Characterization of Polynucleotide Phosphorylase Mutants of Escherichia coli

Author:

Reiner Albey M.1

Affiliation:

1. Biological Laboratories, Harvard University, Cambridge, Massachusetts 02138

Abstract

Three polynucleotide phosphorylase mutations, isolated in heavily mutagenized Escherichia coli strains Q7, Q13, and Q27, were characterized after their transfer by P1 transduction to nearly isogenic strains which lack ribonuclease I. Each strain has a different altered form of polynucleotide phosphorylase. One enzyme exhibited sharply reduced activity under all conditions tested. A second had reduced activity which was stimulated by Mn ++ . The third enzyme was thermolabile and could be >95% inactivated in vivo at 44 C and p H 6 if the cells were prevented from growing; during growth under these and other conditions, the full enzyme level was maintained. The strains showed no differences from the wild type in their growth rates, their adjustments to changes in media and temperature, or their recoveries from starvation.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference13 articles.

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3. Isolation and characterization of ribonuclease I mutants of Escherichia coli;Gesteland R. F.;J. Mol. Biol.,1966

4. Polymerization of nucleoside diphosphate with a manganese-dependent enzyme from Escherichia coil Q13;Hsieh W. T.;Proc. Natl. Acad. Sci. U.,1967

5. The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on the structure of the yeast alcohol dehydrogenase molecule;Kagi J. H. R.;J. Biol. Chem.,1961

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