Selenoprotein synthesis and regulation in Archaea

doi:10.1016/j.bbagen.2018.04.008

Biochimica et Biophysica Acta (BBA) - General Subjects

Volume 1862, Issue 11, November 2018, Pages 2451-2462

https://doi.org/10.1016/j.bbagen.2018.04.008 Get rights and content

Highlights

•
In Archaea, the majority of proteins containing selenocysteine (Sec), selenoproteins, are involved in methanogenesis.
•
The pathway of Sec synthesis in Archaea and Eukarya are principally identical.
•
Sec insertion in Eukarya probably evolved from an archaeal mechanism prior to the separation of the archaeal and eukaryal lines of decent.
•
Archaeal models may be highly valuable tools for unraveling “eukaryotic” principles in molecular and cell biology.

Abstract

Background

The major biological form of selenium is that of the co-translationally inserted amino acid selenocysteine (Sec). In Archaea, the majority of proteins containing Sec, selenoproteins, are involved in methanogenesis. However, the function of this residue is often not known because selenium-independent homologs of the selenoproteins can be employed, sometimes even in one organism.

Scope of review

This review summarizes current knowledge about the selenoproteins of Archaea, the metabolic pathways where they are involved, and discusses the (potential) function of individual Sec residues. Also, what is known about the “archaeal” way of selenoprotein synthesis, and the regulatory mechanism leading to the replacement of the selenoproteins with selenium-independent homologs, will be presented. Where appropriate, similarities with (and differences to) the respective steps employed in the other two domains, Bacteria and Eukarya, will be emphasized.

Major conclusions

Genetic and biochemical studies guided by analysis of genome sequences of Sec-encoding archaea has revealed that the pathway of Sec synthesis in Archaea and Eukarya are principally identical and that Sec insertion in Eukarya probably evolved from an archaeal mechanism employed prior to the separation of the archaeal and eukaryal lines of decent.

General significance

In light of the emerging close phylogenetic relationship of Eukarya and Archaea, archaeal models may be highly valuable tools for unraveling “eukaryotic” principles in molecular and cell biology.

Introduction

The element selenium was discovered in 1817 [1] and for the longest time regarded as toxic. However, in 1954 it was shown that E. coli required selenium for the synthesis of enzymes involved in formate oxidation [2], which hallmarks the role of this trace element for microbial metabolism. Today we know that selenium is essential for many organisms, including humans [3]. Biologically active selenium occurs (i) as a constituent of a base modification (5-[(methylamino)methyl]-2-selenouridine) in certain transfer RNAs (tRNAs, [4]), (ii) as a non-covalently bound selenium-containing cofactor found in xanthine and nicotinate dehydrogenases [5,6], and (iii) as the co-translationally inserted amino acid selenocysteine (Sec, 2-selenoalanine). As the name suggests, it is structurally identical to cysteine (Cys), only with the thiol group replaced by a selenol group.

The occurrence of Sec as the selenium moiety in naturally occurring proteins (selenoproteins) was first demonstrated in clostridial glycine reductase [7]. Selenoproteins are found in members of all three domains of life, the Bacteria, the Archaea, and the Eukarya. However, the majority of known organisms do not employ Sec. Since various aspects of this trait have been conserved in the three domains of life (see below), Sec was probably already present in the last universal common ancestor (LUCA) [[8], [9], [10]]. For most selenoproteins the specific functions of Sec are still unclear, because for all but one of the selenoproteins of prokaryotes (clostridial glycine reductase) homologous proteins with Cys at the respective position exist [11]. Consequently, there is currently only little evidence for natural positive selection in any single Sec residue [12]. The fact that the selenol group is mostly deprotonated at physiological pH due to its lower pk_a value (5.2 for Sec, 8.3 for Cys) might make it more reactive than Cys. Other physico-chemical properties of Sec possibly favor some selenoproteins over their Cys variants [[13], [14], [15], [16]] but a unifying principle encompassing all selenoproteins has, so far, not emerged and may simply not exist.

In this review we aim to summarize current knowledge about the selenoproteins in Archaea, the pathway of Sec synthesis and incorporation into proteins, as well as selenium-dependent gene regulation. Although many still consider Archaea as a “strange bacteria”, they were vital for progressing knowledge about Sec synthesis and incorporation in the eukaryal system. Many members of the Archaea have been developed into powerful genetic model systems [17]. Given the current discussion about the phylogenetic relation of Eukarya and Archaea within the tree of life [18], they may be highly valuable tools for unraveling other eukaryotic “secrets” in the future.

Section snippets

Commonalities of selenoprotein synthesis in the three domains

Unlike canonical translation elongation, where amino acids are acylated to their corresponding tRNAs by aminoacyl-tRNA synthetases, Sec is always synthesized in a tRNA-bound fashion. The Sec-specific tRNA (tRNA^Sec) differs from canonical elongator tRNAs in size and structural interactions (see below) and is in all known cases initially “mis-charged” with serine (Ser) by seryl-tRNA synthetase. The pathways of conversion from Ser-tRNA^Sec to Sec-tRNA^Sec differ between Bacteria on the one hand and

A methanogenic origin of the Sec utilization trait in eukaryotes?

Based on the analysis of ribosomal RNA, “Archaebacteria” were postulated to comprise one of three “urkingdoms” some 40 years ago [20], now known as the domains Bacteria, Eukarya, and Archaea [21]. At the time, the presumed “archaic” life-style of Archaea, being strictly anaerobic and/or inhabiting inhospitable environments like solfataric hot springs, soda lakes, and submarine volcanic vents, may have led to this tendentious designation. However, Archaea are ubiquitous and constitute a

Methanogenesis

Methane is the most abundant hydrocarbon present in our atmosphere. In environments lacking electron acceptors such as oxygen, sulfate, nitrate, or oxidized metal(loid)s, methane is the final breakdown product of organic matter. This process, anaerobic digestion, which is carried out by microorganisms of various trophic groups, can be categorized into four steps: (i) hydrolysis of the polymeric matter into oligomers and monomers, (ii) fermentation of the monomers (sugars, amino acids, fatty

Most selenoproteins of Archaea are involved in methanogenesis

As of 2017, where 498 archaeal (meta-)genomes were analyzed, 21 encode tRNA^Sec [40]. 19 of the respective organisms belong to the order Methanococcales (genera Methanocaldococcus, Methanotorris, Methanothermococcus, Methanococcus), one to the order Methanopyrales (genus Methanopyrus), and one to the uncultivated, proposed archaeal phylum Lokiarchaeota (see above). Table 1 lists known and putative archaeal selenoproteins and their properties (where known) are summarized in the following section.

Selenoprotein synthesis in Archaea

Considering that the ability to use Sec appears to be so asymmetrically distributed among the Archaea [40], it was a fortuitous coincidence that the first genome sequence published from this domain was that of Methanocaldococcus jannaschii [96]. It allowed the identification of putative selenoproteins as well as of some of the cis- and trans-active factors involved in their synthesis [89].

Selenium-dependent gene regulation

The dependence on selenium varies considerably among Sec-encoding methanogens. However, the experimental verification of selenium requirement is difficult, because of contaminating selenium present in (sodium) sulfide used as sulfur source and as a means to provide the strongly reduced conditions required by methanogens [130,162]. Growth of M. jannaschii depends on the presence of selenium [163], that of M. voltae is reduced when the selenium supply is limiting [162], while no effect on

Conclusions

It has been argued that eukaryotes “re-invented” the Sec utilization trait during evolution because their Sec-containing oxidoreductases, mostly involved in antioxidant defense and redox homeostasis, are so different from the selenoproteins of Bacteria and Archaea, which are mostly catabolically active and seem unrelated to the eukaryotic ones. However, this view might be challenged by the finding that an archaeal selenoprotein (HdrA) involved in a very ancient metabolism (methanogenesis)

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Acknowledgements

We thank Miljan Simonović (Chicago, USA) for sharing his contribution to this special issue prior to publication, Tristan Wagner (Marburg, Germany) for fruitful discussions about the possible role of Sec in methanogenic enzymes, and the Deutsche Forschungsgemeinschaft for supporting work in the authors' laboratory (RO 2445/7-1).

References (177)

M.D. Wolfe et al.
Functional diversity of the rhodanese homology domain: the Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase
J. Biol. Chem.
(2004)
E.S. Arner
Selenoproteins — what unique properties can arise with selenocysteine in place of cysteine?
Exp. Cell Res.
(2010)
R.K. Thauer
Anaerobic oxidation of methane with sulfate: on the reversibility of the reactions that are catalyzed by enzymes also involved in methanogenesis from CO₂
Curr. Opin. Microbiol.
(2011)
C. Welte et al.
Bioenergetics and anaerobic respiratory chains of aceticlastic methanogens
Biochim. Biophys. Acta
(2014)
J.G. Ferry
Formate dehydrogenase
FEMS Microbiol. Rev.
(1990)
J.B. Jones et al.
Selenium-dependent and selenium-independent formate dehydrogenases of Methanococcus vannielii. Separation of the two forms and characterization of the purified selenium-independent form
J. Biol. Chem.
(1981)
P.M. Vignais et al.
Classification and phylogeny of hydrogenases
FEMS Microbiol. Rev.
(2001)
S.B. Mulrooney et al.
Nickel uptake and utilization by microorganisms
FEMS Microbiol. Rev.
(2003)
M.W. Adams
The structure and mechanism of iron-hydrogenases
Biochim. Biophys. Acta
(1990)
E. Garcin et al.
The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center
Structure
(1999)

S. Yamazaki

A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue

J. Biol. Chem.

(1982)

J.R. Cupp-Vickery et al.

Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli

J. Mol. Biol.

(2004)

S.W. Kang et al.

Characterization of a mammalian peroxiredoxin that contains one conserved cysteine

J. Biol. Chem.

(1998)

I.Y. Kim et al.

Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide

J. Biol. Chem.

(1992)

I.Y. Kim et al.

Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization

J. Biol. Chem.

(1993)

Y. Itoh et al.

Structure of selenophosphate synthetase essential for selenium incorporation into proteins and RNAs

J. Mol. Biol.

(2009)

R. Wilting et al.

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

J. Mol. Biol.

(1997)

S. Commans et al.

Selenocysteine inserting tRNAs: an overview

FEMS Microbiol. Rev.

(1999)

J.J. Berzelius

Undersökning af en ny Mineral-kropp, funnen i de orenare sorterna af det i Falun tillverkade svaflet, Afhandlingar i fysik, kemi och mineralogi 6

(1818)

J. Pinsent

The need for selenite and molybdate in the formation of formic dehydrogenase by members of the coli-aerogenes group of bacteria

Biochem. J.

(1954)

N.V. Gladyshev

Selenoproteins and selenoproteomes

V.N. Gladyshev et al.

Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme

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

(1994)

D.H. Haft et al.

Orphan SelD proteins and selenium-dependent molybdenum hydroxylases

Biol. Direct

(2008)

J.E. Cone et al.

Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety

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

(1976)

J. Yuan et al.

RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea

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

(2006)

Y. Zhang et al.

Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues

Genome Biol.

(2006)

H. Romero et al.

Evolution of selenium utilization traits

Genome Biol.

(2005)

D.E. Fomenko et al.

High-throughput identification of catalytic redox-active cysteine residues

Science

(2007)

L. White et al.

Evolutionary basis for the use of selenocysteine

L.A. Wessjohann et al.

Selenium in chemistry and biochemistry in comparison to sulfur

Biol. Chem.

(2007)

G.W. Snider et al.

Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes

Biochemistry

(2013)

I. Ingold et al.

Selenium utilization by GPX4 is required to prevent hydroperoxide-induced ferroptosis

Cell

(2018)

J.A. Leigh et al.

Model organisms for genetics in the domain Archaea: methanogens, halophiles, Thermococcales and Sulfolobales

FEMS Microbiol. Rev.

(2011)

L. Eme et al.

Archaea and the origin of eukaryotes

Nat. Rev. Microbiol.

(2017)

M.J. Berry et al.

Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region

Nature

(1991)

C.R. Woese et al.

Phylogenetic structure of the prokaryotic domain: the primary kingdoms

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

(1977)

C.R. Woese et al.

Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya

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

(1990)

E.F. DeLong et al.

Environmental diversity of bacteria and archaea

Syst. Biol.

(2001)

A. Kletzin

General characteristics and important model organisms

P.S. Adam et al.

The growing tree of Archaea: new perspectives on their diversity, evolution and ecology

ISME J.

(2017)

P.N. Evans et al.

Methane metabolism in the archaeal phylum Bathyarchaeota revealed by genome-centric metagenomics

Science

(2015)

I. Vanwonterghem et al.

Methylotrophic methanogenesis discovered in the archaeal phylum Verstraetearchaeota

Nat. Microbiol.

(2016)

K. Raymann et al.

The two-domain tree of life is linked to a new root for the Archaea

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

(2015)

G. Borrel et al.

Methanogenesis and the Wood-Ljungdahl pathway: an ancient, versatile, and fragile association

Genome Biol. Evol.

(2016)

A. Spang et al.

Complex archaea that bridge the gap between prokaryotes and eukaryotes

Nature

(2015)

K. Zaremba-Niedzwiedzka et al.

Asgard archaea illuminate the origin of eukaryotic cellular complexity

Nature

(2017)

T.A. Williams et al.

An archaeal origin of eukaryotes supports only two primary domains of life

Nature

(2013)

M. Mariotti et al.

Lokiarchaeota marks the transition between the archaeal and eukaryotic selenocysteine encoding systems

Mol. Biol. Evol.

(2016)

R.K. Thauer et al.

Methanogenic archaea: ecologically relevant differences in energy conservation

Nat. Rev. Microbiol.

(2008)

M. Rother

Methanogenesis

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The price to pay for the use of Sec in an enzyme is high if considering the highly intricate, energy demanding and often inefficient translation machinery that is required for expression of a selenoprotein. There are qualitative differences between these translation machineries between the kingdoms of life, and between organisms, but all involve the use of a dedicated elongation factor specific for Sec insertion through the recoding of a UGA stop codon, achieved via interactions with a stem loop structure in the selenoprotein-encoding mRNA (a SECIS structure), use of a specific tRNA with an anticodon to the UGA that is originally serylated with the seryl moiety subsequently converted to selenocysteinyl on the tRNA, and a variety of accessory enzymes and factors supporting this translation machinery that is only used for the insertion of a Sec residue in a growing polypeptide chain at the ribosome (Allmang, Wurth, & Krol, 2009; Brocker et al., 2014; Driscoll & Copeland, 2003; Gursinsky et al., 2008; Lescure et al., 2002; Rother & Quitzke, 2018; Yoshizawa & Böck, 2009). This is thus a most complicated translation machinery, with species-specific variations, inefficiency on a cellular level compared to expression of most regular non-selenoproteins, and high complexity, further complicated by the inherent high chemical reactivity of Sec (indeed itself a possible reason why its synthesis has evolved to be so complicated, possibly as a means of controlling the reactivity of Sec that would otherwise lead to uncontrolled redox reactions in cells).
Selenoproteins containing the rare amino acid selenocysteine (Sec), typically being enzymes utilizing the selenium atom of Sec for promoted catalysis of redox reactions, are challenging to obtain at high amounts in pure form. The technical challenges limiting selenoprotein supply derive from intricacies in their translation, necessitating the recoding of a UGA stop codon to a sense codon for Sec. This, in turn, involves the interactions of a Sec-dedicated elongation factor, either directly or indirectly, with a structure in the selenoprotein-encoding mRNA called a SECIS element (Selenocysteine Insertion Sequence), a dedicated tRNA species for Sec with an anticodon for the UGA, and several accessory enzymes and proteins involved in the selenoprotein synthesis. Here, we describe an alternative method for recombinant selenoprotein production using UAG as the Sec codon in a specific strain of E. coli lacking other UAG codons and lacking the release factor RF1 that normally terminates translation at UAG. We also describe how such recombinant selenoproteins can be purified and further analyzed for final Sec contents. The methodology can be used for production of natural selenoproteins in recombinant form as well as for production of synthetic selenoproteins that may be designed to use the unique biophysical properties of Sec for diverse biotechnological applications.
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Three benzimidazolium salts (III-V) and respective selenium adducts (VI-VIII) were designed, synthesized and characterized by various analytical techniques (FT-IR and NMR ¹H, ¹³C). Selected salts and respective selenium N-Heterocyclic carbenes (selenium-NHC) adducts were tested in vitro against Cervical Cancer Cell line (Hela), Breast Adenocarcinoma cell line (MCF-7), Retinal Ganglion Cell line (RGC-5) and Mouse Melanoma Cell line (B16F10) using MTT assay and the results were compared with standard drug 5-Fluorouracil. Se-NHC compounds and azolium salts showed significant anticancer potential. Molecular docking studies of compounds (VI, VII and VIII) showed strong binding energies and ligand affinity toward following angiogenic factors: VEGF-A (vascular endothelial growth factor A), EGF (human epidermal growth factor), HIF (Hypoxia-inducible factor) and COX-1 (Cyclooxygenase-1) suggesting that the anticancer activity of adducts (VI, VII and VIII) may be due to their strong anti-angiogenic effect. In addition, compounds III-VIII were screened for their antibacterial and antifungal potential. Adduct VI was found to be potent anti-fungal agent against A. Niger with zone of inhibition (ZI) value 27.01 ± 0.251 mm which is better than standard drug Clotrimazole tested in parallel.

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^☆: This article is part of a Special Issue entitled Selenium research in biochemistry and biophysics - 200 year anniversary issue, edited by Dr. Elias Arnér and Dr. Regina Brigelius-Flohe.

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ReviewSelenoprotein synthesis and regulation in Archaea☆

Highlights

Abstract

Background

Scope of review

Major conclusions

General significance

Introduction

Section snippets

Commonalities of selenoprotein synthesis in the three domains

A methanogenic origin of the Sec utilization trait in eukaryotes?

Methanogenesis

Most selenoproteins of Archaea are involved in methanogenesis

Selenoprotein synthesis in Archaea

Selenium-dependent gene regulation

Conclusions

Transparency document

Acknowledgements

J. Biol. Chem.

Exp. Cell Res.

Curr. Opin. Microbiol.

Biochim. Biophys. Acta

FEMS Microbiol. Rev.

J. Biol. Chem.

FEMS Microbiol. Rev.

FEMS Microbiol. Rev.

Biochim. Biophys. Acta

Structure

J. Biol. Chem.

J. Mol. Biol.

J. Biol. Chem.

J. Biol. Chem.

J. Biol. Chem.

J. Mol. Biol.

J. Mol. Biol.

FEMS Microbiol. Rev.

Undersökning af en ny Mineral-kropp, funnen i de orenare sorterna af det i Falun tillverkade svaflet, Afhandlingar i fysik, kemi och mineralogi 6

The need for selenite and molybdate in the formation of formic dehydrogenase by members of the coli-aerogenes group of bacteria

Biochem. J.

Selenoproteins and selenoproteomes

Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme

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

Orphan SelD proteins and selenium-dependent molybdenum hydroxylases

Biol. Direct

Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety

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

RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea

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

Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues

Genome Biol.

Evolution of selenium utilization traits

Genome Biol.

High-throughput identification of catalytic redox-active cysteine residues

Science

Evolutionary basis for the use of selenocysteine

Selenium in chemistry and biochemistry in comparison to sulfur

Biol. Chem.

Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes

Biochemistry

Selenium utilization by GPX4 is required to prevent hydroperoxide-induced ferroptosis

Cell

Model organisms for genetics in the domain Archaea: methanogens, halophiles, Thermococcales and Sulfolobales

FEMS Microbiol. Rev.

Archaea and the origin of eukaryotes

Nat. Rev. Microbiol.

Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3′ untranslated region

Nature

Phylogenetic structure of the prokaryotic domain: the primary kingdoms

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

Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eucarya

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

Environmental diversity of bacteria and archaea

Syst. Biol.

General characteristics and important model organisms

The growing tree of Archaea: new perspectives on their diversity, evolution and ecology

ISME J.

Methane metabolism in the archaeal phylum Bathyarchaeota revealed by genome-centric metagenomics

Science

Methylotrophic methanogenesis discovered in the archaeal phylum Verstraetearchaeota

Nat. Microbiol.

Review
Selenoprotein synthesis and regulation in Archaea☆