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Dougan & Truscott Laboratory
Department of Biochemistry
Research:
Substrate recognition
A detailed analysis of protease substrate specificity is central to our understanding of how chaperones and proteases compete for different substrates in vivo. We aim to determine the motifs in proteins recognised directly by the ATPase unfoldase of the AAA+ protease or through specific adaptors. This research incorporates an analysis of the natural target proteins of the AAA+ proteases in bacteria & mitochondria.
Recent publications
- Schuenemann VJ, Kralik SM, Albrecht R, Spall SK, Truscott KN, Dougan DA, Zeth K. (2009). Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS. EMBO Reports 10, 508-514.
- Erbse AH, Wagner JN, Truscott KN, Spall SK, Kirstein J, Zeth K, Turgay K, Mogk A, Bukau B, Dougan DA. (2008). Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. FEBS J. 275, 1400-10.
- Erbse A, Schmidt R, Bornemann T, Schneider-Mergener J, Mogk A, Zahn R, DOUGAN DA, Bukau B. (2006)
ClpS is an essential component of the N-end rule pathway in Escherichia coli. Nature 439, 753-6.
- Schlothauer T, Mogk A, DOUGAN DA, Bukau B, Turgay K. (2003) MecA, an adaptor protein necessary for ClpC chaperone activity. Proc. Natl. Acad. Sci. U S A. 100, 2306-11.
- DOUGAN DA, Reid BG, Horwich AL, Bukau B. (2002) ClpS, a substrate modulator of the ClpAP machine. Mol. Cell. 9, 673-83.
Collaborators
Bernd
Bukau (ZMBH, Heidelberg, Germany)
Bernard Guiard (CNRS Centre de
Genetique Moleculaire, Gif-sur-Yvette, France)
Kursad Turgay (Freie University Berlin, Germany)
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