Expression in <i>Escherichia coli</i> of a Chemically Synthesized Gene for the Hormone Somatostatin

Keiichi Itakura; Tadaaki Hirose; Roberto Crea; Arthur D. Riggs; Herbert L. Heyneker; Francisco Bolívar; Herbert W. Boyer

doi:10.1126/science.412251

Abstract

A gene for somatostatin, a mammalian peptide (14 amino acid residues) hormone, was synthesized by chemical methods. This gene was fused to the Escherichia coli β-galactosidase gene on the plasmid pBR322. Transformation of E. coli with the chimeric plasmid DNA led to the synthesis of a polypeptide including the sequence of amino acids corresponding to somatostatin. In vitro, active somatostatin was specifically cleaved from the large chimeric protein by treatment with cyanogen bromide. This represents the first synthesis of a functional polypeptide product from a gene of chemically synthesized origin.

Keywords

Cyanogen bromideEscherichia coliPlasmidGenePBR322Gene productSomatostatinChemistryTransformation (genetics)Amino acidMolecular biologyPeptide sequencePeptideBiochemistryBiologyGene expression

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Publication Info

Year: 1977
Type: article
Volume: 198
Issue: 4321
Pages: 1056-1063
Citations: 841
Access: Closed

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APA Style

                            
                                
                                    Keiichi Itakura, 
                                
                                    Tadaaki Hirose, 
                                
                                    Roberto Crea
                                
                                et al.
                            
                            (1977). 
                            Expression in <i>Escherichia coli</i> of a Chemically Synthesized Gene for the Hormone Somatostatin. 
                            Science
                            , 198
                            (4321)
                            , 1056-1063.
                            https://doi.org/10.1126/science.412251
                        

Identifiers

DOI: 10.1126/science.412251