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Science 5 January 1990:
Vol. 247. no. 4938, pp. 74 - 77
DOI: 10.1126/science.2294594
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Articles

Science, Vol 247, Issue 4938, 74-77
Copyright © 1990 by American Association for the Advancement of Science

articles

Derepression of ferritin messenger RNA translation by hemin in vitro

JJ Lin, S Daniels-McQueen, MM Patino, L Gaffield, WE Walden, and RE Thach

Department of Biology, Washington University, St. Louis, MO 63130.

Incubation of a 90-kilodalton ferritin repressor protein (FRP), either free or complexed with an L-ferritin transcript, with hemin or Co3+-protoporphyrin IX prevented subsequent repression of ferritin synthesis in a wheat germ extract. Neither FeCl3 in combinations with H2O2, nor Fe3+ or Fe2+ chelated with EDTA, nor Zn2+-protoporphyrin IX, nor protoporphyrin IX caused significant inactivation of FRP. FRP that had been inactivated by hemin remained chemically intact, as revealed by SDS-polyacrylamide gel electrophoresis. Inclusion of chelators of iron or free radical scavengers did not alter the inactivation produced by hemin. These and other results indicate that hemin derepresses ferritin synthesis in vitro.


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