Context and Background

• Researchers from the S.N. Bose National Centre for Basic Sciences (SNBNCBS) in Kolkata have discovered a novel, force-dependent, chaperone-like function of the p47 protein. This revelation offers a transformative understanding of how cells handle protein folding, stability, and translocation under mechanical stress — a vital function for cellular survival and disease prevention.
• This is the first single-molecule experimental evidence that a cofactor protein like p47 can act autonomously as a mechanical chaperone.

What is p47 Protein?

p47 was previously thought to be only a passive assistant to the p97 protein, helping it in pulling proteins out of the endoplasmic reticulum (ER) for degradation or recycling.

New Findings: The Mechanical Chaperone Role

• p47 enhances the mechanical efficiency of extracting proteins from the ER lumen into the cytoplasm.
• It stabilizes proteins (polypeptides) that are being translocated under force.
• p47 reduces the chances of protein misfolding during movement through narrow cellular channels.
• It acts independently, not just as a co-factor to p97 but as an autonomous mechanical chaperone.

This reshapes our understanding of intracellular protein quality control mechanisms.

Why Is This Discovery Important?

The folding, unfolding, and movement of proteins inside the cell are tightly regulated, as improper folding can lead to neurodegenerative diseases, cancers, and metabolic disorders.

• Proteins that misfold due to stress or mechanical strain can lead to protein aggregation — a hallmark of diseases like Alzheimer’s, Parkinson’s, and ALS.
• p47’s ability to stabilize polypeptides under such mechanical strain presents a new target for therapy and biotechnology.

Implications for Biotechnology and Medicine

About the S.N. Bose National Centre for Basic Sciences (SNBNCBS)