Related Experiment Video
Updated: Jun 14, 2025

Fractionation for Resolution of Soluble and Insoluble Huntingtin Species
Published on: February 27, 2018
Two novel DnaJ chaperone proteins CG5001 and P58IPK regulate the pathogenicity of Huntington's disease related
Ankita Deo1, Rishita Ghosh2, Snehal Ahire1
1Department of Biotechnology, Savitribai Phule Pune University, Ganeshkhind, Pune, 411007, India.
Abstract:
Huntington's disease (HD) is a rare neurodegenerative disease caused due to aggregation of Huntingtin (HTT) protein. This study involves the cloning of 40 DnaJ chaperones from Drosophila, and overexpressing them in yeasts and fly models of HD. Accordingly, DnaJ chaperones were catalogued as enhancers or suppressors based on their growth phenotypes and aggregation properties. 2 of the chaperones that came up as targets were CG5001 and P58IPK. Protein aggregation and slow growth phenotype was rescued in yeasts, S2 cells, and Drosophila transgenic lines of HTT103Q with these overexpressed chaperones. Since DnaJ chaperones have protein sequence similarity across species, they can be used as possible tools to combat the effects of neurodegenerative diseases.
More Related Videos
10:52Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System
Published on: December 10, 2021
11:22Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
Published on: June 27, 2018
Related Concept Videos
Hedgehog Signaling Pathway
Molecular Chaperones and Protein Folding
The...
Regulation of Nuclear Protein Sorting
Abnormal Proliferation
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....