Three novel proteins co-localise with polyhydroxybutyrate (PHB) granules in Rhodospirillum rubrum S1

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منابع مشابه

The "intracellular" poly(3-hydroxybutyrate) (PHB) depolymerase of Rhodospirillum rubrum is a periplasm-located protein with specificity for native PHB and with structural similarity to extracellular PHB depolymerases.

Rhodospirillum rubrum possesses a putative intracellular poly(3-hydroxybutyrate) (PHB) depolymerase system consisting of a soluble PHB depolymerase, a heat-stable activator, and a 3-hydroxybutyrate dimer hydrolase (J. M. Merrick and M. Doudoroff, J. Bacteriol. 88:60-71, 1964). In this study we reinvestigated the soluble R. rubrum PHB depolymerase (PhaZ1). It turned out that PhaZ1 is a novel typ...

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Photosynthesis in Rhodospirillum rubrum

Ribulose 1,5-diphosphate carboxylase has been isolated from autotrophically cultured Rhoclospirillum rubrum. The molecular weight is 120,000. The K, for ribulose 1,5diphosphate is 83 mM, and for CO2 is 59 mM. The enzyme is inhibited by three important metabolites: citrate, an intermediate of the tricarboxylic acid cycle; inorganic phosphate; and 3-phosphoglyceric acid, the product of the reacti...

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Comparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16.

Identification of proteins that were present in a polyhydroxybutyrate (PHB) granule fraction isolated from Ralstonia eutropha but absent in the soluble, membrane, and membrane-associated fractions revealed the presence of only 12 polypeptides with PHB-specific locations plus 4 previously known PHB-associated proteins with multiple locations. None of the previously postulated PHB depolymerase is...

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Photosynthesis in Rhodospirillum rubrum

Ribulose 1,5-diphosphate carboxylase has been isolated from autotrophically cultured Rhoclospirillum rubrum. The molecular weight is 120,000. The K, for ribulose 1,5diphosphate is 83 mM, and for CO2 is 59 mM. The enzyme is inhibited by three important metabolites: citrate, an intermediate of the tricarboxylic acid cycle; inorganic phosphate; and 3-phosphoglyceric acid, the product of the reacti...

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The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha.

Analysis of the genome sequence of the polyhydroxyalkanoate- (PHA) accumulating bacterium Ralstonia eutropha strain H16 revealed three homologues (PhaP2, PhaP3 and PhaP4) of the phasin protein PhaP1. PhaP1 is known to constitute the major component of the layer at the surface of poly(3-hydroxybutyrate), poly(3HB), granules. PhaP2, PhaP3 and PhaP4 exhibited 42, 49 and 45 % identity or 61, 62 and...

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ژورنال

عنوان ژورنال: Microbiology

سال: 2018

ISSN: 1350-0872,1465-2080

DOI: 10.1099/mic.0.000642