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New knowledge about the PHA-locus and P(3HB) granule-associated proteins in Chromatium vinosum

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Summary

The isolation of poly(3-hydroxybutyric acid) granules of Chromatium vinosum D was re-examined. Beside the PHA synthase and a 17 kDa protein, a 14 kDa protein was identified as predominant granule-associated protein. The M r as well as the N-terminal amino acid sequence exhibited identity to ORF5Cv, which is located within the pha-locus of C. vinosum. In addition, sequence alignements revealed new information about ORF4Cv, which is also located within the pha-locus, and about the 17 kDa protein, which exhibited homology to heat shock proteins recently detected in Escherichia coli.

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Authors and Affiliations

  1. Institut für Mikrobiologie der Westfälischen Wilhelms-Universität Münster, Corrensstraβe 3, D-48149, Münster, Germany

    Matthias Liebergesell & Alexander Steinbüchel

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  1. Matthias Liebergesell
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  2. Alexander Steinbüchel
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Liebergesell, M., Steinbüchel, A. New knowledge about the PHA-locus and P(3HB) granule-associated proteins in Chromatium vinosum . Biotechnol Lett 18, 719–724 (1996). https://doi.org/10.1007/BF00130772

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