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Protein Unfolding and Degradation by the CLP Family of Proteases

Published online by Cambridge University Press:  02 July 2020

Martin Kessel ,
Fabienne Beuron ,
Frank Booy ,
Eva Kocsis ,
Michael Maurizi  and
Alasdair Steven
Martin Kessel
Affiliation:
Lab. of Structural Biology, NIAMS, NIH, Bethesda, Md.20892
Fabienne Beuron
Affiliation:
Lab. of Structural Biology, NIAMS, NIH, Bethesda, Md.20892
Frank Booy
Affiliation:
Lab. of Structural Biology, NIAMS, NIH, Bethesda, Md.20892
Eva Kocsis
Affiliation:
Lab. of Structural Biology, NIAMS, NIH, Bethesda, Md.20892
Michael Maurizi
Affiliation:
Lab. of Cell Biology, NCI, NIH, Bethesda, Md.20892
Alasdair Steven
Affiliation:
Lab. of Structural Biology, NIAMS, NIH, Bethesda, Md.20892
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Extract

ATP-dependent proteases play a major role in regulatory protein degradation in both prokaryotic and eukaryotic cells. ATP-dependent proteases in E. coli fall into two classes. The first class requires the interaction of structurally separate proteases with an ATPase, whereas in the second class both the protease and ATPase are formed from regions of the same polypeptide chain. We have studied the structure of several of these protein degrading complexes in E. coli and have found a remarkable similarity in the architecture of these macromolecular assemblies.

The prototypical protease of the first class has as its proteolytic component ClpP, a 14 subunit (MW 21,500) complex arranged as two lOnm-diameter stacked rings of seven subunits each. ClpP can interact with either one of two ATPases, ClpA or ClpX, each with unique substrate specificity. ClpA has two ATP-binding sites per subunit (MW 84,000), and its subunits are arranged as a 13nm (diameter) hexameric ring (MW -500,000).

Type
Proteolysis: A Versatile Biological Control Mechanism
Information
Microscopy and Microanalysis , Volume 4 , Issue S2: Proceedings: Microscopy & Microanalysis '98, Microscopy Society of America 56th Annual Meeting, Microbeam Analysis Society 32nd Annual Meeting, Atlanta, Georgia July 12-16, 1998 , July 1998 , pp. 978 - 979
Copyright
Copyright © Microscopy Society of America

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References

1. Kessel, M. et al., J. Mol. Biol. (1995) 250: 587–594CrossRefGoogle Scholar

2. Kocsis, E. et al., Biophys. J (1996) pp. A60Google Scholar

3. Wang, J. et al., Cell (1997) 91: 447–456CrossRefGoogle Scholar

4. Kessel, M. et al., FEBS Lett (1996) 398: 274–278CrossRefGoogle Scholar

5. Peters, J. M., et al., J. Mol. Biol. (1993) 234: 932–937CrossRefGoogle Scholar