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The polyhydroxyalkanoic acid (PHA) granule-associated 16-kDa protein (GA16 protein) ofParacoccus denitrificans was identified, and its corresponding gene was cloned and analyzed at the molecular level. The N-terminal amino acid sequence of GA16 protein revealed that its structural gene is located downstream from the PHA synthase gene (phaC Pd ) cloned recently (S. Ueda, T. Yabutani, A. Maehara, and T. Yamane, J. Bacteriol. 178:774–779, 1996). Gene walking aroundphaC Pd revealed two new open reading frames (ORFs) possibly related to PHA synthesis, one of which was thephaP Pd gene, encoding GA16 protein, and the other was thephaR Pd gene, encoding a protein that is putatively involved in the regulation of the expression ofphaP Pd . Overproduction of PhaPPd was observed inEscherichia coli carryingphaP Pd , but the overproduction was not observed in the presence ofphaR Pd . Coexpression ofphaP Pd and PHA biosynthesis genes inE. coli caused increases in both the number of poly-(3-hydroxybutyric acid) (PHB) granules and PHB content and caused decreases in both the size of the granules and the molecular weight of PHB. GA16 protein was considered a phasin protein. ThephaR Pd gene had significant similarities tostdC , a possible transcriptional factor ofComamonas testosteroni , as well as to other ORFs of unknown function previously found in other PHA-synthetic bacteria.

journal of bacteriology

Analyses of a Polyhydroxyalkanoic Acid Granule-Associated 16-Kilodalton Protein and Its Putative Regulator in the <i>pha</i> Locus of <i>Paracoccus denitrificans</i>

Analyses of a Polyhydroxyalkanoic Acid Granule-Associated 16-Kilodalton Protein and Its Putative Regulator in the pha Locus of Paracoccus denitrificans