The molecular chaperone RavA forms amyloids at low pH and elevated temperatures.
Walid Houry’s group together with Simon Sharpe’s group and others at the University of Toronto unexpectedly discovered that a bacterial chaperone forms amyloids under physiologically-relevant acidic conditions at elevated temperatures. The work has been accepted in Structure. Experimental and theoretical studies revealed that the folded core of one of the domains of the chaperones is amyloidogenic and is protected by its N-terminal loop. While molecular chaperones are thought to be the guardians of the cell against misfolded proteins, this is the first instance to our knowledge where a chaperone is found to ‘behave badly’ and misfold into an amyloidogenic state that could be detrimental to the cell.
