Selective inhibition of collagen synthesis in sea urchin embryos by a low concentration of actinomycin D

1978 ◽  
Vol 112 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Dennis Gould ◽  
Stephen C. Benson
1972 ◽  
Vol 55 (1) ◽  
pp. 74-81 ◽  
Author(s):  
Brian L. Kotzin ◽  
Robert F. Baker

Experimental evidence suggests that exposure of sea urchin gastrulae to 5-bromodeoxyuridine (BUdR), an analog of thymidine, causes a reduction in the rate of synthesis of some RNA species usually transcribed at this stage of development. In pulse-chase experiments, 3H (in gastrula stage 8–15S nuclear DNA labeled with BUdR-3H) could not be chased, with unlabeled BUdR, into 20–60S size-range DNA; in similar experiments in which gastrulae were pulsed with thymidine-3H and then chased with unlabeled thymidine, 3H in 8–15S nuclear DNA could be extensively chased into 20–60S DNA. DNA-RNA hybridization assays indicate that gastrula stage nuclear DNA in the range of 20–60S has greater sequence homology for gastrula stage RNA-3H than does nuclear DNA of similar size-range taken from gastrulae exposed to BUdR for 1 hr. An explanation is offered for the effect of BUdR on transcription and DNA replication in sea urchin embryos.


1972 ◽  
Vol 1 (3) ◽  
pp. 157-165 ◽  
Author(s):  
I. Pucci-Minafra ◽  
C. Casano ◽  
C. La Rosa

1971 ◽  
Vol 50 (2) ◽  
pp. 516-528 ◽  
Author(s):  
Rudolf A. Raff ◽  
Gerald Greenhouse ◽  
Kenneth W. Gross ◽  
Paul R. Gross

Studies employing colchicine binding, precipitation with vinblastine sulfate, and acrylamide gel electrophoresis confirm earlier proposals that Arbacia punctulata and Lytechinus pictus eggs and embryos contain a store of microtubule proteins. Treatment of 150,000 g supernatants from sea urchin homogenates with vinblastine sulfate precipitates about 5% of the total soluble protein, and 75% of the colchicine-binding activity. Electrophoretic examination of the precipitate reveals two very prominent bands. These have migration rates identical to those of the A and B microtubule proteins of cilia. These proteins can be made radioactive at the 16 cell stage and at hatching by pulse labeling with tritiated amino acids. By labeling for 1 hr with leucine-3H in early cleavage, then culturing embryos in the presence of unlabeled leucine, removal of newly synthesized microtubule proteins from the soluble pool can be demonstrated. Incorporation of labeled amino acids into microtubule proteins is not affected by culturing embryos continuously in 20 µg/ml of actinomycin D. Microtubule proteins appear, therefore, to be synthesized on "maternal" messenger RNA. This provides the first protein encoded by stored or "masked" mRNA in sea urchin embryos to be identified.


2021 ◽  
Vol 172 ◽  
pp. 112922
Author(s):  
Laura DeMiguel-Jiménez ◽  
Nestor Etxebarria ◽  
Xabier Lekube ◽  
Urtzi Izagirre ◽  
Ionan Marigómez

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