Evidence for the involvement of a rapidly turning over protease in the degradation of cytochrome oxidase in Neurospora crassa

Abstract

Treatment of N. crassa cultures with cycloheximide followed by washing and incubation in drug-free fresh medium results in a rapid decline in cytochrome oxidase activity. This is associated with the degradation of higher molecular weight subunits of cytochrome oxidase under these conditions. The protease activity associated with the mitochondrial preparation decreases during cycloheximide treatment and rapidly returns to normal levels on subsequent washing and transfer to drug-free fresh medium. It is suggested that the steady-state level of cytochrome oxidase is governed by a rapidly turning over cytoplasmically synthesized mitochondrial protease.