scholarly journals Inhibition of cell-free protein synthesis by low-molecular-weight nuclear polyadenylate-containing ribonucleic acid species isolated from the lactating guinea pig

1980 ◽  
Vol 186 (2) ◽  
pp. 561-570 ◽  
Author(s):  
I C Bathurst ◽  
R K Craig ◽  
P N Campbell

1. Poly(A)-containing RNA was isolated from the nuclei of mammary gland, liver and brain of lactating guinea pigs. 2. Total nuclear poly(A)-containing RNA from mammary gland inhibited mRNA-directed protein synthesis by a wheat-germ cell-free system. It also inhibited the endogenous activity of the wheat-germ and other cell-free systems. It did not inhibit a wheat-germ cell-free system directed by poly(U). 3. Total nuclear poly(A)-containing RNA from liver and brain did not inhibit the mRNA-directed wheat-germ system. 4. Fractionation of the nuclear poly(A)-containing RNA revealed inhibitory activity in the less than 10 S fraction from mammary gland as well as that from liver and brain. 5. The mechanism of protein-synthesis inhibition appeared to be at the level of elongation. 6. The inhibitory activity could be reversed in a wheat-germ system by increasing the amount of S-30 supernatant. 7. The mechanism of inhibition of protein synthesis is discussed in relation to other RNA species known to inhibit such systems.

1984 ◽  
Vol 4 (9) ◽  
pp. 783-788 ◽  
Author(s):  
Andres M. Lozano ◽  
Vasek A. Mezl

Methylglyoxal was a weak inhibitor of translation in the reticulocyte-lysate cell-free system and it did not display cap-dependent inhibition. A similar inhibition was obtained in a wheat-germ cell-free system that displayed extensive cap-dependent inhibition with the cap analogue 7-methylguanosine phosphate. These results show that the chemical reaction of methyl-glyoxat with 7-methylguanosine is not the mechanism for the inhibition of protein synthesis by methylglyoxal and that methylglyoxat is a weak general inhibitor of translation.


1984 ◽  
Vol 4 (7) ◽  
pp. 535-540 ◽  
Author(s):  
Vasek A. Mezl ◽  
Andres Lozano

The translation of polyadenylated and of non-poly-adenylated RNA obtained from lactating rat mammary gland was almost totally inhibited by 0,5 mM 7-methylguanosine-5′-phosphate in the wheat-germ cell-free system, This inhibition was maintained during the preparation of the 9S whey-protein mRNA and of the 12S and ISS casein mRNAs, Chemical decapping of these mRNAs caused a similar reduction of their activity. Although a large fraction of milk-protein mRNAs have been reported to lack 3′-polyadenylation, these results show that the mRNAs in the mammary gland do contain a 5′-terminal 7-methylguanosine cap.


1979 ◽  
Vol 57 (5) ◽  
pp. 429-435
Author(s):  
Elahe Elahi ◽  
George H. Jones

Differential effects of Mg2+, spermidine, and reticulocyte ribosomal wash factors on the translation of endogenous, myeloma, and globin mRNA's have been observed in studies with the wheat germ cell-free protein synthesizing system. Spermidine stimulated globin mRNA translation but not the translation of endogenous wheat germ messages, and the polyamine actually inhibited the translation of myeloma mRNA. Ribosomal wash factors, on the other hand, stimulated endogenous and myeloma mRNA dependent protein synthesis in an Mg2+-dependent fashion but inhibited globin mRNA translation. The combination of ribosomal wash factors and spermidine was either stimulatory or inhibitory depending on the Mg2+ concentration and the message. It was further observed that translation of exogenous myeloma mRNA proceeded for only 60 min at 25 °C under all conditions tested in this study, while translation of endogenous wheat germ messages continued for longer periods of time. No differential effects of spermidine on the synthesis of high molecular weight myeloma proteins were observed.


1976 ◽  
Vol 71 (1) ◽  
pp. 85-91 ◽  
Author(s):  
Radomir CRKVENJAKOV ◽  
Slavko CUSIC ◽  
Ivan IVANOVIC ◽  
Vladimir GLISIN

2020 ◽  
Vol 11 ◽  
Author(s):  
Andrey V. Zhigailov ◽  
Alena M. Alexandrova ◽  
Anna S. Nizkorodova ◽  
Gulshan E. Stanbekova ◽  
Ruslan V. Kryldakov ◽  
...  

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