ORCID Profile
0000-0002-8959-492X
Current Organisations
Max Planck Unit for the Science of Pathogens
,
Leibniz Universitat Hannover
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Publications
AAA+ proteins and substrate recognition, it all depends on their partner in crime
Publisher: Wiley
Date: 14-08-2002
DOI: 10.1016/S0014-5793(02)03179-4
Abstract: Members of the AAA+ superfamily have been identified in all organisms studied to date. They are involved in a wide range of cellular events. In bacteria, representatives of this superfamily are involved in functions as erse as transcription and protein degradation and play an important role in the protein quality control network. Often they employ a common mechanism to mediate an ATP-dependent unfolding/disassembly of protein-protein or DNA-protein complexes. In an increasing number of ex les it appears that the activities of these AAA+ proteins may be modulated by a group of otherwise unrelated proteins, called adaptor proteins. These usually small proteins specifically modify the substrate recognition of their AAA+ partner protein. The occurrence of such adaptor proteins are widespread representatives have been identified not only in Escherichia coli but also in Bacillus subtilis, not to mention yeast and other eukaryotic organisms. Interestingly, from the currently known ex les, it appears that the N domain of AAA+ proteins (the most ergent region of the protein within the family) provides a common platform for the recognition of these erse adaptor proteins. Finally, the use of adaptor proteins to modulate AAA+ activity is, in some cases, an elegant way to redirect the activity of an AAA+ protein towards a particular substrate without necessarily affecting other activities of that AAA+ protein while, in other cases, the adaptor protein triggers a complete switch in AAA+ activity.
Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases
Publisher: Springer Science and Business Media LLC
Date: 08-2009
DOI: 10.1038/NRMICRO2185
Abstract: Members of the AAA+ protein superfamily contribute to many erse aspects of protein homeostasis in prokaryotic cells. As a fundamental component of numerous proteolytic machines in bacteria, AAA+ proteins play a crucial part not only in general protein quality control but also in the regulation of developmental programmes, through the controlled turnover of key proteins such as transcription factors. To manage these many, varied tasks, Hsp100/Clp and AAA+ proteases use specific adaptor proteins to enhance or expand the substrate recognition abilities of their cognate protease. Here, we review our current knowledge of the modulation of bacterial AAA+ proteases by these cellular arbitrators.
Dysregulating ClpP: From Antibiotics to Anticancer?
Publisher: Elsevier BV
Date: 08-2018
DOI: 10.1016/J.CHEMBIOL.2018.08.002
Abstract: In this issue of Cell Chemical Biology, Wong et al. (2018) identify several dysregulators of a key mitochondrial protease: casein lytic protease P (ClpP). These dysregulators were found to trigger programmed cell death and may offer fresh avenues for the development of novel cancer therapeutics.
MecA, an adaptor protein necessary for ClpC chaperone activity
Publisher: Proceedings of the National Academy of Sciences
Date: 21-02-2003
Abstract: ClpC of Bacillus subtilis is an ATP-dependent HSP100/Clp protein involved in general stress survival. A complex of ClpC with the protease ClpP and the adaptor protein MecA also controls competence development by regulated proteolysis of the transcription factor ComK. We investigated the in vitro chaperone activity of ClpC and found that the presence of MecA was crucial for the major chaperone activities of ClpC. In particular, MecA enabled ClpC to solubilize and refold aggregated proteins. Finally, in the presence of ClpP, MecA allowed the ClpC-dependent degradation of unfolded or heat-aggregated proteins. This study demonstrates that adaptor proteins like MecA through interaction with their cognate ClpC proteins can have a dual role in the protein quality-control network by rescuing, or together with ClpP, by degrading, aggregated proteins. MecA can thereby coordinate substrate targeting with ClpC activation, adding another layer to the regulation of HSP100/Clp protein activity.
The tyrosine kinase McsB is a regulated adaptor protein for ClpCP
Publisher: Wiley
Date: 22-03-2007
Conserved residues in the N‐domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding
Publisher: Wiley
Date: 14-02-2008
DOI: 10.1111/J.1742-4658.2008.06304.X
Abstract: 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 peptide‐binding groove within the N‐domain of ClpA, specifically compromised the ability of ClpA to unfold and degrade selected substrates but did not prevent substrate recognition, ClpS‐mediated substrate delivery or ClpP binding. In contrast, a highly conserved tyrosine residue lining the central pore of the ClpA hexamer was essential for the degradation of all substrate types analysed, including both folded and unstructured proteins. Taken together, these data suggest that ClpA utilizes two structural elements, one in the N‐domain and the other in the pore of the hexamer, both of which are required for efficient unfolding of some protein substrates.
Adaptor protein controlled oligomerization activates the AAA+ protein ClpC
Publisher: Wiley
Date: 09-03-2006
Exploring a potential Achilles heel of Mycobacterium tuberculosis: defining the ClpC1 interactome
Publisher: Wiley
Date: 17-06-2020
DOI: 10.1111/FEBS.15430
Broad yet high substrate specificity: the challenge of AAA+ proteins
Publisher: Elsevier BV
Date: 04-2004
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