Increased synthesis of human parathyroid hormone in Escherichia coli through alterations of the 5' untranslated region.
The expression of human parathyroid hormone (hPTH) in Escherichia coli was optimized by variations of the spacing sequence between the ribosome-binding site (RBS) and the beginning of the gene (ATG) and by increasing the complementarity of the RBS to the 16 S rRNA. The expression level of 3 micrograms/liter increased more than 100-fold to 475 micrograms/liter as a direct consequence of modifications in the region 5' of the gene.
D001483:Base Sequence; D004275:DNA, Ribosomal / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D010281:Parathyroid Hormone / Q000096:biosynthesis / Q000235:genetics*; D014176:Protein Biosynthesis; D012336:RNA, Ribosomal, 16S / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis; D014158:Transcription, Genetic
D004275:DNA, Ribosomal; D010281:Parathyroid Hormone; D012336:RNA, Ribosomal, 16S; D011994:Recombinant Proteins