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Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1007/BF00042362
AuthorSearch for: 1; Search for: 1; Search for: 1
Affiliation
  1. National Research Council of Canada. NRC Plant Biotechnology Institute
FormatText, Article
Subjectmolecular chaperone; heterologous gene expression; protein folding
Abstract
It has been suggested that lack of specialized molecular chaperone function(s) in Escherichia coli may account for the fact that although E. coli cells transformed with plant Rubisco genes synthesize the Rubisco subunit polypeptides, the active enzyme fails to assemble. If so, co-expression of plant chaperone and Rubisco genes might permit plant Rubisco assembly in E. coli. Introduction of genes encoding plant chaperonin polypeptides has been shown to enhance the capacity of E. coli to assemble active cyanobacterial Rubisco. We now report that co-expression of plant Rubisco and chaperonin genes affected the solubility and stability of Rubisco large subunit polypeptides, however, neither the assembled oligomeric protein nor Rubisco enzyme activity was detected.
Publication date
PublisherSpringer Nature
In
  • Plant Molecular Biology 23, no. 6 (December 1993): 1285–1290.
LanguageEnglish
Peer reviewedYes
IdentifierBF00042362
NRCC-37341
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Record identifieraac06bc3-37d6-4dad-b262-706375c65d59
Record created2023-11-06
Record modified2023-11-06
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