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Journal of Bacteriology, January 1999, p. 585-592, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Polyhydroxyalkanoate Inclusion Body-Associated Proteins and Coding Region in Bacillus megaterium

Gabriel J. McCool1 and Maura C. Cannon2,*

Department of Microbiology1 and Department of Biochemistry and Molecular Biology,2 University of Massachusetts, Amherst, Massachusetts 01003

Received 20 July 1998/Accepted 9 November 1998

Polyhydroxyalkanoic acids (PHA) are carbon and energy storage polymers that accumulate in inclusion bodies in many bacteria and archaea in response to environmental conditions. This work presents the results of a study of PHA inclusion body-associated proteins and an analysis of their coding region in Bacillus megaterium 11561. A 7,917-bp fragment of DNA was cloned and shown to carry a 4,104-bp cluster of 5 pha genes, phaP, -Q, -R, -B, and -C. The phaP and -Q genes were shown to be transcribed in one orientation, each from a separate promoter, while immediately upstream, phaR, -B, and -C were divergently transcribed as a tricistronic operon. Transfer of this gene cluster to Escherichia coli and to a PhaC- mutant of Pseudomonas putida gave a Pha+ phenotype in both strains. Translational fusions to the green fluorescent protein localized PhaP and PhaC to the PHA inclusion bodies in living cells. The data presented are consistent with the hypothesis that the extremely hydrophilic protein PhaP is a storage protein and suggests that PHA inclusion bodies are not only a source of carbon, energy, and reducing equivalents but are also a source of amino acids.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003. Phone: (413) 545-0092. Fax: (413) 545-1578. E-mail: mcannon{at}bio.umass.edu.

Journal of Bacteriology, January 1999, p. 585-592, Vol. 181, No. 2
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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