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J. Biol. Chem., Vol. 277, Issue 16, 13367-13370, April 19, 2002
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,¶, and
From the The product of the miaB gene, MiaB,
from Escherichia coli participates in the methylthiolation
of the adenosine 37 residue during modification of tRNAs that read
codons beginning with uridine. A His-tagged version of MiaB has been
overproduced and purified to homogeneity. Gel electrophoresis and size
exclusion chromatography revealed that MiaB protein is a monomer. As
isolated MiaB contains both iron and sulfide and an apoprotein form can
chelate as much as 2.5-3 iron and 3-3.5 sulfur atoms per
polypeptide chain. UV-visible and EPR spectroscopy of MiaB indicate the
presence of a [4Fe-4S] cluster under reducing and anaerobic
conditions, whereas [2Fe-2S] and [3Fe-4S] forms are generated under
aerobic conditions. Preliminary site-directed mutagenesis studies
suggest that Cys157, Cys161, and
Cys164 are involved in iron chelation and that the
cluster is essential for activity. Together with the previously shown
requirement of S-adenosylmethionine (AdoMet) for the
methylthiolation reaction, the finding that MiaB is an iron-sulfur
protein suggests that it belongs to a superfamily of enzymes that uses
[Fe-S] centers and AdoMet to initiate radical catalysis. MiaB is the
first and only tRNA modification enzyme known to contain an Fe-S cluster.
Laboratoire de Chimie et Biochimie des
Centres Rédox Biologiques, Département de Biologie
Moléculaire et Structurale-Chimie Biologie, UMR 5047 Commissariat à l'Energie Atomique
(CEA)/CNRS/Université Joseph Fourier,
CEA-Grenoble 17 avenue des Martyrs, 38054 Grenoble Cedex 09, France and
the § Department of Molecular Biology, Umeå
University, S-901 87 Umeå, Sweden
To whom correspondence may be addressed. Fax: 0033438789124;
E-mail: mohamed.atta@cea.fr.
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