| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 275, Issue 31, 23769-23773, August 4, 2000
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the 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. Kinetic
characterization revealed the Km value for selenide approached levels that are toxic to the cell. Our previous
demonstration that a Se0-generating system consisting of
L-selenocysteine and the Azotobacter vinelandii
NifS protein can replace selenide for selenophosphate biosynthesis
in vitro suggested a mechanism whereby cells can overcome
selenide toxicity. Recently, three E. coli NifS-like proteins, CsdB, CSD, and IscS, have been overexpressed and
characterized. All three enzymes act on selenocysteine and cysteine to
produce Se0 and S0, respectively. In the
present study, we demonstrate the ability of each E. coli
NifS-like protein to function as a selenium delivery protein for the
in vitro biosynthesis of selenophosphate by E. coli wild-type SPS. Significantly, the SPS (C17S) mutant,
which is inactive in the standard in vitro assay with
selenide as substrate, was found to exhibit detectable activity in the
presence of CsdB, CSD, or IscS and L-selenocysteine. Taken
together the ability of the NifS-like proteins to generate a selenium
substrate for SPS and the activation of the SPS (C17S) mutant suggest a
selenium delivery function for the proteins in
vivo.
Escherichia coli NifS-like Proteins Provide Selenium
in the Pathway for the Biosynthesis of Selenophosphate*
§,
Laboratory of Biochemistry, NHLBI, National
Institutes of Health, Bethesda, Maryland 20892 and the ¶ Institute
for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan
*
This work was supported by a Short-term Invitation
Fellowship for Research in Japan from the Japanese Society for the
Promotion of Science (to G.M.L.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  T. Tamura, S. Yamamoto, M. Takahata, H. Sakaguchi, H. Tanaka, T. C. Stadtman, and K. Inagaki Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling L-selenocysteine and Sps2 for selenite assimilation PNAS, November 16, 2004; 101(46): 16162 - 16167. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Pilon, J. D. Owen, G. F. Garifullina, T. Kurihara, H. Mihara, N. Esaki, and E. A.H. Pilon-Smits Enhanced Selenium Tolerance and Accumulation in Transgenic Arabidopsis Expressing a Mouse Selenocysteine Lyase Plant Physiology, March 1, 2003; 131(3): 1250 - 1257. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. T. Kaiser, S. Bruno, T. Clausen, R. Huber, F. Schiaretti, A. Mozzarelli, and D. Kessler Snapshots of the Cystine Lyase C-DES during Catalysis. STUDIES IN SOLUTION AND IN THE CRYSTALLINE STATE J. Biol. Chem., January 3, 2003; 278(1): 357 - 365. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Kobayashi, Y. Ogra, K. Ishiwata, H. Takayama, N. Aimi, and K. T. Suzuki Selenosugars are key and urinary metabolites for selenium excretion within the required to low-toxic range PNAS, December 10, 2002; 99(25): 15932 - 15936. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. A.H. Pilon-Smits, G. F. Garifullina, S. Abdel-Ghany, S.-I. Kato, H. Mihara, K. L. Hale, J. L. Burkhead, N. Esaki, T. Kurihara, and M. Pilon Characterization of a NifS-Like Chloroplast Protein from Arabidopsis. Implications for Its Role in Sulfur and Selenium Metabolism Plant Physiology, November 1, 2002; 130(3): 1309 - 1318. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Mihara, S.-i. Kato, G. M. Lacourciere, T. C. Stadtman, R. A. J. D. Kennedy, T. Kurihara, U. Tokumoto, Y. Takahashi, and N. Esaki The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H PNAS, May 14, 2002; 99(10): 6679 - 6683. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. M. Lacourciere Selenium Is Mobilized In Vivo from Free Selenocysteine and Is Incorporated Specifically into Formate Dehydrogenase H and tRNA Nucleosides J. Bacteriol., April 1, 2002; 184(7): 1940 - 1946. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Bebien, G. Lagniel, J. Garin, D. Touati, A. Vermeglio, and J. Labarre Involvement of Superoxide Dismutases in the Response of Escherichia coli to Selenium Oxides J. Bacteriol., March 15, 2002; 184(6): 1556 - 1564. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Frazzon and D. R. Dean Feedback regulation of iron-sulfur cluster biosynthesis PNAS, December 18, 2001; 98(26): 14751 - 14753. [Full Text] [PDF]
|
|
|
|
|
|
Y. Ogasawara, G. Lacourciere, and T. C. Stadtman Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein perselenide in a selenium delivery system PNAS, August 1, 2001; (2001) 171320998. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Ogasawara, G. Lacourciere, and T. C. Stadtman Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: Possible role of a protein perselenide in a selenium delivery system PNAS, August 14, 2001; 98(17): 9494 - 9498. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
