Spacer alterations which increase the expression of porcine growth hormone in E. coli

FEBS Letters

Wells, Julian R.E.¹  Vize, Peter D.¹ 

[1] Department of Biochemistry, University of Adelaide, GPO Box 498, Adelaide, South Australia 5001, Australia

关键词: Translational efficiency;    Oligonucleotide-directed mutagenesis;    Ribosome binding site;    Codon alteration;    Growth hormone;    (Porcine pituitary);   

DOI  :  10.1016/0014-5793(87)81482-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Full-length porcine growth hormone (PGH) cDNA clones were isolated from a porcine pituitary cDNA library. When the coding portion of the PGH gene was cloned into an E. coli expression vector downstream from the powerful trc promoter, high levels of mRNA, but no protein were detected. Mutation directed by an oligodeoxynucleotide primer altered 5'-non-coding sequences and raised the level of PGH produced from undetectable to 15% of the total cellular protein. Alteration of four codons infrequently used by E. coli in the 5'-end of the gene produced no further increases.

【 授权许可】

Unknown