Studies on the Effects of the Removal of the Frontal Ganglion in Locusta Migratoria L

1967 ◽  
Vol 46 (1) ◽  
pp. 27-34
Author(s):  
KENNETH U. CLARKE ◽  
CEDRIC GILLOTT
Keyword(s):  
Protein Synthesis ◽  
Dna Content ◽  
Fat Body ◽  
Locusta Migratoria ◽  
Fourth Instar ◽  
Monod Model ◽  
Cytoplasmic Rna ◽  
Cytochemical Investigation ◽  
Frontal Ganglion ◽  
And Control

1. A cytochemical investigation was made of the RNA content of the cells of the mid-gut, fat body and epidermis in third- and fourth-instar Locusta migratoria L. from which the frontal ganglion had been removed, in control operated and in starved animals. In operated locusts the nucleus was smaller, the nucleoli small or absent, and the cytoplasmic RNA much less than that found in operated controls. No differences were observed in the DNA content of the cells. 2. Autoradiograph studies were made of the uptake of 3H-uridine into the cells of operated and control operated locusts. In operated locusts the appearance of labelled uridine in the nucleus was delayed, the rate of uptake slower, and the total amount incorporated less (never more than 25%) than in the controls. 3. Studies were made of the uptake of 14C-uridine into the nuclei of operated and control-operated locusts. Nuclei were isolated from locusts killed at known times after the isotope had been injected and their radioactivity was measured. The results confirmed those found in the radioautographic studies. 4. The significance of these results is considered in the light of the Jacob & Monod model of the control of protein synthesis.

The effect of removal of the frontal ganglion on growth and protein synthesis in young adults of Locusta migratoria

1974 ◽  
Vol 52 (2) ◽  
pp. 203-208 ◽  
Author(s):  
D. E. Bignell
Keyword(s):  
Young Adults ◽  
Protein Synthesis ◽  
Fat Body ◽  
Locusta Migratoria ◽  
Growth Arrest ◽  
Stomatogastric Nervous System ◽  
Food Passage ◽  
Frontal Ganglion

Removal of the Frontal ganglion in young adult locusts results in growth arrest, disruption of food passage in the gut, reduced faecal out put, and a high mortality. The effects of the operation in young adults differ in degree from those observed in larvae.An in vitro incubation technique was used to make a quantitative estimate of protein synthesis in the fat body after frontal ganglion removal and starvation. A significant reduction of protein synthesis after frontal ganglion removal was observed.The results are discussed in relation to the role of the stomatogastric nervous system in controlling food passage in the gut and the release of neurohormone from the corpora cardiaca.

scholarly journals Multivariate statistical data analysis of cell‐free protein synthesis toward monitoring and control

AIChE Journal ◽  
2021 ◽  
Author(s):  
Carlos A. Duran‐Villalobos ◽  
Olotu Ogonah ◽  
Beatrice Melinek ◽  
Daniel G. Bracewell ◽  
Trevor Hallam ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Data Analysis ◽  
Statistical Data ◽  
Monitoring And Control ◽  
Statistical Data Analysis ◽  
Multivariate Statistical ◽  
Free Protein ◽  
And Control ◽  
Cell Free Protein Synthesis

scholarly journals 40S ribosome profiling reveals distinct roles for Tma20/Tma22 (MCT-1/DENR) and Tma64 (eIF2D) in 40S subunit recycling

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
David J. Young ◽  
Sezen Meydan ◽  
Nicholas R. Guydosh
Keyword(s):  
Protein Synthesis ◽  
Neurological Disease ◽  
Ribosome Profiling ◽  
Minor Role ◽  
Stop Codons ◽  
Genes Encoding ◽  
Ribosome Footprinting ◽  
A Minor ◽  
And Control ◽  
In Cells

AbstractThe recycling of ribosomes at stop codons for use in further rounds of translation is critical for efficient protein synthesis. Removal of the 60S subunit is catalyzed by the ATPase Rli1 (ABCE1) while removal of the 40S is thought to require Tma64 (eIF2D), Tma20 (MCT-1), and Tma22 (DENR). However, it remains unclear how these Tma proteins cause 40S removal and control reinitiation of downstream translation. Here we used a 40S ribosome footprinting strategy to directly observe intermediate steps of ribosome recycling in cells. Deletion of the genes encoding these Tma proteins resulted in broad accumulation of unrecycled 40S subunits at stop codons, directly establishing their role in 40S recycling. Furthermore, the Tma20/Tma22 heterodimer was responsible for a majority of 40S recycling events while Tma64 played a minor role. Introduction of an autism-associated mutation into TMA22 resulted in a loss of 40S recycling activity, linking ribosome recycling and neurological disease.

Protein synthesis is required for rapid degradation of tubulin mRNA and other deflagellation-induced RNAs in Chlamydomonas reinhardi

1986 ◽  
Vol 6 (1) ◽  
pp. 54-61
Author(s):  
E J Baker ◽  
L R Keller ◽  
J A Schloss ◽  
J L Rosenbaum
Keyword(s):  
Protein Synthesis ◽  
Transcriptional Control ◽  
Protein S ◽  
Protein Synthesis Inhibitors ◽  
Control Factors ◽  
Flagellar Proteins ◽  
The Stability ◽  
And Control

After flagellar detachment in Chlamydomonas reinhardi, there is a rapid synthesis and accumulation of mRNAs for tubulin and other flagellar proteins. Maximum levels of these mRNAs (flagellar RNAs) are reached within 1 h after deflagellation, after which they are rapidly degraded to their predeflagellation levels. The degradation of alpha- and beta-tubulin RNAs was shown to be due to the shortening of their half-lives after accumulation (Baker et al., J. Cell Biol. 99:2074-2081, 1984). Deflagellation in the presence of protein synthesis inhibitors results in the accumulation of tubulin and other flagellar mRNAs by kinetics similar to those of controls. However, unlike controls, in which the accumulated mRNAs are rapidly degraded, these mRNAs are stabilized in cycloheximide. The stabilization by cycloheximide is specific for the flagellar mRNAs accumulated after deflagellation, since there is no change in the levels of flagellar mRNAs in nondeflagellated (uninduced) cells in the presence of cycloheximide. The kinetics of flagellar mRNA synthesis after deflagellation are shown to be the same in cycloheximide-treated and control cells by in vivo labeling and in vitro nuclear runoff experiments. These results show that protein synthesis is not required for the induced synthesis of flagellar mRNAs, and that all necessary transcriptional control factors are present in the cell before deflagellation, but that protein synthesis is required for the accelerated degradation of the accumulated flagellar mRNAs. Since cycloheximide prevents the induced synthesis and accumulation of flagellar proteins, it is possible that the product(s) of protein synthesis required for the accelerated decay of these mRNAs is a flagellar protein(s). The possibility that one or more flagellar proteins autoregulate the stability of the flagellar mRNAs is discussed.

scholarly journals A Nuclear-Polyhedrosis Virus of Spodoptera frugiperda Isolated in Puerto Rico.

1969 ◽  
Vol 63 (2) ◽  
pp. 162-169
Author(s):  
Goro Kuno
Keyword(s):  
Puerto Rico ◽  
Spodoptera Frugiperda ◽  
Inclusion Bodies ◽  
Nuclear Polyhedrosis Virus ◽  
Galleria Mellonella ◽  
Fat Body ◽  
Heliothis Zea ◽  
Fourth Instar ◽  
Polyhedrosis Virus ◽  
Nuclear Polyhedrosis

A nuclear-polyhedrosis virus was isolated from a larva of Spodoptera frugiperda collected in Puerto Rico. The virus was found to be pathogenic to the larvae of Heliothis zea and of S. frugiperda but nonpathogenic to those of Diatraea saccharalis and of Galleria mellonella. LD50 for the fourth instar larvae of H. zea and S. frugiperda inoculated per os were 1.25 x 103 and 2.7 x 103 polyhedral inclusion bodies, respectively. The tissues infected included hemocytes, fat body, muscle, and epidermis. Furthermore, transovarian transmission of the virus was found in the inoculated individuals of S. frugiperda.

scholarly journals DNA repair synthesis in human heterokaryons. III. The rapid and slow complementing varieties of xeroderma pigmentosum

1976 ◽  
Vol 20 (1) ◽  
pp. 207-213
Author(s):  
F. Giannelli ◽  
S.A. Pawsey
Keyword(s):  
Protein Synthesis ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Dependent Manner ◽  
Repair Synthesis ◽  
Normal Cells ◽  
Complementation Groups ◽  
Dna Repair Synthesis ◽  
And Control ◽  
The Relationship

Patients with Xeroderma pigmentosum and defective DNA excision repair can be distinguished as a rapid (r-XP) and slow (s-XP) complementing variety. When fused with normal cells, fibroblasts from the r-XP are complemented rapidly and in the absence of protein synthesis while those from the s-XP are complemented slowly by a process partly, but not entirely, dependent on protein synthesis. Heterokaryons with different ratios of r-XP to s-XP nuclei (i.e. 1:1-5 and 1-5:1) and control heterokaryons containing one normal and 1-5 r- or s-XP nuclei show that if cell fusion and incubation is conducted in medium preventing protein synthesis, the rXP cells do not complement the s-XP partner at all and, conversely, that the latter is not as effective as normal cells at complementing the rXP partner. On the contrary, if protein synthesis is permitted, the 2 types of XP cells complement each other in a gene dose-dependent manner and to an extent similar to that observed in the control heterokaryons. These findings indicate that the r- and s-XP varieties are caused by mutations at different loci and suggest that the products of these loci interact to produce a functional unit which is present in normal control cells but absent in the XP strains. The relationship between the complementation groups described here and those already reported in the literature being investigated.

Changes in protein during development of Triturus embryos

Development ◽  
1973 ◽  
Vol 30 (3) ◽  
pp. 647-659
Author(s):  
Hiroshi Imoh ◽  
Tsutomu Minamidani
Keyword(s):  
Protein Synthesis ◽  
Protein Content ◽  
Sodium Carbonate ◽  
Dna Content ◽  
Total Protein ◽  
Soluble Protein ◽  
Nuclear Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Tail Bud ◽  
Stage Of Development

The present paper reports basic data on DNA content, protein content, and protein synthesis in Triturus pyrrhogaster embryos during development from cleavage to the hatching stage. Except for measurements of DNA and total protein contents, embryos were labeled with sodium carbonate-14C for 10 h and fractionated into embryonic cell components, i.e. cytoplasmic mass, yolk and pigment granules, and nuclei, in a discontinuous density gradient of sucrose. The protein content and the radioactivity incorporated into protein were measured in each fraction. Those fractions combining protein soluble in buffer at pH 8·3 and in 0·25 N-HCl were further studied with polyacrylamide gel electrophoresis. In the newt embryo, four stages of active DNA increase were observed when cultured at constant temperature; they were gastrula, neurula, late tail-bud, and before-hatching stages. Total protein per embryo decreased from 3 to 2 mg during the development studied. The content of cytoplasmic soluble protein per embryo was low and constant throughout development. Synthesis of the fraction was observed at the earliest stage of development studied though the rate was not high and specific activity of the soluble protein increased during development. Qualitative changes in the newly synthesized protein were observed. With the yolk fraction, synthesis of protein, other than from probable contamination with the cytoplasmic fraction, was not detected and a detailed description was omitted. Changes were observed at two stages of development in the synthesis of nuclear protein soluble in buffer at pH 8·3, the first at gastrulation and the second at late tail-bud stage. The change at gastrulation seemed to be the start of syntheses of the nuclear soluble proteins, while quantitative enhancement rather than qualitative change was noticed at late tail-bud stage. Most of the nuclear protein soluble in 0·25 N-HCI was histone. The histone content increased in accordance with increase in the DNA content and the rate of DNA accumulation was accompanied by proportionate incorporation of radioactivity into histone. Among histone fractions, unique behaviour of the very lysine-rich histone was observed. The availability of [14C]sodium carbonate in rough estimations of protein synthesis in embryos and significance of the data obtained have been discussed.

Cytoplasmic DNA and basic protein synthesis in Megalobatrachus davidianus oocytes

Development ◽  
1971 ◽  
Vol 26 (2) ◽  
pp. 271-283
Author(s):  
Y. C. Kong ◽  
I. F. Lau ◽  
W. L. Lam ◽  
C. M. Choy
Keyword(s):  
Protein Synthesis ◽  
Dna Synthesis ◽  
Dose Response ◽  
Dna Content ◽  
Active Site ◽  
Basic Protein ◽  
Basic Proteins ◽  
Biochemical Event ◽  
Cytoplasmic Dna

Mature Megalobatrachus oocytes contain 43 µg DNA per oocyte, as compared with 250 pg DNA in a hepatocyte of the same animal. Megalobatrachus oocytes respond to CdR treatment by an increased incorporation of [3H]lysine into basic proteins associated with ooplasmic particles, with an optimal CdR concentration at 2 mM. The nucleolus is the most active site of [3H]lysine incorporation. It is suggested that CdR-stimulated basic protein synthesis is a common biochemical event during amphibian oogenesis. The dose response to CdR treatment may be a function of the c-DNA content or c-DNA synthesis potential in the ooplasm.

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