The low complexity linker of DNAJB6b is key to its anti-amyloid function.

ABSTRACT: Neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases, are associated with the formation of amyloid fibrils. The DNAJB6b (JB6) chaperone greatly inhibits the disease-related self-assembly of amyloid peptides in an ATP-independent manner. The molecular basis of this process is, however, not understood. Here, we studied the low complexity linker between the N- and C-terminal domains of JB6 as an isolated 110 amino acid residue construct, to get a better understanding of the role of the composition of the intact protein. We investigate the structure and aggregation behaviour of the linker and its anti-amyloid activity in comparison with the full-length chaperone. We find that the linker contains ca. 45% α-helix and 20% β-sheet and is in itself an amyloid-like peptide that

SUBMITTER: Merkelis T 

PROVIDER: S-EPMC12722041 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature