Structure of Selenophosphate Synthetase Essential for Selenium Incorporation into Proteins and RNAs

Itoh, Yuzuru; Sekine, S.; Matsumoto, Emiko; Akasaka, Ryogo; Takemoto, Chie; Shirouzu, Mikako; Yokoyama, Shigeyuki

doi:10.1016/j.jmb.2008.08.042

Cited by 40 publications

(70 citation statements)

References 39 publications

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“…Therefore, homodecamerization, and consequently, the Ser-Sec conversion and selenoprotein biosynthesis, is dependent on the N-terminal region (or N terminus), as we observed by functional complementation with the N-terminally truncated E. coli SelA. Similar results from A. aeolicus SelA N-terminal mutants (27) (7,10), to form Sec-tRNA Sec . The SPS dimerization interface is composed of the ␤-sheet domain of each monomer, a common structural characteristic of the PurM protein superfamily (7).…”

Section: Discussionsupporting

confidence: 76%

“…In addition, consistent with the SPS crystallographic structures (PDB ID 3U0O) that were previously described, the glycine-rich N-terminal region of SPS was observed to be flexible in solution, showing high levels of deuterium exchange even after low deuterium exposure time. This flexibility allows the formation of the SPS active site on its "closed" form, upon ATP binding, releasing the catalysis product in its "open" form (7,10).…”

Section: Discussionmentioning

confidence: 99%

“…In E. coli, these PLP-donor enzymes act as ␤-lyases, catalyzing the cleavage of the C-S bond from Cys or the C-Se bond from Sec to Ala and S 0 or Se 0 , respectively (3,11,13). However, an interaction between SPS and NifS-like enzymes has not been described, although a structural basis for the interaction of E. coli CsdB and A. aeolicus SPS was proposed because the molecular surfaces surrounding the active sites of CsdB and SPS exhibit complementarity by molecular docking (10). It is possible that thioredoxin reductase, which is involved in selenite reduction, is also involved in delivering selenide for SPS (3,13).…”

mentioning

confidence: 99%

“…It is possible that thioredoxin reductase, which is involved in selenite reduction, is also involved in delivering selenide for SPS (3,13). After selenophosphate is synthesized, it remains bound to the active-site cavity of SPS until ADP hydrolysis occurs and the product release is completed (7,10).…”

mentioning

confidence: 99%

“…Itoh et al (10) hypothesized that SPS could interact with SelA in a manner similar to that of NifS-like proteins, facilitating the efficient transfer of selenophosphate from SPS to SelA; however, this interaction has never been formally proven. Interestingly, the human SepSecS was reported to interact in vivo with the SPS1 isoform (14), but little is known about the mechanism of this interaction.…”

mentioning

confidence: 99%

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Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria

Silva

Serrão

Manzine

et al. 2015

Journal of Biological Chemistry

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Background: Selenoprotein biosynthesis requires the interaction of tRNA Sec and specific enzymes that drive the synthesis of selenocysteine. Results: Formation of a molecular complex of selenophosphate synthetase, selenocysteine synthase, and tRNA Sec was identified and characterized. Conclusion:The ternary complex formation is necessary for selenoprotein synthesis.Significance: Our findings demonstrate the formation of a ternary complex and provide a possible scenario for selenium metabolism in bacteria.

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Section: Discussionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria

Silva

Serrão

Manzine

et al. 2015

Journal of Biological Chemistry

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Selenocysteine

Rother

2015

Encyclopedia of Life Sciences

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The trace element selenium is present in the form of selenocysteine in selected proteins of organisms from all three domains of life. Most of the selenoproteins (i.e. proteins containing selenocysteine) investigated thus far are oxidoreductases with selenocysteine present in the active site and playing a crucial role in – or creating the required environment for – catalysis. Selenocysteine incorporation is DNA encoded, determined by the UGA codon, and occurs via a unique mechanism representing an expansion of the genetic code. Despite the conceptual conservation of the principal mechanism of selenocysteine synthesis and incorporation in all lines of descent, the bacterial system differs from the archaeal/eukaryal system. Detailed biochemical and structural knowledge of selenoprotein synthesis has allowed rewiring bacterial translation for targeted selenocysteine insertion. Key Concepts Selenium is an essential trace element for many organisms including humans. The most important form of biologically active selenium is the amino acid selenocysteine. Selenocysteine is co‐translationally inserted into growing polypeptides. Selenocysteine insertion proceeds via a unique mechanism recoding UGA. The mechanism of selenocysteine insertion differs in Bacteria, Archaea, and Eukarya.

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The Chemistry of Selenocysteine

Metanis¹,

Beld²,

Hilvert³

2011

Patai's Chemistry of Functional Groups

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Selenocysteine is a redox active amino acid. It is inserted co‐translationally into a number of natural proteins, providing them with a range of interesting enzymatic activities; it can also be incorporated into artificial peptides and proteins as a structural and mechanistic probe. In this chapter, the chemistry and biochemistry of this novel amino acid is reviewed. In addition to the (bio)synthesis of selenocysteine, selenopeptides and selenoproteins, the roles selenium plays in enzyme catalysis and its utility for diverse biotechnological applications are discussed.

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Structure of Selenophosphate Synthetase Essential for Selenium Incorporation into Proteins and RNAs

Cited by 40 publications

References 39 publications

Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria

Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria

Selenocysteine

The Chemistry of Selenocysteine

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