Protein Unfolding and Degradation by the CLP Family of Proteases

Martin Kessel, Fabienne Beuron, Frank Booy, Eva Kocsis, Michael Maurizi, Alasdair Steven

Research output: Contribution to journalArticlepeer-review

Abstract

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).

Original languageEnglish
Pages (from-to)978-979
Number of pages2
JournalMicroscopy and Microanalysis
Volume4
DOIs
StatePublished - 1 Jul 1998
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 1998 Microscopy Society of America.

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