Isolation and identification of granule-associated proteins relevant for poly(3-hydroxyalkanoic acid) biosynthesis in Chromatium vinosum D |
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Authors: | Matthias Liebergesell,Bernhard Schmidt,Alexander Steinbü chel |
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Affiliation: | Institut für Mikrobiologie, George-August-Universität Göttingen, Göttingen, FRG |
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Abstract: | Abstract Poly(3-hydroxybutyric acid) granules, which harbored only four major granule-associated proteins as revealed by SDS polyacrylamide gel electrophoresis, were isolated from crude cellular extracts of Chromatium vinosum D by centrifugation in a linear sucrose gradient. N-Terminal amino acid sequence determination identified two proteins of M r 41 000 and M r 40 000 as the phaE Cv and phaC Cv translational products, respectively, of C. vinosum D. In a previous study it was shown that both proteins are required for the expression opf poly(3-hydroxyalkanoic acid) synthase activity. The N-terminus of the third protein ( M r 17 000) exhibited no homology to other proteins. Lysozyme, which was during purification of the granules, exhibited a strong affinity to PHB granules and was identified as the fourth protein enriched with the granules. |
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Keywords: | PHA synthase Poly(3-hydroxybutyric acid) Biodegradable polyester PHB granule Granule-associated proteins Chromatium vinosum Escherichia coli Alcaligenes eutrophus Lysozyme |
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