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Protein Science (2007), 16:644-653. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Inherent chaperone-like activity of aspartic proteases reveals a distant evolutionary relation to double-{psi} barrel domains of AAA-ATPases

Michael Hulko, Andrei N. Lupas, and Jörg Martin

Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, D-72076 Tübingen, Germany

(RECEIVED August 2, 2006; FINAL REVISION January 10, 2007; ACCEPTED January 14, 2007)

Chaperones and proteases share the ability to interact with unfolded proteins. Here we show that enzymatically inactive forms of the aspartic proteases HIV-1 protease and pepsin have inherent chaperone-like activity and can prevent the aggregation of denatured substrate proteins. In contrast to proteolysis, which requires dimeric enzymes, chaperone-like activity could be observed also with monomeric domains. The involvement of the active site cleft in the chaperone-like function was demonstrated by the inhibitory effect of peptide substrate inhibitors. The high structural similarity between aspartic proteases and the N-terminal double-{psi} barrels of Cdc48-like proteins, which are involved in the unfolding and dissociation of proteins, suggests that they share a common ancestor. The latent chaperone-like activity in aspartic proteases can be seen as a relic that has further evolved to serve substrate binding in the context of proteolytic activity.

Keywords: aspartic proteases; chaperones; double-{psi} barrel; AAA-ATPase; protein evolution


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