Literature DB >> 11004196

Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.

R Handrick1, S Reinhardt, D Jendrossek.   

Abstract

Ralstonia eutropha H16 degraded (mobilized) previously accumulated poly(3-hydroxybutyrate) (PHB) in the absence of an exogenous carbon source and used the degradation products for growth and survival. Isolated native PHB granules of mobilized R. eutropha cells released 3-hydroxybutyrate (3HB) at a threefold higher rate than did control granules of nonmobilized bacteria. No 3HB was released by native PHB granules of recombinant Escherichia coli expressing the PHB biosynthetic genes. Native PHB granules isolated from chromosomal knockout mutants of an intracellular PHB (i-PHB) depolymerase gene of R. eutropha H16 and HF210 showed a reduced but not completely eliminated activity of 3HB release and indicated the presence of i-PHB depolymerase isoenzymes.

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Year:  2000        PMID： 11004196      PMCID： PMC94719          DOI： 10.1128/JB.182.20.5916-5918.2000

Source DB:  PubMed          Journal:  J Bacteriol        ISSN： 0021-9193            Impact factor:   3.490


  12 in total

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  33 in total

1.  Poly(3-hydroxybutyrate) (PHB) depolymerase PhaZa1 is involved in mobilization of accumulated PHB in Ralstonia eutropha H16.

Authors:  Keiichi Uchino; Terumi Saito; Dieter Jendrossek
Journal:  Appl Environ Microbiol       Date:  2007-12-21       Impact factor: 4.792

Review 2.  Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes).

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

3.  Comparative proteome analysis reveals four novel polyhydroxybutyrate (PHB) granule-associated proteins in Ralstonia eutropha H16.

Authors:  Anna Sznajder; Daniel Pfeiffer; Dieter Jendrossek
Journal:  Appl Environ Microbiol       Date:  2014-12-29       Impact factor: 4.792

4.  Poly-3-hydroxybutyrate metabolism in the type II methanotroph Methylocystis parvus OBBP.

Authors:  Allison J Pieja; Eric R Sundstrom; Craig S Criddle
Journal:  Appl Environ Microbiol       Date:  2011-07-01       Impact factor: 4.792

5.  3-Hydroxybutyrate Derived from Poly-3-Hydroxybutyrate Mobilization Alleviates Protein Aggregation in Heat-Stressed Herbaspirillum seropedicae SmR1.

Authors:  Luis Paulo Silveira Alves; Arquimedes Paixão Santana-Filho; Guilherme Lanzi Sassaki; Fabio de Oliveira Pedrosa; Emanuel Maltempi de Souza; Leda Satie Chubatsu; Marcelo Müller-Santos
Journal:  Appl Environ Microbiol       Date:  2020-08-18       Impact factor: 4.792

6.  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

7.  Photoautotrophic Polyhydroxybutyrate Granule Formation Is Regulated by Cyanobacterial Phasin PhaP in Synechocystis sp. Strain PCC 6803.

Authors:  Waldemar Hauf; Björn Watzer; Nora Roos; Alexander Klotz; Karl Forchhammer
Journal:  Appl Environ Microbiol       Date:  2015-04-24       Impact factor: 4.792

8.  PhaM is the physiological activator of poly(3-hydroxybutyrate) (PHB) synthase (PhaC1) in Ralstonia eutropha.

Authors:  Daniel Pfeiffer; Dieter Jendrossek
Journal:  Appl Environ Microbiol       Date:  2013-11-08       Impact factor: 4.792

9.  Unraveling the function of the Rhodospirillum rubrum activator of polyhydroxybutyrate (PHB) degradation: the activator is a PHB-granule-bound protein (phasin).

Authors:  Rene Handrick; Simone Reinhardt; Daniel Schultheiss; Thomas Reichart; Dirk Schüler; Verena Jendrossek; Dieter Jendrossek
Journal:  J Bacteriol       Date:  2004-04       Impact factor: 3.490

10.  Purification and properties of an intracellular 3-hydroxybutyrate-oligomer hydrolase (PhaZ2) in Ralstonia eutropha H16 and its identification as a novel intracellular poly(3-hydroxybutyrate) depolymerase.

Authors:  Teruyuki Kobayashi; Mari Shiraki; Tomoko Abe; Akinori Sugiyama; Terumi Saito
Journal:  J Bacteriol       Date:  2003-06       Impact factor: 3.490
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