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An Expanded Eukaryotic Genetic Code
A general and rapid route for the addition of unnatural amino acids to the genetic code of Saccharomyces cerevisiae is described, providing a gateway to the systematic expansion of the genetic codes of multicellular eukaryotes. Expand
Site-specific PEGylation of proteins containing unnatural amino acids.
A generally applicable PEGylation methodology based on the site-specific incorporation of para-azidophenylalanine into proteins in yeast is reported, useful for the generation of selectively P EGylated proteins for therapeutic applications. Expand
Structure and function of the macrolide biosensor protein, MphR(A), with and without erythromycin.
The combination of these two structures illustrates the molecular basis of erythromycin-induced gene expression and provides a framework for additional applied uses of this protein in the isolation and engineered biosynthesis of polyketide natural products. Expand
Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae.
Using a novel genetic selection, we have identified a series of mutants of the E. coli tyrosyl-tRNA synthetase that selectively charge an amber suppressor tRNA with p-(propargyloxy)phenylalanine andExpand
Biochemical Evidence for an Editing Role of Thioesterase II in the Biosynthesis of the Polyketide Pikromycin*
The results provide the first unequivocal in vitro evidence that TEII can hydrolyze acyl-ACP thioesters and a model for the action of TEII in which the enzyme remains primarily dissociated from the polyketide synthase, preferentially removing aberrant acel-ACP species with long half-lives. Expand
A general method for scanning unnatural amino acid mutagenesis.
A simple, fast, and effective way to perform scanning codon mutagenesis throughout a protein sequence that allows the researcher to define the new codon change, and therefore any amino acid mutation can be achieved. Expand
A genetically encoded photocaged amino acid.
Using a novel genetic selection, a series of synthetase mutants are identified that selectively charge the amber suppresor tRNA with the C8 amino acid, alpha-aminocaprylic acid, and the photocaged amino acids, o-nitrobenzyl cysteine, allowing them to be inserted into proteins in yeast in response to the amber nonsense codon, TAG. Expand
An unexpected interaction between the modular polyketide synthases, erythromycin DEBS1 and pikromycin PikAIV, leads to efficient triketide lactone synthesis.
Plasmid-based expression of DEBS1, which comprises the loading domain and the first two modules of the Saccharopolyspora erythrea 6-deoxyerythronolide B synthase, in S. venezuelae leads to efficient 15 +/- 3 mg/L production of triketide lactone products (TKLs). Expand
Site-specific incorporation of fluorotyrosines into proteins in Escherichia coli by photochemical disguise.
This work genetically encoded the unnatural amino acids o-nitrobenzyl-2-fluorotyrosine, -3-fluorschmidtine, and -2,6-difluorotYrosine in Escherichia coli, effectively preventing global incorporation of fluorotyosine into proteins. Expand
Condensed E. coli cultures for highly efficient production of proteins containing unnatural amino acids.
This work presents a universal approach to improve the efficiency of biosynthetic processes using condensed Escherichia coli cultures to produce proteins containing site-specifically incorporated unnatural amino acids. Expand