JBC, Vol. 253, Issue 23, 8351-8354, Dec, 1978
The peptide chain elongation factor genes tufA and fus of Escherichia coli are intimately related physically
A. V. Furano and M. Sullivan
Recent work from several laboratories has established the following points
about the synthesis of the polypeptide chain elongation factors Tu and G in
Escherichia coli. (i) Elongation factor Tu is the product of duplicate,
highly conserved genes, tufA and tufB, which are widely separate parts of
the chromosome. (ii) The molar concentration of this factor is
considerably higher than that of elongation factor G which is encoded by
the fus gene. (iii) Although the tufA and fus genes are close together and
can be co-transcribed in the direction from fus to tufA, the tufA gene
product is synthesized at several times the rate of the fus gene product.
In an attempt to understand what mechanism(s) could account for the
differential expression of the tufA and fus genes, we sought to obtain more
precise information on the physical relationship of these genes. By
examining heteroduplexes between restriction endonuclease-generated
fragments of DNA containing the tufA, fus, and tufB genes, we have
demonstrated that the fus and tufA genes are intimately related physically
in one of two possible arrangements. Either the NH2-terminal region of the
tufA gene is contiguous with the COOH-terminal region of the fus gene or
the beginning of the tufA gene overlaps part of the fus gene. These results
mean that if the tufA gene is always co-transcribed with the fus gene, then
some mechanism must allow the tufA portion of the transcript to be
translated more often than the fus gene portion of the transcript.
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