The 22nd Amino Acid

@article{Atkins2002The2A,
  title={The 22nd Amino Acid},
  author={John F. Atkins and Raymond F. Gesteland},
  journal={Science},
  year={2002},
  volume={296},
  pages={1409 - 1410}
}
Images of the human brain. (A) Five-year-old child in an MRI scanner. (B) Recent noninvasive MRI methods measure the function and structure of a child’s brain. The top row depicts patterns of brain activity indexed by fMRI in three representative axial (Z) slices. The bottom row shows corticospinal white-matter fiber tracts (green) projecting through the same three axial slices measured by DTI. 

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...

References

SHOWING 1-10 OF 10 REFERENCES

The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the ‘termination’ codon, TGA.

The identification of a genomic recombinant as encoding the entire mouse GSHPx gene is reported, and the selenocysteine in the active site of the enzyme is encoded by TGA.

Expanding the Genetic Code of Escherichia coli

A unique transfer RNA/aminoacyl-tRNA synthetase pair has been generated that expands the number of genetically encoded amino acids in Escherichia coli and should provide a general method for increasing the genetic repertoire of living cells to include a variety of amino acids with novel structural, chemical, and physical properties not found in the common 20 amino acids.

The renaissance of aminoacyl‐tRNA synthesis

The role of tRNA as the adaptor in protein synthesis has held an enduring fascination for molecular biologists, but recent developments in genomics and structural biology have revealed an unexpected array of new enzymes, pathways and mechanisms involved in aminoacyl‐tRNA synthesis.

Recoding: dynamic reprogramming of translation.

A minority of genes in probably all organisms rely on "recoding" for translation of their mRNAs. In these cases, the rules for decoding are temporarily altered through the action of specific signals

Selenocysteine incorporation directed from the 3'UTR: characterization of eukaryotic EFsec and mechanistic implications.

Key questions about the mechanistic details and efficiency of this intriguing process can begin to be addressed, through identification of the factors catalyzing cotranslational selenocysteine insertion in eukaryotes.

Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii.

It is speculated that in Archaea the functions of bacterial SelB are distributed over at least two proteins, one, serving as the specific translation factor, like MJ0495, and another one, binding to the SECIS which interacts with the ribosome and primes it to decode UGA.

Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli.

The results are consistent with a co-translational selenocysteine incorporation mechanism.

Pyrrolysine Encoded by UAG in Archaea: Charging of a UAG-Decoding Specialized tRNA

Results indicate that pyrrolysine is the 22nd genetically encoded natural amino acid to be encoded by the UAG codon in methylamine methyltransferase genes of Methanosarcina barkeri.

A New UAG-Encoded Residue in the Structure of a Methanogen Methyltransferase

The UAG-encoded residue in a 1.55 angstrom resolution structure of the Methanosarcina barkerimonomethylamine methyltransferase (MtmB) reveals a homohexamer comprised of individual subunits with a TIM barrel fold that appears consistent with a lysine in amide-linkage to (4R,5R)-4-substituted-pyrroline-5-carboxylate.