Global ETD Search

1	Requirements and rationale for amber translation as pyrrolysine Longstaff, David Gordon 10 December 2007 (has links) No description available. pyrrolysine pyrrolysyl-tRNA pyrrolysyl-tRNA synthetase pyrrolysine biosynthesis genetic code expansion PYLIS element pyrrolysine function
2	STUDIES OF THE PYRROLYSYL-TRNA SYNTHETASE Jiang, Ruisheng 23 July 2013 (has links) No description available. Biochemistry Microbiology Archaeology pyrrolysine Amino Acid Aminoacyl tRNA Synthetase Archaea Bacteria RNA-binding Protein Transfer RNA (tRNA) 22nd Amino Acid Genetic Code Pyrrolysyl-tRNA Synthetase
3	A novel aminoacyl-tRNA synthetase and its amino acid, pyrrolysine, the 22nd genetically encoded amino acid Larue, Ross C. January 2009 (has links) No description available. Biochemistry Microbiology Molecular Biology pyrrolysine aminoacyl tRNA-synthetases genetic code Methanosarcina aminoacylation PylS tRNA novel amino acid pyrrolysyl-tRNA pyrrolysine biosynthesis
4	Orthogonality and Codon Preference of the Pyrrolysyl-tRNA Synthetase-tRNAPyl pair in Escherichia coli for the Genetic Code Expansion Odoi, Keturah 2012 May 1900 (has links) Systematic studies of basal nonsense suppression, orthogonality of tRNAPyl variants, and cross recognition between codons and tRNA anticodons are reported. E. coli displays detectable basal amber and opal suppression but shows a negligible ochre suppression. Although detectable, basal amber suppression is fully inhibited when a pyrrolysyl-tRNA synthetase (PylRS)-tRNAPyl_CUA pair is genetically encoded. trnaPyl_CUA is aminoacylated by an E. coli aminoacyl-tRNA synthetase at a low level, however, this misaminoacylation is fully inhibited when both PylRS and its substrate are present. Besides that it is fully orthogonal in E. coli and can be coupled with PylRS to genetically incorporate a NAA at an ochre codon, tRNAPyl_UUA is not able to recognize an UAG codon to induce amber suppression. This observation is in direct conflict with the wobble base pair hypothesis and enables using an evolved M. jannaschii tyrosyl-tRNA synthetase-tRNAPyl_UUA pair and the wild type or evolved PylRS-tRNAPyl_UUA pair to genetically incorporate two different NAAs at amber and ochre codons. tRNAPyl_UCA is charged by E. coli tryptophanyl-tRNA synthetase, thus not orthogonal in E. coli. Mutagenic studies of trnaPyl_UCA led to the discovery of its G73U form which shows a higher orthogonality. Mutating trnaPyl_CUA to trnaPyl_UCCU not only leads to the loss of the relative orthogonality of tRNAPyl in E. coli but also abolishes its aminoacylation by PylRS. Pyl, pyrrolysine PylRS, pyrrolysyl-tRNA synthetase NAA, noncanonical amino acid aaRS, aminoacyl-tRNA synthetase T4 PNK, T4 polynucleotide kinase AzF, para-azido-L-phenylalanine PCR, polymerase chain reaction RF, release factor TrpRS, tryptophanyl-tRNA synthetase ArgRS, arginyl-tRNA synthetase Trp, tryptophan Lys, lysine Glu, glutamate Gln, glutamine Phe, phenylalanine Arg, arginine.

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