The heat shock protein AgsA has been investigated by
biochemistry researchers to help understand how it is able to promote survival when lethal temperature levels are reached.
A study conducted at the University of Tokushima in Japan and published in the latest issue of BMC
Biochemistry explains that different substances aggregate to a variety of degrees in the presence of AgsA and at varying temperatures.
Insulin aggregates at 25 degrees C, but citrate synthase, malate dehydrogenase and denatured lysozyme all do not.
"Temperature-controlled gel filtration chromatography showed that purified AgsA could maintain large oligomeric complexes up to 50 degrees C," the scientists add.
According to the researchers, the regions of AgsA necessary for chaperone activity are located in different places; insulin chaperone activity is regulated inside the oligomeric complex, while lysozyme chaperone activity occurs at the surface.
BMC
Biochemistry is open access and addresses topics including supramolecular complexes, enzymes, proteins and metabolic pathways among its broad-ranging remit.
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