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The mechanism and functions of ATP-dependent proteases in bacterial and animal cells

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EJB Reviews

Part of the book series: EJB Reviews ((EJB REVIEWS,volume 1992))

Abstract

In eukaryotes and prokaryotes, the degradation of most cell proteins requires metabolic energy (Goldberg and St. John, 1976; Hershko and Ciechanover, 1982). This feature of intracellular proteolysis applies not only for cytosolic proteins in bacterial and animal cells. Mitochondria (Desautels and Goldberg, 1982a) and chloroplasts (Malek et al., 1984) also contain systems for complete degradation of abnormal proteins, and this process also requires ATP. An ATP requirement for proteolysis is surprising on thermodynamic grounds, since hydrolysis of peptide bonds should be a spontaneous, exergonic process, and protein breakdown by traditional proteases does not require energy-rich cofactors (Goldberg and St. John, 1976). Initial speculations concerning the energy requirement for proteolysis in eukaryotic cells led to the suggestion that ATP might be necessary for the function of lysosomes in which protein degradation was assumed to occur. However, bacteria lack such organelles, but do show a similar ATP dependence for proteolysis as animal cells (Olden and Goldberg, 1978). Therefore, this requirement must represent a more fundamental property of the degradative process.

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Abbreviations

Ub:

ubiquitin

UCDEN:

ubiquitin-conjugate-degrading enzyme

MalNEt:

N-ethylmaleimide

iPr2 P-F:

diisopropyl-fluorophosphate

PhMeSO2F:

phenylmethanesulfonyl fluoride

Git:

glutaryl

Mna:

methoxynaphthylamine

Suc:

succinyl

Moc:

methoxycoumarin

Mca:

aminomethylcoumarin

Phe-COCH2Cl:

phenyl-alanylchloromethylketone

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Goldberg, A.L. (1993). The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. In: EJB Reviews. EJB Reviews, vol 1992. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78046-2_1

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