PMID:11997471
| Citation |
Mihara, H, Kato, S, Lacourciere, GM, Stadtman, TC, Kennedy, RA, Kurihara, T, Tokumoto, U, Takahashi, Y and Esaki, N (2002) The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H. Proc. Natl. Acad. Sci. U.S.A. 99:6679-83 |
|---|---|
| Abstract |
Three NifS-like proteins, IscS, CSD, and CsdB, from Escherichia coli catalyze the removal of sulfur and selenium from L-cysteine and L-selenocysteine, respectively, to form L-alanine. These enzymes are proposed to function as sulfur-delivery proteins for iron-sulfur cluster, thiamin, 4-thiouridine, biotin, and molybdopterin. Recently, it was reported that selenium mobilized from free selenocysteine is incorporated specifically into a selenoprotein and tRNA in vivo, supporting the involvement of the NifS-like proteins in selenium metabolism. We here report evidence that a strain lacking IscS is incapable of synthesizing 5-methylaminomethyl-2-selenouridine and its precursor 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA, suggesting that the sulfur atom released from L-cysteine by the action of IscS is incorporated into mnm(5)s(2)U. In contrast, neither CSD nor CsdB was essential for production of mnm(5)s(2)U and 5-methylaminomethyl-2-selenouridine. The lack of IscS also caused a significant loss of the selenium-containing polypeptide of formate dehydrogenase H. Together, these results suggest a dual function of IscS in sulfur and selenium metabolism. |
| Links |
PubMed PMC124462 Online version:10.1073/pnas.102176099 |
| Keywords |
Carbon-Sulfur Lyases/genetics; Carbon-Sulfur Lyases/physiology; Escherichia coli/enzymology; Escherichia coli/genetics; Formate Dehydrogenases/biosynthesis; Hydrogenase/biosynthesis; Multienzyme Complexes/biosynthesis; Mutagenesis; Organoselenium Compounds; RNA, Transfer/biosynthesis; Selenocysteine/metabolism; Thiouridine/analogs & derivatives; Thiouridine/metabolism; Uridine/analogs & derivatives; Uridine/biosynthesis |
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