Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion

Wilting, Reinhard; Schorling, Stefan; Persson, Britt C.; Böck, August

doi:10.1006/jmbi.1996.0812

Cited by 140 publications

(130 citation statements)

References 15 publications

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“…In eukarya, it is located in the 3Ј nontranslated region and thus decoding from an appreciable distance is necessary (Berry et al, 1993;Low and Berry, 1996). In this respect the archaeal selenoprotein biosynthesis is more similar to the eukaryotic system than to the bacterial system (Wilting et al, 1997). Considering the similarity of the systems, a SelB-orthologous translation factor is also postulated for eukarya, which should have affinity to both SECIS and tRNA sec , and should control the correct decoding of the distant UGA codon by competing with the termination factor (Nasim et al, 2000).…”

Section: The Biosynthesis Of Selenoproteinsmentioning

confidence: 99%

Selenium in Biology: Facts and Medical Perspectives

Köhrl¹,

Brigelius‐Flohé²,

Böck³

et al. 2000

Biological Chemistry

245

143

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Several decades after the discovery of selenium as an essential trace element in vertebrates approximately 20 eukaryotic and more than 15 prokaryotic selenoproteins containing the 21 st proteinogenic amino acid, selenocysteine, have been identified, partially characterized or cloned from several species. Many of these proteins are involved in redox reactions with selenocysteine acting as an essential component of the catalytic cycle. Enzyme activities have been assigned to the glutathione peroxidase family, to the thioredoxin reductases, which were recently identified as selenoproteins, to the iodothyronine deiodinases, which metabolize thyroid hormones, and to the selenophosphate synthetase 2, which is involved in selenoprotein biosynthesis. Prokaryotic selenoproteins catalyze redox reactions and formation of selenoethers in (stress-induced) metabolism and energy production of E. coli, of the clostridial cluster XI and of other prokaryotes. Apart from the specific and complex biosynthesis of selenocysteine, selenium also reversibly binds to proteins, is incorporated into selenomethionine in bacteria, yeast and higher plants, or posttranslationally modifies a catalytically essential cysteine residue of CO dehydrogenase. Expression of individual eukaryotic selenoproteins exhibits high tissue specificity, depends on selenium availability, in some cases is regulated by hormones, and if impaired contributes to several pathological conditions. Disturbance of selenoprotein expression or function is associated with deficiency syndromes (Keshan and Kashin-Beck disease), might contribute to tumorigenesis and atherosclerosis, is altered in several bacterial and viral infections, and leads to infertility in male rodents.

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Section: The Biosynthesis Of Selenoproteinsmentioning

confidence: 99%

Selenium in Biology: Facts and Medical Perspectives

Köhrl¹,

Brigelius‐Flohé²,

Böck³

et al. 2000

Biological Chemistry

245

143

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“…Replacement of Cys-17 with serine results in the complete loss of activity with ATP and selenide as substrates (6). Analysis of the total genomic sequences of Methanococcus jannaschii (11) and Haemophilus influenzae (12) revealed that the selD gene in these organisms possesses a TGA codon at the position of the E. coli Cys-17, indicating the presence of a SeCys residue (9,10). Moreover, SeCys-containing variants also were identified in mouse and human enzymes (9).…”

mentioning

confidence: 99%

“…One group of SPS enzymes, which have a cysteine or SeCys residue at the site corresponding to Cys-17 in E. coli SELD, can catalyze the selenide-dependent formation of monoselenophosphate in vitro (3,4,9,10). Replacement of Cys-17 with serine results in the complete loss of activity with ATP and selenide as substrates (6).…”

mentioning

confidence: 99%

Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling l -selenocysteine and Sps2 for selenite assimilation

Tamura

Yamamoto

Takahata

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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A labile selenium donor compound monoselenophosphate is synthesized from selenide and ATP by selenophosphate synthetase (SPS). In the present study, Sps1 and Sps2 were cloned from a cDNA library prepared from human lung adenocarcinoma cells (NCI-H441). The human lung Sps1 has been cloned as an ORF of 1,179 bp, identical in sequence to that of the recently revised human liver Sps1. The in-frame TGA codon of the lung Sps2 was genetically altered to TGT (Cys) to obtain the Sps2Cys gene. Expression of the recombinant plasmids containing Sps1 or Sps2Cys was highly toxic to Escherichia coli host cells grown aerobically. Accordingly, the human lung Sps homologs were characterized by an in vivo complementation assay using a selD mutant strain. An added selenium source and a low salt concentration (0.1-0.25% NaCl) in the medium were required for reproducible and sensitive in vivo complementation. Sps2Cys effectively complemented the selD mutant, and the resulting formate dehydrogenase H activity was as high as that of WT E. coli MC4100. In contrast, only a weak complementation of the selD mutant by the Sps1 gene was observed when cells were grown in selenite media. Better complementation with added L-selenocysteine suggested involvement of a selenocysteine lyase for mobilization of selenium. Based on this apparent substrate specificity of the Sps1 and Sps2 gene products we suggest that the Sps1-encoded enzyme depends on a selenium salvage system that recycles L-selenocysteine, whereas the Sps2 enzyme can function with a selenite assimilation system. I n many biological systems, the concentration of sulfurcontaining compounds is on the order of 1,000 times greater than their selenium analogs (1). Thus a selenium-specific pathway for biosynthesis of proteins that contain selenocysteine (SeCys) residues inserted as directed by the UGA codon is required. In Escherichia coli the insertion of selenium into selenium-dependent enzymes and Se-containing tRNAs requires the participation of the selD gene product (2). This protein, later identified as selenophosphate synthetase (SPS), forms a highly reactive, reduced selenium compound, monoselenophosphate (3). Monoselenophosphate is the product of the reaction catalyzed by SPS in which the ␥-phosphoryl group of ATP is transferred to selenide and inorganic phosphate and AMP are formed (4, 5). The mechanism of this reaction has yet to be determined. The identification of an essential cysteine residue, Cys-17, in the N-terminal glycine-rich region of the E. coli enzyme (SELD) has led to the assumption that this residue behaves as a nucleophile in the hydrolysis of ATP (6, 7 The E. coli selD gene product and its homologs present in mammals and Drosophila can be divided into two major groups. One group of SPS enzymes, which have a cysteine or SeCys residue at the site corresponding to Cys-17 in E. coli SELD, can catalyze the selenide-dependent formation of monoselenophosphate in vitro (3, 4, 9, 10). Replacement of Cys-17 with serine results in the complete loss of activity with ATP and s...

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“…Sec is bound to nickel and is directly involved in catalysis [60]. Two different hydrogenase subunits may contain Sec, including one which may have two Sec residues [61].…”

Section: Prokaryotic Selenoproteinsmentioning

confidence: 99%

Selenoproteins and Selenoproteomes

Gladyshev

2011

Selenium

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Summary:In the past several years, progress in genome sequencing and development of specialized bioinformatics tools allowed effi cient identifi cation of selenocysteine-containing proteins encoded in completely sequenced genomes. Information is currently available on selenoproteomes from a variety of organisms, including humans, which contain 25 known selenoprotein genes. This review provides basic information about mammalian selenoproteins and other known selenoprotein families. Analysis of full sets of selenoproteins in organisms provides exciting avenues for examining selenoprotein evolution and dependence of organisms on the trace element selenium and allows linking selenoproteins with specifi c biological and biomedical effects of dietary selenium.

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Selenoprotein synthesis in archaea: identification of an mRNA element of Methanococcus jannaschii probably directing selenocysteine insertion

Cited by 140 publications

References 15 publications

Selenium in Biology: Facts and Medical Perspectives

Selenium in Biology: Facts and Medical Perspectives

Selenophosphate synthetase genes from lung adenocarcinoma cells: Sps1 for recycling l -selenocysteine and Sps2 for selenite assimilation

Selenoproteins and Selenoproteomes

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