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Journal of Bacteriology, April 2002, p. 1940-1946, Vol. 184, No. 7
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.7.1940-1946.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Selenium Is Mobilized In Vivo from Free Selenocysteine and Is Incorporated Specifically into Formate Dehydrogenase H and tRNA Nucleosides

Gerard M. Lacourciere*

Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892

Received 30 March 2001/ Accepted 3 December 2001

Selenophosphate synthetase (SPS), the selD gene product from Escherichia coli, catalyzes the biosynthesis of monoselenophosphate, AMP, and orthophosphate in a 1:1:1 ratio from selenide and ATP. It was recently demonstrated that selenium delivered from selenocysteine by an E. coli NifS-like protein could replace free selenide in the in vitro SPS assay for selenophosphate formation (G. M. Lacourciere, H. Mihara, T. Kurihara, N. Esaki, and T. C. Stadtman, J. Biol. Chem. 275:23769-23773, 2000). During growth of E. coli in the presence of 0.1 µM 75SeO32- and increasing amounts of L-selenocysteine, a concomitant decrease in 75Se incorporation into formate dehydrogenase H and nucleosides of bulk tRNA was observed. This is consistent with the mobilization of selenium from L-selenocysteine in vivo and its use in selenophosphate formation. The ability of E. coli to utilize selenocysteine as a selenium source for selenophosphate biosynthesis in vivo supports the participation of the NifS-like proteins in selenium metabolism.


* Mailing address: Laboratory of Biochemistry NHLBI, NIH 50 South Drive, Room 2126, Bethesda, MD 20892. Phone: (301) 435-8354. Fax: (301) 496-0599. E-mail: lacourcg{at}nhlbi.nih.gov.


Journal of Bacteriology, April 2002, p. 1940-1946, Vol. 184, No. 7
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.7.1940-1946.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




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