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ATP-dependent release of TCA-precipitable peptides from mitochondria-containing stroma (MCS) is described. The process is independent of ubiquitin, but is sensitive to hemin and to heat treatment. Neither chloramphenicol nor EGTA inhibit. 50% of the activity is dependent on charged tRNA. The peptides released from MCS possess a molecular mass of about 1-5 kDa and are degraded to TCA-soluble compounds...
The ATP-dependent breakdown of mitochondria-containing stroma proceeds via the ubiquitin-requiring pathway. The proteolysis is linked to a large ATP-cleaved consumption amounting to 1 ATP per peptide bond or more. Proteins of mitochondria-containing stroma are much better substrates of ATP-ubiquitindependent proteolysis than heat-denatured ones. Hemin suppresses both proteolysis and ATP hydrolysis.
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