Messenger RNA for the insect storage protein calliphorin: In vitro translation and chromosomal hybridization analyses of a 20 S poly(A)-RNA fraction

1978 ◽  
Vol 16 (3-4) ◽  
pp. 355-371 ◽  
Author(s):  
D. J. Kemp ◽  
J. A. Thomson ◽  
W. J. Peacock ◽  
T. J. V. Higgins
Keyword(s):  
Storage Protein ◽  
Messenger Rna ◽  
In Vitro Translation

scholarly journals In vitro translation of avian vitellogenin messenger RNA.

1977 ◽  
Vol 252 (22) ◽  
pp. 8320-8327 ◽  
Author(s):  
J.I. Gordon ◽  
R.G. Deeley ◽  
A.T. Burns ◽  
B.M. Paterson ◽  
J.L. Christmann ◽  
...  
Keyword(s):  
Messenger Rna ◽  
In Vitro Translation

scholarly journals Identification of storage-protein messenger RNA of the fleshfly Sarcophaga peregrina

1982 ◽  
Vol 203 (3) ◽  
pp. 571-575 ◽  
Author(s):  
T Tahara ◽  
Y Maeda ◽  
A Kuroiwa ◽  
K Ueno ◽  
M Obinata ◽  
...  
Keyword(s):  
Density Gradient ◽  
Storage Protein ◽  
Messenger Rna ◽  
Fat Body ◽  
Density Gradient Centrifugation ◽  
Signal Sequence ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Sucrose Density Gradient Centrifugation

Storage-protein mRNA was found to be abundant in poly(A)-containing RNA extracted from the fat-body of third-instar larvae of Sarcophaga peregrina (fleshfly). This RNA sedimented at the position of 19S on sucrose-density-gradient centrifugation and the product of its translation in vitro was 75K protein (protein of mol.wt. 75 000), which was precipitated specifically with antibody against storage protein. This product was suggested to contain a signal sequence that is missing in mature storage protein. The poly(A)-containing RNA was also found to contain much of another mRNA coding for 25K protein (protein of mol.wt. 25 000), but the function of this protein is unknown.

scholarly journals Comparison of messenger RNA pools in active and dormant Artemia franciscana embryos: evidence for translational control

1992 ◽  
Vol 164 (1) ◽  
pp. 103-116 ◽  
Author(s):  
G. E. Hofmann ◽  
S. C. Hand
Keyword(s):  
Protein Synthesis ◽  
Translational Control ◽  
Messenger Rna ◽  
Artemia Franciscana ◽  
In Vitro Translation ◽  
Translation Techniques ◽  
Polysome Profile ◽  
Anaerobic Dormancy ◽  
Qualitative Changes

In response to environmental anoxia, embryos of the brine shrimp Artemia franciscana enter a dormant state during which energy metabolism and development are arrested. The intracellular acidification that correlates with this transition into anaerobic dormancy has been linked to the inhibition of protein synthesis in quiescent embryos. In this study, we have addressed the level of control at which a mechanism mediated by intracellular pH might operate to arrest protein synthesis. Two independent lines of evidence suggest that there is an element of translational control when protein synthesis is arrested in dormant embryos. First, as determined by in vitro translation techniques, there were no significant quantitative differences in mRNA pools in dormant as compared to actively developing embryos. In addition, fluorography of the translation products showed that there are no large qualitative changes in mRNA species when embryos become dormant. These data suggest that there was no net degradation of mRNA pools in dormant embryos and that protein synthesis may therefore be controlled more strongly at translation than at transcription. Second, polysome profile studies showed that dormant embryos possess reduced levels of polysomes relative to those found in cells or active embryos. The disaggregation of polysomes is an indication that the initiation step in protein synthesis is disrupted and is further evidence that the mechanism involved in protein synthesis arrest in dormant Artemia involves translational control.

scholarly journals Erythrocyte membrane protein band 3: its biosynthesis and incorporation into membranes.

1981 ◽  
Vol 91 (3) ◽  
pp. 637-646 ◽  
Author(s):  
E Sabban ◽  
V Marchesi ◽  
M Adesnik ◽  
D D Sabatini
Keyword(s):  
Plasma Membrane ◽  
Electrophoretic Mobility ◽  
Messenger Rna ◽  
Transmembrane Protein ◽  
Band 3 ◽  
In Vitro Translation ◽  
Intact Cells ◽  
Amino Terminal ◽  
In Cells

Band 3, a transmembrane protein that provides the anion channel of the erythrocyte plasma membrane, crosses the membrane more than once and has a large amino terminal segment exposes on the cytoplasmic side of the membrane. The biosynthesis of band 3 and the process of its incorporation into membranes were studied in vivo in erythroid spleen cells of anemic mice and in vitro in protein synthesizing cell-free systems programmed with polysomes and messenger RNA (mRNA). In intact cells newly synthesized band 3 is rapidly incorporated into intracellular membranes where it is glycosylated and it is subsequently transferred to the plasma membrane where it becomes sensitive to digestion by exogenous chymotrypsin. The appearance of band 3 in the cell surface is not contingent upon its glycosylation because it proceeds efficiently in cells treated with tunicamycin. The site of synthesis of band 3 in bound polysomes was established directly by in vitro translation experiments with purified polysomes or with mRNA extracted from them. The band-3 polypeptide synthesized in an mRNA-dependent system had the same electrophoretic mobility as that synthesized in cells treated with tunicamycin. When microsomal membranes were present during translation, the in vitro synthesized band-3 polypeptide was cotranslationally glycosylated and inserted into the membranes. This was inferred from the facts that when synthesis was carried out in the presence of membranes the product had a lower electrophoretic mobility and showed partial resistance to protease digestion. Our observations indicate that the primary translation product of band-3 mRNA is not proteolytically processed either co- or posttranslationally. It is, therefore, proposed that the incorporation of band 3 into the endoplasmic reticulum (ER) membrane is initiated by a permanent insertion signal. To account for the cytoplasmic exposure of the amino terminus of the polypeptide we suggest that this signal is located within the interior of the polypeptide. a mechanism that explains the final transmembrane disposition of band 3 in the plasma membrane as resulting from the mode of its incorporation into the ER is presented.

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