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Papers In Press, published online ahead of print May 24, 2003
DRDC/CB, CEA/GRENOBLE, Grenoble 38054
Corresponding Author: mohamed.atta{at}cea.fr
In Escherichia coli, the MiaB protein catalyzes the methylthiolation of N-6-isopentenyl adenosine in tRNAs, the last reaction step during biosynthesis of 2-methylthio-N-6-isopentenyl adenosine (ms2i6A-37). For the first time the thermophilic bacterium The rmotoga martima is shown here to contain such a MiaB tRNA-modifying enzyme, named MiaBTm, and to synthesize ms2i6A-37 as demonstrated by an analysis of modified nucleosides from tRNA hydrolysates. The corresponding gene, (TM0653), was identified by sequen ce similarity to the miaB gene of E. coli was cloned and expressed in E. coli. MiaBTm was purified to homogeneity and thoroughly characterized by biochemical and spectroscopic methods. It is a monomer of 443 residues with a molecular mass of 50710 kilodaltons. Its amino-acid sequence shares the CysXXXCysXXCys sequence with MiaB from E. coli as well as with biotin synthase and lipoate synthase. This sequence was shown to be essential for chelation of an iron-sulfur center and for activity in these enzymes. As isolated, MiaBTm contains both iron and sulfide and an apoprotein form can coordinate up to 4 Fe and 4 S atoms per polypeptide chain. UV-visible absorption, resonance Raman, variable-temperature magnetic circular dichroism and EPR spectroscopy of MiaB Tm indicate the presence of a [4Fe-4S]+2/+1 cluster under reducing and anaerobic conditions, whereas [3Fe-4S]+1 and [2Fe-2S]+2 forms are generated under aerobic conditions. The redox potential of the [4Fe-4S]+2/+1 transition is –495 ±10 mV (vs. the normal hydrogen electrode). Finally, the expression of MiaBTm from T. maritima in an E. coli mutant strain lacking functional miaB gene allowed production of ms2i6A-37. These results provide further information on the enzymes involved in methylthiolation of tRNAs.p
J. Biol. Chem, 10.1074/jbc.M301518200
Submitted on February 12, 2003
Revised on May 21, 2003
Accepted on May 24, 2003
MiaB protein from thermotoga maritima: characterization of an extremely thermophilic tRNA-methylthiotransferaseÏ
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