Molecular characterization of a heme-binding chaperone - CHAPHEME

Abstract:

Protein folding is crucial for proper function, and chaperones play a key role in preventing protein aggregation and facilitating folding. Within the bacterial envelope, the periplasmic space is a site of passage and activity for many proteins, whose proper folding depends on a network of chaperones essential for maintaining proteostasis. Unexpectedly, we have discovered that one of the periplasmic chaperones of E. coli, though already well studied, binds to a heme. This observation, based on solid preliminary results, raises new questions about the role of a holo-chaperone form in periplasmic proteostasis. To this end, we have formed a multidisciplinary consortium bringing together microbiologists from the LCB, biochemists from the BIAM, and physico-chemists from the BIP.