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Ribosomal Alterations Controlling Alkaline Phosphatase Isozymes in Escherichia coli

^a Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115

ABSTRACT

Different patterns of isozymes were obtained by starch-gel electrophoresis of alkaline phosphatase from Escherichia coli strains differing only by strA or ram mutations, or both, in the 30S ribosomal subunit. The isozyme spread was reduced in strA and increased in ram strains; this strictly parallels the restriction and enhancement of translational ambiguity produced by these mutations. Streptomycin present during growth had an effect similar to ram on both isozymes and ambiguity. The three isozymes analyzed have different N-terminal residues: aspartic acid, valine, and threonine. Different patterns of isozymes were also obtained in a wild-type strain through the specific action of exogenous arginine. A link between the mechanism of the effect of arginine and that of the ribosome is not obvious. The possibility is discussed that in both cases, although by different mechanisms, N-terminals are formed with different sensitivity to limited degradative attack.

¹ Present address: Department of Biochemistry, University of Oxford, Oxford, England.

² Present address: Department of Medicine, Jewish Hospital of St. Louis, St. Louis, Mo. 63134.