Researchers at the S. N. Bose National Centre for Basic Sciences (SNBNCBS) highlighted protein p47’s unexpected ability to act as a “mechanical chaperone.”
About P-47 Protein:
It is a cofactor protein usually known as a helper for the cellular machine p97 (it is a powerhouse involved in moving and degrading proteins).
It was long thought to be just an assistant known primarily for its role in protein trafficking, degradation, and membrane fusion.
Highlight of the study:
It is revealed that p47 can enhance the mechanical efficiency of protein extraction from the Endoplasmic Reticulum (ER) lumen into the cytoplasm.
P47 stabilizes polypeptides under stress and guiding them through narrow pores, reduces the risk of misfolding and improves the success of protein translocation.
This finding represents the first direct, single-molecule evidence that cofactors like p47 possess autonomous, force-dependent chaperone-like activity.
It is found that p47 is not just a passive helper for p97, it can directly stabilize proteins under force, effectively acting as a “mechanical chaperone”.
The findings suggest that targeting mechanical cofactors like p47 could lead to novel therapeutic strategies for diseases linked to protein instability.
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