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Markus Pötter

Researcher at University of Münster

Publications -  14
Citations -  1655

Markus Pötter is an academic researcher from University of Münster. The author has contributed to research in topics: Ralstonia & PHA granule. The author has an hindex of 12, co-authored 14 publications receiving 1511 citations.

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Genome sequence of the bioplastic-producing “Knallgas” bacterium Ralstonia eutropha H16

TL;DR: The complete genome sequence of the two chromosomes of R. eutropha H16 is reported, offering the genetic basis for exploiting the biotechnological potential of this organism and providing insights into its remarkable metabolic versatility.
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Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16.

TL;DR: Regulation of expression of the phasin PhaP, which is the major protein at the surface of polyhydroxyalkanoate (PHA) granules in Ralstonia eutropha H16, was studied and analysed at the molecular level to support the following model for the regulation of phaP expression.
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Poly(3-hydroxybutyrate) granule-associated proteins: impacts on poly(3-hydroxybutyrate) synthesis and degradation.

TL;DR: The intention of this review is to give an overview about the current knowledge of the structure of the PHA granule surface and the P HA granule-associated proteins involved in biogenesis and degradation.
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The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha.

TL;DR: In vitro experiments clearly demonstrated binding of PhaP2 to the poly(3HB) granules in the cells and these new and unexpected findings should affect current models of PHA-granule structure and may also have a considerable impact on the establishment of heterologous production systems for PHAs.
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Influence of homologous phasins (PhaP) on PHA accumulation and regulation of their expression by the transcriptional repressor PhaR in Ralstonia eutropha H16.

TL;DR: The current model for the regulation of phasins in R. eutropha strain H16 was extended and confirmed and the capability of the transcriptional repressor PhaR to bind to a DNA region +36 to +46 bp downstream of the phaP3 start codon was demonstrated.