Tandem repeats of highly bioluminescent NanoLuc are refolded noncanonically by the Hsp70 machinery.

ABSTRACT: Chaperones are a large family of proteins crucial for maintaining cellular protein homeostasis. One such chaperone is the 70 kDa heat shock protein (Hsp70), which plays a crucial role in protein (re)folding, stability, functionality, and translocation. While the key events in the Hsp70 chaperone cycle are well established, a relatively small number of distinct substrates were repetitively investigated. This is despite Hsp70 engaging with a plethora of cellular proteins of various structural properties and folding pathways. Here we analyzed novel Hsp70 substrates, based on tandem repeats of NanoLuc (Nluc), a small and highly bioluminescent protein with unique structural characteristics. In previous mechanical unfolding and refolding studies, we have identified interesting misfolding propens

SUBMITTER: Apostolidou D 

PROVIDER: S-EPMC10804678 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature