Initiation of protein synthesis in bacteria at a translational start codon of mamalian cDNA: effects of the preceding nucleotide sequence.

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Abstract
Plasmids containing a mouse c[complementary]DNA sequence encoding the enzyme dihydrofolate reductase (DHFR; tetrahydrofolate dehydrogenase; 5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) were used to study the efficiency of initiation of protein synthesis at an ATG (AUG) translational start codon indigenous to the eukaryotic cDNA. Differences in DHFR production assayed phenotypically, enzymatically and immunologically were correlated with the primary structure of the DNA segment that precedes the translational start codon. The initiation of a structurally discrete and biologically functional eukaryotic protein can occur in bacteria on a fused mRNA molecule, and the efficiency of expression is strongly affected by: the extent of homology of the translational control region with the 3''-OH end of 16S rRNA and the distance between the protein start codon and the ribosome-binding sequence on the mRNA.