title: Isolation and identification of granule-associated proteins relevant for poly(3-hydroxyalkanoic acid) biosynthesis in Chromatium vinosum D.
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 phaECv and phaCCv translational products, respectively, of C. vinosum D. In a previous study it was shown that both proteins are required for the expression of 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 added during purification of the granules, exhibited a strong affinity to PHB granules and was identified as the fourth protein enriched with the granules.
authors: Institut für Mikrobiologie, Georg-August-Universität Göttingen, FRG.
authors: M
authors: M
authors: Liebergesell
authors: B
authors: B
authors: Schmidt
authors: A
authors: A
authors: Steinbüchel
mesh_terms: D000217:Acyltransferases / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002844:Chromatium / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D006885:Hydroxybutyrates / Q000378:metabolism*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000235:genetics; D011091:Polyesters / Q000378:metabolism*; D000094122:Polyhydroxybutyrates
chemical_list: D000217:Acyltransferases; D001426:Bacterial Proteins; D006885:Hydroxybutyrates; D009113:Muramidase; D011091:Polyesters; C003182:poly-beta-hydroxybutyrate; D000094122:Polyhydroxybutyrates; C077225:poly(3-hydroxyalkanoic acid) synthase