ClpL Chaperone as a Possible Component of the Disaggregase Activity of Limosilactobacillus fermentum U-21.

ABSTRACT: The L. fermentum U-21 strain, known for secreting chaperones into the extracellular milieu, emerges as a promising candidate for the development of novel therapeutics termed disaggregases for Parkinson's disease. Our study focuses on characterizing the secreted protein encoded by the C0965_000195 locus in the genome of this strain. Through sequence analysis and structural predictions, the protein encoded by C0965_000195 is identified as ClpL, homologs of which are known for their chaperone functions. The chaperone activity of ClpL from L. fermentum U-21 is investigated in vivo by assessing the refolding of luciferases with varying thermostabilities from Aliivibrio fischeri and Photorhabdus luminescens within Escherichia coli cells. The results indi

SUBMITTER: Al Ebrahim RN 

PROVIDER: S-EPMC11351774 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature