Literature DB >> 7606669

Considerations on the structure and biochemistry of bacterial polyhydroxyalkanoic acid inclusions.

A Steinbuchel1, K Aerts, W Babel, C Follner, M Liebergesell, M H Madkour, F Mayer, U Pieper-Furst, A Pries, H E Valentin.   

Abstract

Some mathematical calculations were done that provided information about the structure and biochemistry of polyhydroxyalkanoic acid (PHA) granules and about the amounts of the different constituents that contribute to the PHA granules. The data obtained from these calculations are compared with data from the literature, which show that PHA granules consist not only of the polyester but also of phospholipids and proteins. The latter are referred to as granule-associated proteins, and they are always located at the surface of the PHA granules. A concept is proposed that distinguishes four classes of structurally and functionally different granule-associated proteins: (i) class I comprises the PHA synthases, which catalyze the formation of ester linkages between the constituents; (ii) class II comprises the PHA depolymerases, which are responsible for the intracellular degradation of PHA, (iii) class III comprises a new type of protein, which is referred to as phasins and which has most probably a function analogous to that of oleosins in oilseed plants, and (iv) class IV comprises all other proteins, which have been found to be associated with the granules but do not belong to classes I-III. Particular emphasis is placed on the phasins, which constitute a significant fraction of the total cellular protein. Phasins are assumed to form a close protein layer at the surface of the granules, providing the interface between the hydrophilic cytoplasm and the much more hydrophobic core of the PHA inclusion.

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Year:  1995        PMID: 7606669     DOI: 10.1139/m95-175

Source DB:  PubMed          Journal:  Can J Microbiol        ISSN: 0008-4166            Impact factor:   2.419


  54 in total

1.  In vivo immobilization of fusion proteins on bioplastics by the novel tag BioF.

Authors:  Cristina Moldes; Pedro García; José L García; María A Prieto
Journal:  Appl Environ Microbiol       Date:  2004-06       Impact factor: 4.792

2.  Polyhydroxyalkanoate production in Rhodobacter capsulatus: genes, mutants, expression, and physiology.

Authors:  R G Kranz; K K Gabbert; T A Locke; M T Madigan
Journal:  Appl Environ Microbiol       Date:  1997-08       Impact factor: 4.792

3.  Positive selection systems for discovery of novel polyester biosynthesis genes based on fatty acid detoxification.

Authors:  R G Kranz; K K Gabbert; M T Madigan
Journal:  Appl Environ Microbiol       Date:  1997-08       Impact factor: 4.792

Review 4.  Neutral lipid bodies in prokaryotes: recent insights into structure, formation, and relationship to eukaryotic lipid depots.

Authors:  Marc Wältermann; Alexander Steinbüchel
Journal:  J Bacteriol       Date:  2005-06       Impact factor: 3.490

5.  Preparation of poly(3-hydroxybutyrate-co-hydroxyvalerate) films from halophilic archaea and their potential use in drug delivery.

Authors:  Ozkan Danis; Ayse Ogan; Pınar Tatlican; Azade Attar; Emrah Cakmakci; Bulent Mertoglu; Meral Birbir
Journal:  Extremophiles       Date:  2015-02-08       Impact factor: 2.395

Review 6.  Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes).

Authors:  Dieter Jendrossek
Journal:  J Bacteriol       Date:  2009-03-06       Impact factor: 3.490

7.  Polyhydroxyalkanoate inclusion body-associated proteins and coding region in Bacillus megaterium.

Authors:  G J McCool; M C Cannon
Journal:  J Bacteriol       Date:  1999-01       Impact factor: 3.490

8.  Development of a transferable bimolecular fluorescence complementation system for the investigation of interactions between poly(3-hydroxybutyrate) granule-associated proteins in Gram-negative bacteria.

Authors:  Daniel Pfeiffer; Dieter Jendrossek
Journal:  Appl Environ Microbiol       Date:  2013-02-22       Impact factor: 4.792

9.  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.

Authors:  René Handrick; Simone Reinhardt; Philipp Kimmig; Dieter Jendrossek
Journal:  J Bacteriol       Date:  2004-11       Impact factor: 3.490

10.  PhaP is involved in the formation of a network on the surface of polyhydroxyalkanoate inclusions in Cupriavidus necator H16.

Authors:  Douglas Dennis; Vicki Sein; Edgar Martinez; Brian Augustine
Journal:  J Bacteriol       Date:  2007-11-02       Impact factor: 3.490

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