Protein organization on the PHA inclusion cytoplasmic boundary.

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  • Additional Information
    • Source:
      Publisher: Elsevier Science Publishers Country of Publication: Netherlands NLM ID: 8411927 Publication Model: Print Cited Medium: Print ISSN: 0168-1656 (Print) Linking ISSN: 01681656 NLM ISO Abbreviation: J Biotechnol Subsets: MEDLINE
    • Publication Information:
      Original Publication: Amsterdam : Elsevier Science Publishers, c1984-
    • Subject Terms:
      Acids, Acyclic/*metabolism ; Bacterial Proteins/*metabolism ; Cytoplasmic Granules/*metabolism; Cupriavidus necator/genetics ; Cupriavidus necator/metabolism ; Cupriavidus necator/ultrastructure ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli/ultrastructure ; Freeze Fracturing ; Genes, Bacterial ; Microscopy, Electron ; Pseudomonas/genetics ; Pseudomonas/metabolism ; Pseudomonas/ultrastructure
    • Abstract:
      Polyhydroxyalkanoate (PHA) cellular inclusions consist of polyesters, phospholipids, and proteins. Both the polymerase and the depolymerase enzymes are active components of the structure. Recently, proteins associated with these inclusions have been described in a number of bacterial species. In order to further clarify the structure and function of these proteins in relation to polymer inclusions, ultrastructural studies of isolated polymer inclusions were initiated. The surface boundary characteristics of polymer inclusions, produced by several genera of bacteria, two different Pseudomonas putida deletion mutants and by Escherichia coli recombinants, were examined. The recombinant E. coli carried either the PHB biosynthesis operon (phaCAB) from Ralstonia eutropha alone, or both this operon and a gene encoding an inclusion surface protein of R. eutropha (phaP). The results support two suggestions: (i) specific genes in the PHA gene cluster code for the proteins forming the surface boundary arrays which characterize the polymer inclusion; and (ii) transfer of such a gene would result in subcellular compartmentalization of accumulating polymer. Although the proteins appear to serve a similar function among different genera, nevertheless, the different surface proteins are encoded by a variety of non-homologous genetic sequences.
    • Accession Number:
      0 (Acids, Acyclic)
      0 (Bacterial Proteins)
    • Publication Date:
      Date Created: 19981120 Date Completed: 19981218 Latest Revision: 20190915
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/s0168-1656(98)00096-0
    • Accession Number:
      9821672