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

DOI Web Site 被引用文献4件
  • Markus Pötter
    Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, 48149 Münster, Germany
  • Helena Müller
    Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, 48149 Münster, Germany
  • Frank Reinecke
    Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, 48149 Münster, Germany
  • Roman Wieczorek
    Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, 48149 Münster, Germany
  • Florian Fricke
    Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Grisebachstrasse 8, 37077 Göttingen, Germany
  • Botho Bowien
    Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Grisebachstrasse 8, 37077 Göttingen, Germany
  • Bärbel Friedrich
    Institut für Biologie, Humboldt-Universität Berlin, Chausseestrasse 117, 10115 Berlin, Germany
  • Alexander Steinbüchel
    Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, Corrensstrasse 3, 48149 Münster, Germany

抄録

<jats:p>Analysis of the genome sequence of the polyhydroxyalkanoate- (PHA) accumulating bacterium<jats:italic>Ralstonia eutropha</jats:italic>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 63 % similarity to PhaP1, respectively. The calculated molecular masses of PhaP1, PhaP2, PhaP3 and PhaP4 were 20·0, 20·2, 19·6 and 20·2 kDa, respectively. RT-PCR analysis showed that<jats:italic>phaP2</jats:italic>,<jats:italic>phaP3</jats:italic>and<jats:italic>phaP4</jats:italic>were transcribed under conditions permissive for accumulation of poly(3HB). 2D PAGE of the poly(3HB) granule proteome and analysis of the detected proteins by MALDI-TOF clearly demonstrated that PhaP1, PhaP3 and PhaP4 are bound to the poly(3HB) granules in the cells. PhaP3 was expressed at a significantly higher level in PhaP1-negative mutants. Occurrence of an unknown protein with an N-terminal amino-acid sequence identical to that of PhaP2 in crude cellular extracts of<jats:italic>R. eutropha</jats:italic>had previously been shown by others. Although PhaP2 could not be localized<jats:italic>in vivo</jats:italic>on poly(3HB) granules,<jats:italic>in vitro</jats:italic>experiments clearly demonstrated binding of PhaP2 to these granules. Further analysis of complete or partial genomes of other poly(3HB)-accumulating bacteria revealed the existence of multiple phasin homologues in<jats:italic>Ralstonia solanacearum</jats:italic>,<jats:italic>Burkholderia fungorum</jats:italic>and<jats:italic>Azotobacter vinelandii</jats:italic>. These new and unexpected findings should affect our current models of PHA-granule structure and may also have a considerable impact on the establishment of heterologous production systems for PHAs.</jats:p>

収録刊行物

  • Microbiology

    Microbiology 150 (7), 2301-2311, 2004-07-01

    Microbiology Society

被引用文献 (4)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ