Effect of the multicatalytic proteinase (prosome) on translational activity in rabbit reticulocyte lysates

In a message-dependent reticulocyte lysate translation system, incorporation of 3H]leucine into acid-insoluble protein is increased following selective removal of the multicatalytic proteinase (MCP) with a monospecific antibody. Re-addition of active proteinase to previously depleted lysates reverses this effect in that the same low levels of translational product are measured as in untreated lysates. Addition of histone-stimulated MCP further depresses the level of protein product. Conversely, lysates supplemented with inactivated MCP retain the higher level of translational activity which is measured after precipitation of the enzyme with antibody. In these lysates, the effect of the antibody on translational activity is inversely correlated with that on hydrolytic activity towards 14C]methylcasein or N-succinyl-Leu-Leu-Val-Tyr-4-methyl-7-coumarylamide, two substrates of the MCP. These results showing that the MCP is capable of modulating translational activity in vitro, suggest an important role of this molecule in the in vivo translational process.