Journal
CHEMISTRY & BIOLOGY
Volume 18, Issue 6, Pages 794-804Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2011.03.015
Keywords
-
Categories
Funding
- EU-SFMET [201640]
- EU Bio-NMR [261863]
- Italian MIUR-FIRB [PROTEOMICA-RBRN07BMCT]
- IMBB-FORTH
- University of Crete
- European Social Fund and national resources
Ask authors/readers for more resources
Human anamorsin was implicated in cytosolic iron-sulfur (Fe/S) protein biogenesis. Here, the structural and metal-binding properties of anamorsin and its interaction with Mia40, a well-known oxidoreductase involved in protein trapping in the mitochondrial intermembrane space (IMS), were characterized. We show that (1), anamorsin contains two structurally independent domains connected by an unfolded linker; (2), the C-terminal domain binds a [2Fe-2S] cluster through a previously unknown cysteine binding motif in Fe/S proteins; (3), Mia40 specifically introduces two disulfide bonds in a twin CX(2)C motif of the C-terminal domain; (4), anamorsin and Mia40 interact through an intermolecular disulfide-bonded intermediate; and (5), anamorsin is imported into mitochondria. Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available