Molecular biology: Genetic code seizes pyrrolysine
نویسندگان
چکیده
منابع مشابه
Genetic Code: Introducing Pyrrolysine
Monomethylamine methyltransferase of the archaebacterium Methanosarcina barkeri contains a novel amino acid, pyrrolysine, encoded by the termination codon UAG. Initial studies suggest that pyrrolysine may be co-translationally inserted during protein synthesis, probably by a mechanism analogous to that operating during selenocysteine incorporation.
متن کاملAdding pyrrolysine to the Escherichia coli genetic code.
Pyrrolysyl-tRNA synthetase and its cognate suppressor tRNA(Pyl) mediate pyrrolysine (Pyl) insertion at in frame UAG codons. The presence of an RNA hairpin structure named Pyl insertion structure (PYLIS) downstream of the suppression site has been shown to stimulate the insertion of Pyl in archaea. We study here the impact of the presence of PYLIS on the level of Pyl and the Pyl analog N-epsilon...
متن کاملA natural genetic code expansion cassette enables transmissible biosynthesis and genetic encoding of pyrrolysine.
Pyrrolysine has entered natural genetic codes by the translation of UAG, a canonical stop codon. UAG translation as pyrrolysine requires the pylT gene product, an amber-decoding tRNA(Pyl) that is aminoacylated with pyrrolysine by the pyrrolysyl-tRNA synthetase produced from the pylS gene. The pylTS genes form a gene cluster with pylBCD, whose functions have not been investigated. The pylTSBCD g...
متن کاملMolecular evolution: Please release me, genetic code
The genetic code is no longer universal, even in non-mitochondrial genomes. Recent studies have implicated the eukaryotic release factor eRF1 in mediating coding changes that are not as inconceivable as once thought. Specific residues in eRF1 proteins can be correlated with specific code changes in a wide variety of taxa.
متن کاملThe molecular basis for the genetic code.
* One of the authors (F.R.) was supported by grant PF-244 from the American Cancer Society. Present address: Department of Biochemistry, Michigan State University, East Lansing, Michigan. t Present address: Department of Chemistry, Princeton University, Princeton, New Jersey. 1 Madison, J. T., and R. W. Holley, Biochem. Biophys. Res. Commun., 18, 153 (1965). 2 Zachau, G. F., D. D'Utting, and H....
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ژورنال
عنوان ژورنال: Nature
سال: 2004
ISSN: 0028-0836,1476-4679
DOI: 10.1038/431257a