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ATP-dependent proteolysis in yeast mitochondria

T Yasuhara¹, Y Mera, T Nakai

¹Meiji Institute of Health Science, Kanagawa.

Journal of Biochemistry

|June 1, 1994

Summary

Yeast mitochondria possess an ATP-dependent proteolysis system that degrades mitochondrial translation products. This system is sensitive to hemin and associated with the inner mitochondrial membrane.

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Area of Science:

Mitochondrial biology
Protein degradation
Biochemistry

Background:

Mitochondria contain unique protein synthesis machinery.
Regulation of mitochondrial protein turnover is crucial for cellular function.

Purpose of the Study:

To characterize the ATP-dependent proteolysis system in yeast mitochondria.
To identify factors influencing the degradation of mitochondrial translation products.

Main Methods:

Incubation of isolated yeast mitochondria with radiolabeled mitochondrial translation products.
Assay of proteolysis in response to ATP and related nucleotides.
Inhibition studies using specific chemical agents and metal ions.
Analysis of degradation products using SDS-PAGE.

Main Results:

ATP addition stimulated the degradation of mitochondrial polypeptides.
ADP, GTP, and CTP showed partial activation, while non-hydrolyzable ATP analogs did not.
Carboxyatractyloside and o-phenanthroline inhibited proteolysis, with inhibition reversed by Mn2+ or Co2+.
Hemin inhibited the system with a half-maximum inhibition at 12 microM.
Submitochondrial particles retained activity, indicating association with the inner membrane.

Conclusions:

Yeast mitochondria possess an ATP-dependent and hemin-sensitive proteolysis system.
This system is localized to the inner mitochondrial membrane.
A chelator-sensitive protease likely plays a role in this degradation pathway.

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