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Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria
Lee, Changhan,Franke, Kamila B.,Kamal, Shady Mansour,Kim, Hyunhee,Lunsdorf, Heinrich,Jager, Jasmin,Nimtz, Manfred,Trč,ek, Janja,Jansch, Lothar,Bukau, Bernd,Mogk, Axel,Romling, Ute National Academy of Sciences 2018 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.115 No.2
<P><B>Significance</B></P><P>Severe heat stress causes massive protein loss by aggregation ultimately causing cell death. Cellular survival relies on protein disaggregation mediated by the Hsp70-ClpB (Hsp100) bichaperone system in most bacteria. <I>Pseudomonas aeruginosa</I> additionally codes for two stand-alone ClpG disaggregases, which had been acquired by horizontal gene transfer by the species and most abundant clone C strains, respectively. These ClpG disaggregases largely contribute to the resolution of protein aggregates to confer superior heat tolerance partially replacing the DnaK-ClpB system.</P><P>AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent ClpG disaggregase homologs acquired through horizontal gene transfer by the species <I>Pseudomonas aeruginosa</I> and subsequently abundant <I>P. aeruginosa</I> clone C. ClpG exhibits high, stand-alone disaggregation potential without involving any partner cooperation. Specific molecular features, including high basal ATPase activity, a unique aggregate binding domain, and almost exclusive expression in stationary phase distinguish ClpG from other AAA+ disaggregases. Consequently, ClpG largely contributes to heat tolerance of <I>P. aeruginosa</I> primarily in stationary phase and boosts heat resistance 100-fold when expressed in <I>Escherichia coli</I>. This qualifies ClpG as a potential persistence and virulence factor in <I>P. aeruginosa</I>.</P>