Loop mutations affect ferritin solubility causing non-native aggregation of subunits or precipitation of fully assembled polymers.

Abstract excerpt

As a consequence of elevated expression rates, the intracellular aggregation of polypeptide chains is commonly observed in E. coli. Although wild-type human ferritin, a polymeric iron storage protein, accumulates in the soluble form at high level in the bacterial cytoplasmic fraction, some amino acid substitutions in an exposed loop direct the synthesis of a highly insoluble product. We found that two mechanisms...

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