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Papers In Press, published online ahead of print March 6, 2002
DBMS/CB, CEA/Grenoble, Grenoble 38054
Corresponding Author: mohamed.atta{at}cea.fr
The product of the miaB gene, MiaB, from Escherichia coli participates to the methylthiolation of the adenosine-37 residue during modification of tRNAs that read codons beginning with uridine. An 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 to 3 Fe and 3 to 3.5 S per polypeptide chain. UV-visible and EPR spectroscopy of MiaB indicate the presence of a [4Fe-4S] cluster under reducing and anaerobic conditions, whereas [2Fe2S] and [3Fe4S] forms are generated under aerobic conditions. Preliminary site-directed mutagenesis studies suggest that Cys 157, Cys 161, Cys 164 are involved in Fe 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.
J. Biol. Chem, 10.1074/jbc.C100609200
Submitted on October 18, 2001
Revised on March 4, 2002
Accepted on March 5, 2002
Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein
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