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Effect of the multicatalytic proteinase (prosome) on translational activity in rabbit reticulocyte lysates
Author(s) -
Kuehn Lothar,
Dahlmann Burkhardt,
Kopp Friedrich
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80570-9
Subject(s) - reticulocyte , protein biosynthesis , in vivo , biochemistry , in vitro , chemistry , antibody , microbiology and biotechnology , leucine , proteinase k , translation (biology) , translational regulation , enzyme , biology , messenger rna , amino acid , immunology , gene
In a message‐dependent reticulocyte lysate translation system, incorporation of [ 3 H]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 [ 14 C]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.