ArticleProtein expression and purification2001
Expression of a highly toxic protein, Bax, in Escherichia coli by attachment of a leader peptide derived from the GroES cochaperone.
Article in Protein expression and purification, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 22 citations in OpenAlex.
- Protective efficacy of the recombinantly expressed C-terminal domain ofJournal of veterinary research · 2025Article
- Heterologous Expression, Purification, and Characterization of a High-Temperature Requirement A (HtrA) Protease Homologue from Leptospira.Applied biochemistry and biotechnology · 2025Article
- Improved soluble expression of the gene encoding amylolytic enzyme Amo45 by fusion with the mobile-loop-region of co-chaperonin GroES inBiocatalysis and biotransformation · 2013Article
- High-throughput protein purification and quality assessment for crystallization.Methods (San Diego, Calif.) · 2011Review
- PSI:Biology-materials repository: a biologist's resource for protein expression plasmids.Journal of structural and functional genomics · 2011Article
- A family of LIC vectors for high-throughput cloning and purification of proteins.Methods in molecular biology (Clifton, N.J.) · 2009Article
- Bacterial expression strategies for human angiogenesis proteins.Journal of structural and functional genomics · 2006Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Expression of the human apoptosis modulator protein Bax in Escherichia coli is highly toxic, resulting in cell lysis at very low concentrations (Asoh, S., et al., J. Biol. Chem. 273, 11384-11391, 1998). Attempts to express a truncated form of murine Bax in the periplasm by using an expression vector that attached the OmpA signal sequence to the protein failed to alleviate this toxicity. In contrast, attachment of a peptide based on a portion of the E. coli cochaperone GroES reduced Bax's toxicity significantly and allowed good expression. The peptide, which was attached to the N-terminus, included the amino acid sequence of the mobile loop of GroES that has been demonstrated to interact with the chaperonin, GroEL. Under normal growth conditions, expression of this construct was still toxic, but generated a small amount of detectable recombinant Bax. However, when cells were grown in the presence of 2% ethanol, which stimulated overproduction of the molecular chaperones GroEL and DnaK, toxicity was reduced and good overexpression occurred. Two-dimensional gel electrophoresis analysis showed that approximately 15-fold more GroES-loop-Bax was produced under these conditions than under standard conditions and that GroEL and DnaK were elevated approximately 3-fold.
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