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J Biol Chem, Vol. 273, Issue 37, 24044-24051, September 11, 1998
From the Institut für Mikrobiologie, Westfälische
Wilhelms-Universität Münster, Corrensstra To investigate the metabolic link between fatty
acid de novo synthesis and polyhydroxyalkanoic acid (PHA)
synthesis, we isolated mutants of Pseudomonas putida KT2440
deficient in this metabolic route. The gene phaG was cloned
by phenotypic complementation of these mutants; it encoded a protein of
295 amino acids with a molecular mass of 33,876 Da, and the amino acid
sequence exhibited 44% amino acid identity to the primary structure of
the rhlA gene product, which is involved in the rhamnolipid
biosynthesis in Pseudomonas aeruginosa PG201.
S1 nuclease protection assay identified the transcriptional
start site 239 base pairs upstream of the putative translational start
codon. Transcriptional induction of phaG was observed when
gluconate was provided, and PHA synthesis occurred from this carbon
source. No complementation of the rhlA mutant P. aeruginosa UO299-harboring plasmid pBHR81, expressing phaG gene under lac promoter control, was
obtained. Heterologous expression of phaG in
Pseudomonas oleovorans, which is not capable of
PHA synthesis from gluconate, enabled PHA synthesis on gluconate as the
carbon source. Native recombinant PhaG was purified by native
polyacrylamide gel electrophoresis from P. oleovorans-harboring plasmid pBHR81. It catalyzes the transfer of
the acyl moiety from in vitro synthesized
3-hydroxydecanoyl-CoA to acyl carrier protein, indicating that PhaG
exhibits a 3-hydroxyacyl-CoA-acyl carrier protein transferase
activity.
A New Metabolic Link between Fatty Acid de Novo
Synthesis and Polyhydroxyalkanoic Acid Synthesis
THE PHAG GENE FROM PSEUDOMONAS PUTIDA
KT2440 ENCODES A 3-HYDROXYACYL-ACYL CARRIER PROTEIN-COENZYME A
TRANSFERASE
e 3, D-48149, Münster, Germany
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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