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Cupriavidus pinatubonensis  JMP134 utilizes a variety of aromatic substrates as sole carbon sources, including  meta -nitrophenol (MNP). Two polyhydroxyalkanoate (PHA) synthase genes,  phaC1  and  phaC2 , were annotated and categorized as class I and class II PHA synthase genes, respectively. In this study, both His-tagged purified PhaC1 and PhaC2 were shown to exhibit typical class I PHA synthase substrate specificity to make short-chain-length (SCL) PHA from 3-hydroxybutyryl-CoA and failed to make medium-chain-length (MCL) PHA from 3-hydroxyoctanoyl-CoA. The  phaC1  or  phaC2  deletion strain could also produce SCL PHA when grown in fructose or octanoate, but the double mutant of  phaC1  and  phaC2  lost this ability. The PhaC2 also exhibited substrate preference towards SCL substrates when expressed in  Pseudomonas aeruginosa  PAO1  phaC  mutant strain. On the other hand, the transcriptional level of  phaC1  was 70-fold higher than that of  phaC2  in MNP-grown cells, but 240-fold lower in octanoate-grown cells. Further study demonstrated that only  phaC1  was involved in PHA synthesis in MNP-grown cells. These findings suggested that  phaC1  and  phaC2  genes were differentially regulated under different growth conditions in this strain. Within the  phaC2 -containing gene cluster, a single copy of PHA synthase gene was present clustering with genes encoding enzymes in the biosynthesis of PHA precursors. This is markedly different from the genetic organization of all other previously reported class II PHA synthase gene clusters and this cluster likely comes from a distinct evolutionary path.

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Two Polyhydroxyalkanoate Synthases from Distinct Classes from the Aromatic Degrader Cupriavidus pinatubonensis JMP134 Exhibit the Same Substrate Preference