Abstract
Here, we review the diverse roles and functions of AAA+ protease complexes in protein homeostasis, control of stress response and cellular development pathways by regulatory and general proteolysis in the Gram-positive model organism Bacillus subtilis. We discuss in detail the intricate involvement of AAA+ protein complexes in controlling sporulation, the heat shock response and the role of adaptor proteins in these processes. The investigation of these protein complexes and their adaptor proteins has revealed their relevance for Gram-positive pathogens and their potential as targets for new antibiotics.
Highlights
Bacteria, like all living organisms must rapidly sense and adapt to drastic changes in their environment (Roux, 1914)
Alteration of substrate specificity or structural changes that result in a more accessible axial pore of the protease complex were discussed. These hypotheses were based on the observation that the cyclomarin binding region at the N-terminal domain of ClpC1 overlaps with the site corresponding to the MecA interaction site on the NTD of B. subtilis ClpC (Schmitt et al, 2011; Vasudevan et al, 2013; Culp and Wright, 2016; Malik and Brötz-Oesterhelt, 2017)
MecA was first described in B. subtilis as an adaptor protein for specific substrate recognition by ClpCP (Turgay et al, 1998). These examples support the notion that B. subtilis is a useful model organism for the study of the role of AAA+ protease complexes
Summary
Like all living organisms must rapidly sense and adapt to drastic changes in their environment (Roux, 1914). The unifying activity of the AAA+ family proteins participating in protein quality control systems is to unfold proteins facilitated by ATP hydrolysis-dependent translocation using specific loops in the pore formed by the AAA+ hexameric ring structure. This unfoldase activity is central for the function of AAA+ proteins in protein disaggregation and degradation (Horwich et al, 1999; Sauer and Baker, 2011). Adaptor proteins play an important role in controlling and facilitating the various and different regulatory and general functions of their cognate AAA+ proteins (Kirstein et al, 2009b; Sauer and Baker, 2011; Battesti and Gottesman, 2013; Joshi and Chien, 2016; Kuhlmann and Chien, 2017)
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