Chaperone-assisted protein remodeling enables microbial survival under extreme composting heat. (IMAGE)
Caption
Chaperone-assisted protein remodeling enables microbial survival under extreme composting heat. During hyperthermophilic composting, microbial communities endure temperatures approaching 87 °C by activating a network of heat shock proteins that stabilize enzymes and maintain cellular functions. The schematic illustrates how conventional thermophiles (left) transition to hyperthermophiles (right), where dnaJ, dnaK, and groEL work in sequence to recognize, refold, and protect misfolded proteins such as CTPase. Enhanced hydrogen-bond networks, ATP-driven chaperone cycles, and coordinated metabolic regulation collectively ensure thermal stability, allowing microbes to sustain energy production and biodegradation efficiency at 360 K.
Credit
Environmental Science and Ecotechnology
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