Recent advances in heterologous gene expression in Escherichia coli.
Recent advances in protein expression in E. coli have focused primarily on the enhancement of protein quality. Problems in mRNA translation such as inefficient initiation, mistranslation, frame-shifting and frame-hopping can often be addressed by altering heterologous gene-coding sequences. Fusion technology can also be used to address problems in translational initiation, the authenticity of amino-terminal amino acids, in vivo protein activity and protein purification. Accessory molecules, such as chaperones, are increasingly used to enhance protein quality in vivo and in vitro. E. coli has recently gained wide use as a host both for the engineering of proteins with altered activities and for the creation of multi-functional hybrids.
Olins
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Monsanto Corporate Research, Monsanto Company, St. Louis, Missouri 63198.
Lee
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D001709:Biotechnology; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D015870:Gene Expression; D015394:Molecular Structure; D014176:Protein Biosynthesis; D015202:Protein Engineering; D012333:RNA, Messenger / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
D012333:RNA, Messenger; D011994:Recombinant Proteins