Dramatic effects of truncation and sub-cellular targeting on the accumulation of recombinant microbial cellulase in tobacco View Full Text


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Article Info

DATE

2001-09

AUTHORS

Thomas Ziegelhoffer, John A. Raasch, Sandra Austin-Phillips

ABSTRACT

The economical bioconversion of lignocellulosic biomass to ethanol is dependent on the availability of large quantities of inexpensive cellulase enzymes. One way to reduce the cost of such enzymes is to produce them in crop plants at high levels. In order to assess factors that limit recombinant cellulase expression in plants, we have introduced the gene encoding E1 endo-1,4-β-glucanase (cellulase) of Acidothermus cellulolyticus into tobacco (Nicotiana tabacum) plants. Both the holoenzyme (E1) and catalytic domain (E1cd) were targeted to three sub-cellular compartments; the cytosol, chloroplast and apoplast. Accumulation of both E1 and E1cd was greatest in the apoplast, with levels more than 100-fold higher than observed for cytosolic accumulation. In all three compartments, E1cd accumulated to higher levels than the full-length enzyme. By combining truncation and apoplastic localization, an increase in expression of more than 500-fold was achieved, compared to cytosolic full-length E1. This effect is primarily post-transcriptional, since E1cd mRNA levels are very similar despite the range of E1cd accumulation observed. Recombinant E1cd, expressed at up to 1.6% total soluble protein, is extremely stable in both crude leaf extracts and dried leaf material. More... »

PAGES

147-158

References to SciGraph publications

  • 1996-10. Optimizing expression of transgenes with an emphasis on post-transcriptional events in PLANT MOLECULAR BIOLOGY
  • 1999-08. Expression of bacterial cellulase genes in transgenic alfalfa (Medicago sativa L.), potato (Solanum tuberosum L.) and tobacco (Nicotiana tabacum L.) in MOLECULAR BREEDING
  • 1999-03. Expression of Trichoderma reesei exo-cellobiohydrolase I in transgenic tobacco leaves and calli in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • 2000-02. Accumulation of a thermostable endo-1,4-β-D-glucanase in the apoplast of Arabidopsis thaliana leaves in MOLECULAR BREEDING
  • 1985-05. Cellular location of peroxidase isoenzymes in leaf tissue of Petunia and their affinity for Concanavalin A-Sepharose in PLANTA
  • 1996-10. Molecular chaperones and protein folding in plants in PLANT MOLECULAR BIOLOGY
  • 1989-08. Ultra-Thermostable Cellulases From Acidothermus cellulolyticus: Comparison of Temperature Optima with Previously Reported Cellulases in NATURE BIOTECHNOLOGY
  • 1995-02. Production and field performance of transgenic alfalfa (Medicago sativa L.) expressing alpha-amylase and manganese-dependent lignin peroxidase in EUPHYTICA
  • 2000-02. Expression of Acidothermus cellulolyticus endoglucanase E1 in transgenic tobacco: biochemical characteristics and physiological effects in TRANSGENIC RESEARCH
  • 1993-12. Post-transcriptional regulation of nuclear-encoded genes in higher plants: the roles of mRNA stability and translation in PLANT MOLECULAR BIOLOGY
  • 2000-06. Improved plant-based production of E1 endoglucanase using potato: expression optimization and tissue targeting in MOLECULAR BREEDING
  • 1995-10. Mutations in the processing site of the precursor of ribulose-1,5-bisphosphate carboxylase/oxygenase small subunit: effects on import, processing, assembly and stability in PLANT MOLECULAR BIOLOGY
  • 1992-10. Arabidopsis thaliana small subunit leader and transit peptide enhance the expression ofBacillus thuringiensis proteins in transgenic plants in PLANT MOLECULAR BIOLOGY
  • 1998-09. Compartment-specific accumulation of recombinant immunoglobulins in plant cells: an essential tool for antibody production and immunomodulation of physiological functions and pathogen activity in PLANT MOLECULAR BIOLOGY
  • 1994-03. A new thermostable endoglucanase,Acidothermus cellulolyticus E1 in APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • Journal

    TITLE

    Molecular Breeding

    ISSUE

    2

    VOLUME

    8

    Author Affiliations

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1023/a:1013338312948

    DOI

    http://dx.doi.org/10.1023/a:1013338312948

    DIMENSIONS

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    37 schema:description The economical bioconversion of lignocellulosic biomass to ethanol is dependent on the availability of large quantities of inexpensive cellulase enzymes. One way to reduce the cost of such enzymes is to produce them in crop plants at high levels. In order to assess factors that limit recombinant cellulase expression in plants, we have introduced the gene encoding E1 endo-1,4-β-glucanase (cellulase) of Acidothermus cellulolyticus into tobacco (Nicotiana tabacum) plants. Both the holoenzyme (E1) and catalytic domain (E1cd) were targeted to three sub-cellular compartments; the cytosol, chloroplast and apoplast. Accumulation of both E1 and E1cd was greatest in the apoplast, with levels more than 100-fold higher than observed for cytosolic accumulation. In all three compartments, E1cd accumulated to higher levels than the full-length enzyme. By combining truncation and apoplastic localization, an increase in expression of more than 500-fold was achieved, compared to cytosolic full-length E1. This effect is primarily post-transcriptional, since E1cd mRNA levels are very similar despite the range of E1cd accumulation observed. Recombinant E1cd, expressed at up to 1.6% total soluble protein, is extremely stable in both crude leaf extracts and dried leaf material.
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