of the cycloheximide particles is different from that of particles from control cells, and that the entire protein complement is not necessary for the first cleavages in the maturation process, although it is necessary for the normal rate of processing and for the eventual appearance of both 18S and 28S rRNA in mature ribosomes.

scholarly journals SPECIFIC PROTEIN SYNTHESIS IN CELLULAR DIFFERENTIATION

1972 ◽  
Vol 55 (3) ◽  
pp. 653-680 ◽  
Author(s):  
M. Paul ◽  
M. R. Goldsmith ◽  
J. R. Hunsley ◽  
F. C. Kafatos
Keyword(s):  
Protein Synthesis ◽  
Messenger Rna ◽  
Developmental Stages ◽  
Specific Protein ◽  
Chain Elongation ◽  
Synthetic Activity ◽  
Translational Efficiency ◽  
Kinetics Of

Silkmoth follicles, arranged in a precise developmental sequence within the ovariole, yield pure and uniform populations of follicular epithelial cells highly differentiated for synthesis of the proteinaceous eggshell (chorion). These cells can be maintained and labeled efficiently in organ culture; their in vitro (and cell free) protein synthetic activity reflects their activity in vivo. During differentiation the cells undergo dramatic changes in protein synthesis. For 2 days the cells are devoted almost exclusively to production of distinctive chorion proteins of low molecular weight and of unusual amino acid composition. Each protein has its own characteristic developmental kinetics of synthesis. Each is synthesized as a separate polypeptide, apparently on monocistronic messenger RNA (mRNA), and thus reflects the expression of a distinct gene. The rapid changes in this tissue do not result from corresponding changes in translational efficiency. Thus, the peptide chain elongation rate is comparable for chorion and for proteins synthesized at earlier developmental stages (1.3–1.9 amino acids/sec); moreover, the spacing of ribosomes on chorion mRNA (30–37 codons per ribosome) is similar to that encountered in other eukaryotic systems.

scholarly journals Measurement of the protein-synthetic activity in vivo of various tissues in rats by using [3H]Puromycin

1979 ◽  
Vol 184 (3) ◽  
pp. 663-668 ◽  
Author(s):  
K Nakano ◽  
H Hara
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Relative Rate ◽  
Chain Elongation ◽  
Synthetic Activity ◽  
Tissue Protein Synthesis ◽  
A New Technique ◽  
Protein Free Diet

The validity of a new technique was examined for estimating the protein-synthetic activity of various tissues in vivo. The basic assumption underlying the method is that the number of peptide chains growing on each active ribosome would increase as the protein-synthetic activity of each tissue increases. The principle of the procedure, which was devised originally by Wool & Kurihara [(1967) Proc. Natl. Acad. Sci. U.S.A. 58, 2401-2407] to determine in vitro the number of functional ribosomes in skeletal muscle, is as follows. Puromycin is known to bind easily to the C-terminal end of the growing peptide on ribosomes and thus stop further chain elongation. Hence, if the number of puromycin molecules attached to the nascent peptide is determined by using radioactive puromycin as a tracer, one can estimate the number of growing peptides, i.e. the activity of tissue protein synthesis. By using this technique, it is shown that both starvation and the feeding of a protein-free diet caused marked decreases in the relative rate of formation of peptidyl-puromycin, i.e. activity of protein synthesis in liver, skeletal muscle, heart, spleen, testis, lung, kidney and intestine.

Role of elongation factor 2 in regulating peptide-chain elongation in the heart

1994 ◽  
Vol 266 (4) ◽  
pp. E628-E634 ◽  
Author(s):  
T. C. Vary ◽  
A. Nairn ◽  
C. J. Lynch
Keyword(s):  
Protein Synthesis ◽  
Elongation Factor ◽  
Diabetic Rats ◽  
Peptide Chain ◽  
Chain Elongation ◽  
Translational Efficiency ◽  
Ribosomal Subunits ◽  
Elongation Factor 2 ◽  
Cardiac Muscles

Cardiac muscles of experimentally induced diabetic rats show a progressive decrease in the rate of protein synthesis. The decline in protein synthesis is associated with decreases in both the number and efficiency of cardiac ribosomes. In hearts from 48 h diabetic rats, the decrease in protein synthesis was accounted for solely by a 28% reduction in the ribosome content. In contrast, the inhibition of protein synthesis in hearts from 72 h diabetic rats resulted from a reduction in both the ribosome content (28%) and the translational efficiency (30%). The decreased translational efficiency was not associated with an increase of RNA in ribosomal subunits, indicating the defect resulted from an inhibition of peptide-chain elongation/termination. Diabetes of 72 h duration resulted in a 37% inhibition in the rate of peptide-chain elongation. The decreased rate of peptide-chain elongation was associated with a 66% reduction in the amount of elongation factor 2 (EF-2). Treatment of diabetic rats with insulin for 3 days was sufficient to reverse the effects of 72 h diabetes on protein synthesis, RNA content, and translational efficiency. Also, insulin therapy increased the EF-2 content of diabetic rats to control values. These studies suggest that decreased EF-2 content is a molecular mechanism for the impaired rates of peptide-chain elongation in diabetes.

Role of small nuclear RNAs in eukaryotic gene expression

2013 ◽  
Vol 54 ◽  
pp. 79-90 ◽  
Author(s):  
Saba Valadkhan ◽  
Lalith S. Gunawardane
Keyword(s):  
Gene Expression ◽  
Protein Interactions ◽  
Rna Stability ◽  
Splice Sites ◽  
Branch Site ◽  
Small Nuclear Rnas ◽  
Eukaryotic Gene Expression ◽  
Eukaryotic Gene ◽  
Rna Biogenesis

Eukaryotic cells contain small, highly abundant, nuclear-localized non-coding RNAs [snRNAs (small nuclear RNAs)] which play important roles in splicing of introns from primary genomic transcripts. Through a combination of RNA–RNA and RNA–protein interactions, two of the snRNPs, U1 and U2, recognize the splice sites and the branch site of introns. A complex remodelling of RNA–RNA and protein-based interactions follows, resulting in the assembly of catalytically competent spliceosomes, in which the snRNAs and their bound proteins play central roles. This process involves formation of extensive base-pairing interactions between U2 and U6, U6 and the 5′ splice site, and U5 and the exonic sequences immediately adjacent to the 5′ and 3′ splice sites. Thus RNA–RNA interactions involving U2, U5 and U6 help position the reacting groups of the first and second steps of splicing. In addition, U6 is also thought to participate in formation of the spliceosomal active site. Furthermore, emerging evidence suggests additional roles for snRNAs in regulation of various aspects of RNA biogenesis, from transcription to polyadenylation and RNA stability. These snRNP-mediated regulatory roles probably serve to ensure the co-ordination of the different processes involved in biogenesis of RNAs and point to the central importance of snRNAs in eukaryotic gene expression.

Characteristics Of The Structure Formation Of Gypsum Binder Modified With Zinc Hydrosilicates

2020 ◽  
pp. 40-46
Keyword(s):  
Synergistic Effect ◽  
Physicochemical Properties ◽  
Structure Formation ◽  
Silicic Acid ◽  
Chemical Properties ◽  
Crystal Formation ◽  
Ability To Act ◽  
Chemical Factors ◽  
Sorption Characteristics

The authors' methodic for assessing the role of chemical and physic-chemical factors during the structure formation of gypsum stone is presented in the article. The methodic is also makes it possible to reveal the synergistic effect and to determine the ranges of variation of controls factors that ensure maximum values of such effect. The effect of a micro-sized modifier based on zinc hydro-silicates on the structure formation of building gypsum is analyzed and corresponding dependencies are found. It is shown that effects of influence of modifier on the properties of gypsum compositions are determined by chemical properties of modifier. Among the mentioned properties are sorption characteristics (which depend on the amount of silicic acid and its state) and physicochemical properties - the ability to act as a substrate during crystal formation. The proposed method can also be extended to other binding substances and materials. This article contributes to the understanding of the processes that occur during the structure formation of composites, which will make it possible to control the structure formation in the future, obtaining materials with a given set of properties.

The Nature of S-N Bonding in Sulfonamides and Related Compounds: Insights into π-Bonding Contributions from Sulfur K-Edge XAS

2020 ◽  
Author(s):  
Tulin Okbinoglu ◽  
Pierre Kennepohl
Keyword(s):  
Density Functional ◽  
Chemical Properties ◽  
Functional Theory ◽  
Rotational Barriers ◽  
Td Dft ◽  
Nitrogen Bonds ◽  
X Ray Absorption ◽  
Related Compounds ◽  
And Chemical Properties

Molecules containing sulfur-nitrogen bonds, like sulfonamides, have long been of interest due to their many uses and chemical properties. Understanding the factors that cause sulfonamide reactivity is important, yet their continues to be controversy regarding the relevance of S-N π bonding in describing these species. In this paper, we use sulfur K-edge x-ray absorption spectroscopy (XAS) in conjunction with density functional theory (DFT) to explore the role of S<sub>3p</sub> contributions to π-bonding in sulfonamides, sulfinamides and sulfenamides. We explore the nature of electron distribution of the sulfur atom and its nearest neighbors and extend the scope to explore the effects on rotational barriers along the sulfur-nitrogen axis. The experimental XAS data together with TD-DFT calculations confirm that sulfonamides, and the other sulfinated amides in this series, have essentially no S-N π bonding involving S<sub>3p</sub> contributions and that electron repulsion and is the dominant force that affect rotational barriers.

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