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Originally published In Press as doi:10.1074/jbc.C000279200 on June 2, 2000

J. Biol. Chem., Vol. 275, Issue 30, 22615-22618, July 28, 2000
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ACCELERATED PUBLICATION
Transfer of Iron-Sulfur Cluster from NifU to Apoferredoxin*

Kazuaki Nishio and Masato NakaiDagger

From the Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan

Iron-sulfur proteins are present in a wide variety of organisms and are known to play important physiological roles, not only in electron transfer and metabolic reactions, but also in transcriptional regulation. However, little is known about how iron-sulfur clusters themselves are synthesized and assembled within polypeptides. Here we show that a [2Fe-2S] cluster-containing NifU of cyanobacterium Synechocystis PCC6803, SyNifU, possesses the ability to deliver its [2Fe-2S] cluster to an apoferredoxin without the aid of other proteinaceous or nonproteinaceous factor(s). Upon delivery the reconstituted holoferredoxin regained electron transfer ability. The [2Fe-2S] cluster contained within SyNifU was labile upon exposure to the iron-chelating reagent EDTA, suggesting that the iron-sulfur cluster is abnormally exposed to solvent. We propose that NifU serves as a scaffold for iron-sulfur cluster assembly and functions as a mediator for iron-sulfur cluster delivery.

* This work was supported in part by a grant-in-aid for scientific research from the Ministry of Education, Science and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 81-6-6879-8612; Fax: 81-6-6879-8613; E-mail: nakai@protein.osaka-u.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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