Literature DB >> 1476771

Biological complexes of poly-beta-hydroxybutyrate.

R N Reusch1.   

Abstract

Short-chain complexed poly-beta-hydroxybutyrate, 130-170 monomer units, is a ubiquitous constituent of cells, wherein it is usually associated with other macromolecules by multiple coordinate bonds, or by hydrogen bonding and hydrophobic interactions. This conserved PHB has been isolated from the plasma membranes of bacteria, from a variety of plant tissues, and from the plasma membranes, mitochondria, and microsomes of animal cells. In bacterial membranes, PHB has been found complexed to the calcium salts of inorganic polyphosphates, and to single-stranded DNAs. The ability of PHB to solvate salts, consisting of cations having high solvation energies and large delocalized anions, is in accordance with its molecular characteristics, that of a flexible linear molecule possessing a large number of electron-donating ester oxygens suitably spaced to replace the hydration shell of cations. In turn, PHB may be rendered soluble in aqueous media by complexation to water-soluble proteins, such as serum lipoproteins and albumin. Such solvates are highly resistant to hydrolytic enzymes. These findings suggest that the physiological roles of this unique biopolymer may include the solvation of salts of polymeric anions to facilitate their movement through hydrophobic barriers, and the protection of cellular polymers from enzymatic degradation.

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Year:  1992        PMID: 1476771     DOI: 10.1111/j.1574-6968.1992.tb05829.x

Source DB:  PubMed          Journal:  FEMS Microbiol Rev        ISSN: 0168-6445            Impact factor:   16.408


  11 in total

1.  Haemophilus influenzae outer membrane protein P5 is associated with inorganic polyphosphate and polyhydroxybutyrate.

Authors:  E Zakharian; R N Reusch
Journal:  Biophys J       Date:  2006-10-20       Impact factor: 4.033

Review 2.  Translocation of DNA across bacterial membranes.

Authors:  B Dreiseikelmann
Journal:  Microbiol Rev       Date:  1994-09

3.  Resolving the native conformation of Escherichia coli OmpA.

Authors:  Alexander Negoda; Elena Negoda; Rosetta N Reusch
Journal:  FEBS J       Date:  2010-11       Impact factor: 5.542

4.  High rate of N2 fixation by East Siberian cryophilic soil bacteria as determined by measuring acetylene reduction in nitrogen-poor medium solidified with gellan gum.

Authors:  Shintaro Hara; Yasuyuki Hashidoko; Roman V Desyatkin; Ryusuke Hatano; Satoshi Tahara
Journal:  Appl Environ Microbiol       Date:  2009-03-13       Impact factor: 4.792

5.  Poly-3-hydroxybutyrate in Legionella pneumophila, an energy source for survival in low-nutrient environments.

Authors:  B W James; W S Mauchline; P J Dennis; C W Keevil; R Wait
Journal:  Appl Environ Microbiol       Date:  1999-02       Impact factor: 4.792

6.  Poly-3-hydroxybutyrate synthase from the periplasm of Escherichia coli.

Authors:  Dongsheng Dai; Rosetta N Reusch
Journal:  Biochem Biophys Res Commun       Date:  2008-07-18       Impact factor: 3.575

7.  Recovery and characterization of poly(3-hydroxybutyric acid) synthesized in Alcaligenes eutrophus and recombinant Escherichia coli.

Authors:  S K Hahn; Y K Chang; S Y Lee
Journal:  Appl Environ Microbiol       Date:  1995-01       Impact factor: 4.792

8.  Poly-3-hydroxybutyrate/polyphosphate complexes form voltage-activated Ca2+ channels in the plasma membranes of Escherichia coli.

Authors:  R N Reusch; R Huang; L L Bramble
Journal:  Biophys J       Date:  1995-09       Impact factor: 4.033

Review 9.  The role of short-chain conjugated poly-(R)-3-hydroxybutyrate (cPHB) in protein folding.

Authors:  Rosetta N Reusch
Journal:  Int J Mol Sci       Date:  2013-05-23       Impact factor: 5.923

10.  Potentiation of the cytotoxic activity of copper by polyphosphate on biofilm-producing bacteria: a bioinspired approach.

Authors:  Werner E G Müller; Xiaohong Wang; Yue-Wei Guo; Heinz C Schröder
Journal:  Mar Drugs       Date:  2012-10-25       Impact factor: 5.118

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