scholarly journals Effect of virus infection on the stability and synthesis of actinomycin-resistant ribonucleic acid in baby-hamster kidney cells

1967 ◽  
Vol 105 (3) ◽  
pp. 987-993 ◽  
Author(s):  
S J Martin ◽  
F. Brown

1. The sucrose-gradient pattern of 32P-labelled RNA synthesized in actinomycintreated baby-hamster kidney cells infected with foot-and-mouth-disease virus depends greatly on the period of labelling. 2. Fractions are formed in infected cells that sediment at 12–20s and have the same base composition as similar fractions found in non-infected cells that have been treated with actinomycin. 3. In the presence of guanidine, which completely inhibits viral RNA synthesis, these fractions are labelled to a greater extent than in non-infected cells.

1975 ◽  
Vol 53 (9) ◽  
pp. 950-957 ◽  
Author(s):  
Dennis E. Vance ◽  
Rita M. Dahlke

Semliki Forest virus inhibits phosphatidylethanolamine biosynthesis in baby hamster kidney-21 cells 6 h after infection. Viral infection reduced the incorporation of [1,2-14C]-ethanolamine into intact cells by approximately 50%. A similar reduction in the activity of the ethanolaminephosphotransferase (EC 2.7.8.1) was also observed. The apparent Km for CDPethanolamine was 60 μM for the microsomal enzymes from infected or mock-infected cells. In addition, exogenous diglyceride only stimulated by 1.5-fold the ethanolaminephosphotransferase from virus- or mock-infected cells, whereas the same diglyceride preparations stimulated the cholinephosphotransferase (EC 2.7.8.2) from baby hamster kidney cells by sixfold. Generation of endogenous diglyceride by pretreatment of the microsomes with phospholipase C (EC 3.1.4.3) stimulated the activity of the cholinephosphotransferase but not the ethanolaminephosphotransferase. Semliki Forest virus does not inhibit all microsomal enzymes, since the activities of NADH- K3Fe(CN)6 reductase and NADH dehydrogenase (EC 1.6.99.3) were not affected. The ethanolaminephosphotransferase from virus- and mock-infected cells showed similar profiles of activity as a function of temperature; this result and other studies suggest that that membranous environment of the ethanolaminephosphotransferase was not significantly modified by the virus.


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