TAILIEUCHUNG - Báo cáo khoa học: Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding

Protein degradation in the cytosol ofEscherichia coliis carried out by a variety of different proteolytic machines, including ClpAP. The ClpA com-ponent is a hexameric AAA+ (ATPase associated with various cellular activities) chaperone that utilizes the energy of ATP to control substrate recognition and unfolding. | ễFEBS Journal Conserved residues in the N-domain of the AAA chaperone ClpA regulate substrate recognition and unfolding Annette H. Erbse1 Judith N. Wagner1 Kaye N. Truscott2 Sukhdeep K. Spall2 Janine Kirstein1 3 Kornelius Zeth4 Kursad Turgay1 3 Axel Mogk1 Bernd Bukau1 and David A. Dougan1 2 1 Zentrum fur Molekulare Biologie Heidelberg Universitat Heidelberg Heidelberg Germany 2 Department of Biochemistry La Trobe University Melbourne Australia 3 Institut fur Biologie Freie Universitat Berlin Berlin Germany 4 MPI fur Entwicklungsbiologie Tubingen Germany Keywords AAA binding ClpA SsrA unfolding Correspondence D. A. Dougan Department of Biochemistry La Trobe University Melbourne 3086 Australia Fax 61 3 9479 2467 Tel 61 3 9479 3276 E-mail B. Bukau Zentrum fur Molekulare Biologie Heidelberg Universitat Heidelberg INF 282 Heidelberg D-69120 Germany Fax 49 6221 54 5894 Tel 49 6221 54 6795 E-mail bukau@ These authors contributed equally to this work Received 22 November 2007 revised 10 January 2008 accepted 14 January 2008 doi Protein degradation in the cytosol of Escherichia coli is carried out by a variety of different proteolytic machines including ClpAP. The ClpA component is a hexameric AAA ATPase associated with various cellular activities chaperone that utilizes the energy of ATP to control substrate recognition and unfolding. The precise role of the N-domains of ClpA in this process however remains elusive. Here we have analysed the role of five highly conserved basic residues in the N-domain of ClpA by monitoring the binding unfolding and degradation of several different substrates including short unstructured peptides tagged and untagged proteins. Interestingly mutation of three of these basic residues within the N-domain of ClpA H94 R86 and R100 did not alter substrate degradation. In contrast mutation of two conserved arginine residues R90 and R131 flanking a putative .

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