Hsp10 a chaperone by itself?

For a long time Hsp10 has been believed to be just a helper, a co-chaperone. Recent evidence suggest that it has also chaperone activity in absence of Hsp60; it inhibits the aggregation of the Alzheimer's peptide and supports the folding of malate dehydrogenase. We are currently solving the structure of Hsp10 and elaborating the mechanism of how Hsp10 functions.

Hsp10 inhibits Ab aggregation

The Alzheimer's peptide aggregates over time and forms amyloid fibrils. Hsp10 inhibits this toxic event and may play a role in Alzheimer's disease.

Hsp10 supports folding of MDH

Malate dehydrogenase is an obligate substrate of Hsp60. Hsp10 in absence of Hsp60 can also support the folding of MDH.

Cryo-EM structure of Hsp10

The structure of Hsp10 was solved in the apo form by cryo-electron microscopy.