Summary
The utilisation of acetylhistidine by histidine auxotrophs of E. coli K-12 was found to require a functioning acetylornithinase. The growth, on acetylhistidine-containing media, of his mutants possessing this enzyme was inhibited by arginine or its precursors acetylornithine, ornithine and citrulline. Mutants able to overcome this inhibition belonged to two classes: those (selected on acetylhistidine+acetylornithine or arginine) in which the arginine biosynthetic enzymes were repressible, as in the parent strains; and those (selected on acetylhistidine+acetylornithine, ornithine, citrulline or arginine) in which these enzymes were formed at high, non-repressible levels. The altered properties of the first class were shown genetically not to result from mutation in the argR or argECBH regions; the data are consistent with the second class carrying mutations at the argR locus.
It is supposed that arginine, ornithine or citrulline, by repressing the formation of acetylornithinase, diminish the rate at which acetylhistidine can be utilised (although an acetylhistidine uptake system under arginine control would equally explain the results); non-repressible mutants would escape this effect. The kinetic properties, in crude extracts, of acetylornithinase from the parent strains and from members of each mutant class, with acetylornithine and acetylhistidine as substrates, were investigated. It was tentatively concluded that, in accord with the genetic results, the first class do not possess an acetylornithinase altered to make it function better with acetylhistidine as substrate. It is suggested that arginine may affect acetylhistidine utilisation by affecting its uptake in a manner not shared with ornithine or citrulline, as well as by repressing proteins of the arginine system, and that this arginine-specific effect is inoperative in the first class of mutants. The nature of the changes leading to ability to grow on acetylhistidine+acetylornithine remains unknown. Possible applications of these findings to the selection of hitherto undiscovered but potentially informative mutant types are discussed.
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Communicated by W. K. Maas
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Baumberg, S. Acetylhistidine as substrate for acetylornithinase: A new system for the selection of arginine regulation mutants in Escherichia coli . Molec. Gen. Genet. 106, 162–173 (1970). https://doi.org/10.1007/BF00323835
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DOI: https://doi.org/10.1007/BF00323835