TY - JOUR
T1 - Protein Unfolding and Degradation by the CLP Family of Proteases
AU - Kessel, Martin
AU - Beuron, Fabienne
AU - Booy, Frank
AU - Kocsis, Eva
AU - Maurizi, Michael
AU - Steven, Alasdair
N1 - Publisher Copyright:
© 1998 Microscopy Society of America.
PY - 1998/7/1
Y1 - 1998/7/1
N2 - 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).
AB - 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).
UR - http://www.scopus.com/inward/record.url?scp=85180066576&partnerID=8YFLogxK
U2 - 10.1017/S1431927600025010
DO - 10.1017/S1431927600025010
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AN - SCOPUS:85180066576
SN - 1431-9276
VL - 4
SP - 978
EP - 979
JO - Microscopy and Microanalysis
JF - Microscopy and Microanalysis
ER -