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Deletions fusing the hisG and hisD genes in Salmonella typhimurium.

Frameshift mutation hisD497 occurs in the operator-proximal portion of the Salmonella typhimurium gene coding for the dimeric protein, L-histidinol dehydrogenase ( HDH). Rare revertants of hisD497 are deletions fusing the hisD gene to the adjacent preceding structural gene, hisG (adenosine 5'-triphosphate-PR transferase). HDH purified from one revertant, hisGD4908, contains subunits of approximately normal molecular weight but with no clearly demonstrable unique amino-terminal sequence. We propose that a combined inactive G-D polypeptide is synthesized and then cleaved at a number of closely juxtaposed sites by endoproteolytic activity. At least some of the resulting fragments then participate in formation of active HDH dimers.[1]

References

  1. Deletions fusing the hisG and hisD genes in Salmonella typhimurium. Ino, I., Hartman, P.E., Hartman, Z., Yourno, J. J. Bacteriol. (1975) [Pubmed]
 
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