In vitro inactivation of ascites ribosomes by colicin E 3 |
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Authors: | F Turnowsky J Drews F Eich G Högenauer |
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Institution: | SANDOZ Forschungsinstitut Ges.m.b.H. A-1235 Vienna, Brunnerstraße 59 / Austria |
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Abstract: | Colicin E 3 treatment of 80 S ribosomes from mouse ascites cells completely arrests in vitro protein synthesis. Isolated 40 S subunits are resistant to the colicin action while the larger subunit becomes inactivated after treatment with this protein. 40 S subunits derived from colicin E 3 treated 80 S ribosomes lose their ability to participate in polyphenylalanine synthesis. Colicin E 3 damaged 80 S ribosomes appear to be functional with regard to Met-tRNAfMet binding while they fail to attach Phe-tRNA to the A-site. Thus, except for the susceptibility of their larger subunits to colicin, the inactivation mechanism of 80 S particles resembles the process which alters the bacterial ribosome. |
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