Affiliation:
1. Faculty of Science, Monash University, Clayton 3168 and School of Microbiology, University of Melbourne, Parkville 3052, Victoria, Australia
Abstract
The pathway of pyrimidine biosynthesis in
Pseudomonas aeruginosa
has been shown to be the same as in other bacteria. Twenty-seven mutants requiring uracil for growth were isolated and the mutant lesions were identified. Mutants lacking either dihydroorotic acid dehydrogenase, orotidine monophosphate pyrophosphorylase, orotidine monophosphate decarboxylase, or aspartic transcarbamylase were isolated; none lacking dihydroorotase were found. By using transduction and conjugation, four genes affecting pyrimidine biosynthetic enzymes have been identified and shown to be unlinked to each other. The linkage of
pyrB
to
met-28
and
ilv-2
was shown by contransduction. Repression by uracil alone or by broth could not be demonstrated for any enzymes of this pathway, in contrast to the situation in
Escherichia coli
and
Serratia marcescens
. In addition, derepression of these enzymes could not be demonstrated. A low level of feedback inhibition of aspartic transcarbamylase was found to occur. It is suggested that the control of such constitutive biosynthetic enzymes in
P. aeruginosa
may be related to the comprehensive metabolic activities of this organism.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
112 articles.
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