Selenoproteins in Archaea and Gram-positive bacteria

Stock, Tilmann; Rother, Michael

doi:10.1016/j.bbagen.2009.03.022

Cited by 73 publications

(60 citation statements)

References 162 publications

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“…Among Grampositive bacteria, all the selenoproteins experimentally known were found exclusively in anaerobic bacteria belonging to the clostridial clade. Examples include glycine reductase from Clostridium sticklandii (12) and Eubacterium acidaminophilum (13), proline reductase in C. sticklandii (14), xanthine dehydrogenase in C. acidiurici (15), and several antioxidant defense proteins (16). Enterococcus faecalis is the only member of the Firmicutes/Lactobacillales subdivision containing a SeCysdecoding trait (SelD) (17).…”

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confidence: 99%

Privileged Incorporation of Selenium as Selenocysteine in Lactobacillus reuteri Proteins Demonstrated by Selenium-specific Imaging and Proteomics

Galano

Mangiapane

Bianga³

et al. 2013

Molecular & Cellular Proteomics

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An analytical approach was developed to study the incorporation of selenium (Se), an important trace element involved in the protection of cells from oxidative stress, into the well-known probiotic Lactobacillus reuteri Lb2 BM-DSM 16143. The analyses revealed that about half of the internalized Se was covalently incorporated into soluble proteins. Se-enriched proteins were detected in 2D gels by laser ablation inductively coupled plasma mass spectrometry imaging (LA-ICP MSI) and identified by capillary HPLC with the parallel ICP MS ( 78 Se) and electrospray Orbitrap MS/MS detection. On the basis of the identification of 10 richest in selenium proteins, it was demonstrated that selenium was incorporated by the strain exclusively as selenocysteine. Also, the exact location of selenocysteine within the primary sequence was determined. This finding is in a striking contrast to another common nutraceutical, Se-enriched yeast, which incorporates Se principally as selenomethionine. Molecular & Cellular

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confidence: 99%

Privileged Incorporation of Selenium as Selenocysteine in Lactobacillus reuteri Proteins Demonstrated by Selenium-specific Imaging and Proteomics

Galano

Mangiapane

Bianga³

et al. 2013

Molecular & Cellular Proteomics

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“…The results presented cannot confirm that the Selenium was exclusively required for this enzyme system, but it is clearly vital to the proper functioning of this pathway. Oxyanions are also required for formyl-methanofuran dehydrogenase, and Se for hydrogenase and heterodisulfide reductase (Müller, 2003;Thauer et al, 2008;Stock and Rother, 2009;Zhu and Tan, 2009). …”

Section: 2mentioning

confidence: 99%

Trace element requirements for stable food waste digestion at elevated ammonia concentrations

Banks

Zhang

Jiang

et al. 2012

Bioresource Technology

318

162

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The work investigated why anaerobic digesters treating food waste and operating at high ammonia concentrations suffer from propionic acid accumulation which may result in process failure. The results showed deficiency of selenium, essential for both propionate oxidation and syntrophic hydrogenotrophic methanogenesis, leads to this while supplementation allows operation at substantially higher organic loading rates (OLR). At high loadings cobalt also becomes limiting, due to its role either in acetate oxidation in a reverse Wood-Ljungdahl pathway or in hydrogenotrophic methanogenesis. Population structure analysis using fluorescent in-situ hybridisation showed only hydrogenotrophic methanogens. Critical Se and Co concentrations were established as 0.16 and 0.22 mg kg -1 fresh matter feed at moderate loading. At this dosage the OLR could be raised to 5 g VS l -1 day -1 giving specific and volumetric biogas productions of 0.75 m 3 kg -1 VS added and 3.75 STP m 3 m -3 day -1 , representing a significant increase in process performance and operational stability.

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“…Although cases of conversion of Cys to Sec have been proposed (Zhang et al 2006), this is the first clearly documented case. Among archaea, SelD was found only in Methanococcales and Methanopyri genomes, whose selenoproteins have been previously characterized (Stock and Rother 2009). The SeU trait was found only in Methanococcales, although with a peculiarity: ybbB is split in two adjacent genes (Su et al 2012).…”

Section: Resultsmentioning

confidence: 99%

Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization

et al. 2015

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Selenoproteins are proteins that incorporate selenocysteine (Sec), a nonstandard amino acid encoded by UGA, normally a stop codon. Sec synthesis requires the enzyme Selenophosphate synthetase (SPS or SelD), conserved in all prokaryotic and eukaryotic genomes encoding selenoproteins. Here, we study the evolutionary history of SPS genes, providing a map of selenoprotein function spanning the whole tree of life. SPS is itself a selenoprotein in many species, although functionally equivalent homologs that replace the Sec site with cysteine (Cys) are common. Many metazoans, however, possess SPS genes with substitutions other than Sec or Cys (collectively referred to as SPS1). Using complementation assays in fly mutants, we show that these genes share a common function, which appears to be distinct from the synthesis of selenophosphate carried out by the Sec-and Cys-SPS genes (termed SPS2), and unrelated to Sec synthesis. We show here that SPS1 genes originated through a number of independent gene duplications from an ancestral metazoan selenoprotein SPS2 gene that most likely already carried the SPS1 function. Thus, in SPS genes, parallel duplications and subsequent convergent subfunctionalization have resulted in the segregation to different loci of functions initially carried by a single gene. This evolutionary history constitutes a remarkable example of emergence and evolution of gene function, which we have been able to trace thanks to the singular features of SPS genes, wherein the amino acid at a single site determines unequivocally protein function and is intertwined to the evolutionary fate of the entire selenoproteome.[Supplemental material is available for this article.]Selenoproteins are proteins that incorporate the nonstandard amino acid selenocysteine (Sec or U) in response to the UGA codon. The recoding of UGA, normally a stop codon, to code for Sec is arguably the most outstanding programmed exception to the genetic code. Selenoproteins are found, albeit in small numbers, in organisms across the entire tree of life. Recoding of UGA is mediated by RNA structures within selenoprotein transcripts, the SECIS (SElenoCysteine Insertion Sequence) elements. Sec biosynthesis and insertion also require a dedicated system of trans-acting factors that include elements that are common and others that are specific to the three domains of life: bacteria (Kryukov and Gladyshev

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Selenoproteins in Archaea and Gram-positive bacteria

Cited by 73 publications

References 162 publications

Privileged Incorporation of Selenium as Selenocysteine in Lactobacillus reuteri Proteins Demonstrated by Selenium-specific Imaging and Proteomics

Privileged Incorporation of Selenium as Selenocysteine in Lactobacillus reuteri Proteins Demonstrated by Selenium-specific Imaging and Proteomics

Trace element requirements for stable food waste digestion at elevated ammonia concentrations

Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization

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