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Design of a Single-chain Multi-enzyme Fusion Protein Establishing the Polyhydroxybutyrate Biosynthesis Pathway by Jane A. Mullaney; Bernd H.A. Rehm is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Polyhydroxyalkanoates are biodegradable biocompatible polymers naturally produced by various bacteria and archaea. Biotechnological production in transgenic plants has already been demonstrated with efficient polyhydroxybutyrate production requiring targeting of the enzymes to the chloroplasts. Three enzymes are required to establish the polyhydroxybutyrate biosynthesis pathway in non-naturally producing microorganisms or plants. To facilitate production of biopolyesters in plants, a gene encoding a translational fusion of the polyhydroxybutyrate biosynthesis enzymes PhaA (␤-ketothiolase), PhaB (acetoacetyl-CoA reductase) and PhaC (PHA synthase) was constructed. Escherichia coli harboring a plasmid encoding this fusion protein (PhaA-PhaB-PhaC) under control of the lac promoter accumulated polyhydroxybutyrate contributing to 0.4% (w/w) of cellular dry weight. Insertion of an extended linker between PhaA and PhaB increased polyhydroxybutyrate accumulation to 3.9% (w/w) of cellular dry weight. Introduction of a second plasmid encoding PhaA and PhaB restored polyhydroxybutyrate accumulation to wildtype levels of about 35% (w/w) of cellular dry weight suggesting that the functions of Ph

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Author

Jane A. Mullaney; Bernd H.A. Rehm

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0168-1656)

Published

2010

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)