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J Bacteriol. 1972 April; 110(1): 171-178
Copyright © 1972 American Society for Microbiology. All Rights Reserved.

Construction and Properties of Escherichia coli Strains Exhibiting {alpha}-Complementation of ß-Galactosidase Fragments In Vivo

Patrice J. Zamenhof and Merna Villarejo

Department of Biological Chemistry, School of Medicine, and Molecular Biology Institute, University of California, Los Angeles, California 90024

ABSTRACT

In vivo {alpha}-complementation of ß-galactosidase was demonstrated in 16 Z gene terminator (nonsense) mutant strains of Escherichia coli upon introduction of the episome F'M15 which specifies production of a mutant Z gene polypeptide containing a small deletion in the N-terminal region of the enzyme monomer. Genetic and biochemical analyses of the merodiploids showed that restoration of enzyme activity was due to their terminator/F'M15 genetic constitution resulting in the production of two enzymatically inactive polypeptides which associate in vivo to reconstitute active, stable ß-galactosidase. The prematurely terminated polypeptide fragments known to be rapidly degraded in haploid cells were shown by phenotypic and biochemical studies to be stabilized (i.e., protected) in merodiploids by formation of complemented enzyme complexes with the M15 protein. Phenotypic properties of complementing diploids are described and are discussed in relation to in vitro determination of ß-galactosidase activity.

J Bacteriol. 1972 April; 110(1): 171-178
Copyright © 1972 American Society for Microbiology. All Rights Reserved.



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