Catalase dismutates hydrogen peroxide and this is important for the fungal antioxidant response. Large-subunit catalases (LSC) have a carboxyl-terminal domain (C-terminal domain) whose structure is similar to DJ-1 protein. DJ-1 is a chaperone that inhibits aggregation of α-synuclein in the human brain. We have demostrate that C-terminal domain has also chaperone activity.
Like other chaperones, LSCs are abundant proteins that are induced under stress conditions and during cell differentiation in different microorganisms. Here we document that the C-terminal domain of LSCs assist other proteins to preserve their active conformation under denaturing conditions.  The C-terminal domain of CAT-3 (TDC3) also protected the catalitic domain of CAT-3 (C3DTD) and the bovine liver catalase (small subunit catalase) from heat denaturation. The chaperone activity of CAT-3 or the TDC3 increased survival of E. coli under different stress conditions like HSP31 chaperone, whereas the C3DTD did not.

Chaperone activity of large—subunit catalases

LatinXChem

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.