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Journal of Biochemistry Advance Access published online on June 1, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm120
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© 2007 The Japanese Biochemical Society

The Cooperative Role of OsCnfU-1A Domain I and Domain II in the Iron-Sulfur Cluster Transfer Process as Revealed by NMR

Tomohide Saioa, Hiroyuki Kumetaa, Kenji Oguraa, Masashi Yokochia, Munehiko Asayamab, Shizue Katohc, Etsuko Katohc, Keizo Teshimad and Fuyuhiko Inagakia,*

aLaboratory of Structural Biology, Graduate School of Pharmaceutical Science, Hokkaido University, Sapporo, Hokkaido, Japan.
bLaboratory of Molecular Genetics, College of Agriculture, Ibaraki University, Ami 3-21-1, Ibaraki 300-0393, Japan
cBiochemistry Department, National Institute of Agrobiological Science, Tsukuba, Ibaraki 305-8602, Japan
dFaculty of Integrated Arts and Sciences, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima 739-8521, Japan

Corresponding Author: Fuyuhiko Inagaki: Laboratory of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita 21 jo, 11 chome, Kita-ku, Sapporo, Hokkaido, Japan. Tel: +81-11-706-9011, Fax: +81-11-706-9012, E-mail: finagaki{at}pharm.hokudai.ac.jp

Received March 7, 2007; Accepted May 6, 2007


  Abstract

OsCnfU-1A is a chloroplast-type Nfu-like protein that consists of tandem repeats sharing high sequence homology. Domain I of this protein, but not domain II, has a C-X-X-C motif that is thought to assemble an iron-sulfur cluster. Herein we report the solution structure of OsCnfU-1A domain I (73-153). Although OsCnfU-1A domain I is structurally similar to OsCnfU-1A domain II (154-226), the electrostatic surface potential of the 2 domains differs. Domain I has an acidic surface, whereas that of domain II is predominantly basic. Chemical shift perturbation studies on OsCnfU-1A domain I and domain II with ferredoxin revealed negligible chemical shift changes in domain I, whereas much larger chemical shift changes were observed in domain II. The residues with larger chemical shift changes were located on the basic surface of domain II. Considering that ferredoxin is predominantly negatively charged, we propose the following hypothesis: First, an iron-sulfur cluster is assembled on domain I. Next, domain II interacts with the ferredoxin, thus tethering domain I close to the ferredoxin. Finally, domain I transfers the iron-sulfur cluster to the ferredoxin. Thus, domain II facilitates the efficient transfer of the iron-sulfur cluster from domain I to the ferredoxin.

Key Words: cell-free protein synthesis, Fe-S cluster, Nfu-like protein, NMR structure, Oryza sativa


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