Abstract
Prohibitins (PHB) are highly conserved and ubiquitously expressed proteins in eukaryotic cells. The prohibitin family exist in two isoforms PHB1 (also known as BAP32) and PHB2 ( also known as BAP37 and REA). The PHB1 and PHB2 together form large ring shaped complexes in the inner‐mitochondrial membrane, although PHB has also been reported to be localized in the nucleus and the cell membrane. PHB proteins have been implicated in mitochondrial biogenesis as well as scaffold for mitochondrial proteins. Details on the structure and function of PHB1 are still unclear. To better understand the functional mechanisms of PHB1 , we conducted biophysical analysis on recombinant human PHB1 and a truncated form of PHB1 (aa 52‐197). Our results show that PHB1 variants can form oligomers, and that varying salt concentration can modulate the polymerization of PHB1. Furthermore, addition of iron to PHB1 in solution affects the stability of the PHB1 oligomers. These data suggest that PHB1 could have diverse oligomeric forms depending on its local environmentGrant Funding Source: Supported by: Manitoba Health Research Council,
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
