Characterization of Mammalian Selenoproteomes

@article{Kryukov2003CharacterizationOM,
  title={Characterization of Mammalian Selenoproteomes},
  author={Gregory V. Kryukov and Sergio Castellano and Sergey V. Novoselov and Alexey V. Lobanov and Omid Zehtab and Roderic Guig{\'o} and Vadim N. Gladyshev},
  journal={Science},
  year={2003},
  volume={300},
  pages={1439 - 1443},
  url={https://api.semanticscholar.org/CorpusID:10363908}
}
This work identified selenoprotein genes in sequenced mammalian genomes by methods that rely on identification of selenocysteine insertion RNA structures, the coding potential of UGA codons, and the presence of cysteine-containing homologs.
View on AAAS
digitalcommons.unl.edu
2,209 Citations
Highly Influential Citations
84
Background Citations
797
Methods Citations
88
Results Citations
9

2,209 Citations

Computational Design of New and Recombinant Selenoproteins

Selenoproteins contain the 21th amino acid Selenocysteine, which is encoded by the STOP-codon UGA. For its insertion it requires a specific mRNA sequence downstream the UGA-codon that forms a…

The prokaryotic selenoproteome

Characterization of selenoproteomes allows interpretation of other UGA codons in completed genomes of prokaryotes as terminators, addressing the UGA dual‐function problem.

A selenocysteine tRNA and SECIS element in Plasmodium falciparum.

To the knowledge of this work, this is the first report of an identification of protozoan selenocysteine insertion machinery at the sequence level in Plasmodium falciparum.

Selenocysteine Biosynthesis, Selenoproteins, and Selenoproteomes

Roles of selenium and selenoproteins in health have also been addressed through sophisticated transgenic/knockout models that targeted removal or modulation of Sec tRNA expression.

Overexpression of Recombinant Selenoproteins in E. coli.

This chapter summarizes a method to achieve recombinant selenoprotein production in E. coli by decoding of a UGA codon from termination of translation to insertion of selenocysteine.

Selenocysteine Extinctions in Insects

Selenocysteine (Sec) is a nonstandard amino acid present in a minor fraction of proteins, called selenoproteins. Sec is an analog of cysteine (Cys) with selenium replacing sulfur. Sec is inserted…

A Method for Identification of Selenoprotein Genes in Archaeal Genomes

Making sense of nonsense: the evolution of selenocysteine usage in proteins

A recent analysis of sequences derived from organisms in the Sargasso Sea has revealed a surprisingly different set of selenium-containing proteins than that previously found in sequenced genomes and…

Biosynthesis, Engineering, and Delivery of Selenoproteins

Methods to produce selenoproteins with 21 or more amino acids and approaches to delivering recombinant selenoproteins to mammalian cells as new applications for selenoproteins in synthetic biology are reviewed.

Facile Recoding of Selenocysteine in Nature.

TRNA(Sec) species with different anticodons enabled E. coli to synthesize active formate dehydrogenase H, a selenoenzyme, and show the genetic code is much more flexible than previously thought.
...

41 References

Knowing when not to stop: selenocysteine incorporation in eukaryotes.

In silico identification of novel selenoproteins in the Drosophila melanogaster genome

A method to predict selenoproteins in genomic sequences, which relies on the prediction of SECIS elements in coordination with the Prediction of genes in which the strong codon bias characteristic of protein coding regions extends beyond a TGA codon interrupting the open reading frame is described.

Mammalian Selenoprotein in Which Selenocysteine (Sec) Incorporation Is Supported by a New Form of Sec Insertion Sequence Element

A new eukaryotic selenoprotein is identified, designated SelM, which is expressed in a variety of tissues, with increased levels in the brain, and its N-terminal signal peptide is necessary for protein translocation.

Novel Selenoproteins Identified in Silico andin Vivo by Using a Conserved RNA Structural Motif*

Four novel selenoproteins were discovered based on a computational screen for the RNA hairpin directing selenocysteine incorporation, and it is found that another protein, SelX, displays sequence similarity to a protein involved in bacterial pilus formation.

Decoding apparatus for eukaryotic selenocysteine insertion

expression of the two functional domains of the bacterial elongation factor–SECIS binding protein as two separate proteins in eukaryotes suggests a mechanism for rapid exchange of charged for uncharged selenocysteyl‐tRNA–elongation factor complex, allowing a single SECIS element to serve multiple UGA codons.

New Mammalian Selenocysteine-containing Proteins Identified with an Algorithm That Searches for Selenocysteine Insertion Sequence Elements*

A computer program is described here a computer program, SECISearch, that identifies mammalian selenoprotein genes by recognizing SECIS elements on the basis of their primary and secondary structures and free energy requirements.

Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation

Several lines of evidence enabled us to establish that mSelB is the bona fide mammalian elongation factor for selenoprotein translation: it binds GTP, recognizes the Sec‐tRNASec in vitro and in vivo, and is required for efficient selenobrotein translation in vivo.

Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?

The molecular cloning of human and mouse homologs of the selD gene, designated Sps2, which contains an in-frame TGA codon at a site corresponding to the enzyme's putative active site suggests the existence of an autoregulatory mechanism involving the incorporation of Sec into SPS2 that might be relevant to blood cell biology.

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

It is shown that successful incorporation of seleno-cysteine into this enzyme requires a specific 3′ untranslated (3′ut) segment of about 200 nucleotides, which is found in both rat and human 5′DI messenger RNAs.

A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs

It is established that SBP2 is essential for the co‐translational insertion of Sec into selenoproteins and hypothesize that the binding activity of SBp2 may be involved in preventing termination at the UGA/Sec codon.