Science, Technology and Engineering

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

• 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)