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A newly characterized protein HmuF serves a dual function in iron sequestration and transport

Jan. 1, 2024

Iron is an essential element for cell growth often in short supply for fast-growing cells. Virulent bacteria will use multiple pathways to uptake high amounts of environmental iron. If not properly sequestered, high levels of cytosolic iron are toxic and need to be trafficked and sequestered by proteins to reduce their toxicity without sacrificing potential growth.

In this work, McGregor et al. characterize a new protein (HmuF) from Fusobacterium nucleatum, a bacteria involved in oral disease. HmuF plays double duty in sequestering free iron within the cell, and aids in the breakdown of the iron-binding molecule anaerobilin. These actions allow the bacterium to utilize more toxic iron sources providing an edge in colonizing iron-poor environments. Targeting HmuF provides a new opportunity to disrupt colonization and may allow for a new method of treatment for periodiontal disease.

PDB: 8G64

Reference: McGregor, Alexandra K., et al. "A new member of the flavodoxin-superfamily from Fusobacterium nucleatum that functions in heme-trafficking and reduction of anaerobilin." Journal of Biological Chemistry (2023): 104902.