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J Biol Chem, Vol. 273, Issue 30, 18685-18688, July 24, 1998

COMMUNICATION
Localized Unfolding at the Junction of Three Ferritin Subunits
A MECHANISM FOR IRON RELEASE?

Hidenori TakagiDagger , Dashuang Shi, Ya Ha, Norma M. Allewell, and Elizabeth C. TheilDagger

From the Dagger  Department of Biochemistry, North Carolina State University, Raleigh, North Carolina 27695-7622 and the  Department of Biochemistry, University of Minnesota, St. Paul, Minnesota 55108

How and where iron exits from ferritin for cellular use is unknown. Twenty-four protein subunits create a cavity in ferritin where iron is concentrated >1011-fold as a mineral. Proline substitution for conserved leucine 134 (L134P) allowed normal assembly but increased iron exit rates. X-ray crystallography of H-L134P ferritin revealed localized unfolding at the 3-fold axis, also iron entry sites, consistent with shared use sites for iron exit and entry. The junction of three ferritin subunits appears to be a dynamic aperture with a "shutter" that cytoplasmic factors might open or close to regulate iron release in vivo.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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