Abstract
Plasmids containing a mouse cDNA sequence encoding the enzyme dihydrofolate reductase (DHFR; tetrahydrofolate dehydrogenase; 5,6,7,8-tetrahydrofolate:NADP+ oxidoreductase, EC 1.5.1.3) have been 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. Our results indicate that initiation of a structurally discrete and biologically functional eukaryotic protein can occur in bacteria on a fused mRNA molecule, and that the efficiency of expression is strongly affected by: (i) the extent of homology of the translational control region with the 3'-OH end of 16S ribosomal RNA, and (ii) the distance between the protein start codon and the ribosome-binding sequence on the mRNA.
MeSH Terms
Animals
Base Sequence
Codon
DNA, Recombinant
Epitopes
Escherichia coli/genetics
Genes
Mice
Operon
Peptide Chain Initiation, Translational
RNA, Messenger/genetics
Tetrahydrofolate Dehydrogenase/genetics,immunology
beta-Lactamases/genetics
Chemicals
Codon
DNA, Recombinant
Epitopes
RNA, Messenger
Tetrahydrofolate Dehydrogenase
beta-Lactamases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Chang A C
Erlich H A
Gunsalus R P
Nunberg J H
Kaufman R J
Schimke R T
Cohen S N
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