Abstract
In response to advances in proteomics research and the use of proteins in medical and biotechnological applications, recombinant protein production and the design of specific protein characteristics and functions has become a widely used technology. In this context, protein fusion tags have been developed as indispensable tools for protein expression, purification, and the design of functionalized surfaces or artificially bifunctional proteins. Here we summarize how positively or negatively charged polyionic fusion peptides with or without an additional cysteine can be used as protein tags for protein expression and purification, for matrix-assisted refolding of aggregated protein, and for coupling of proteins either to technologically relevant matrices or to other proteins. In this context we used cysteine-containing polyionic fusion peptides for the design of immunotoxins. In general, polyionic fusion tags can be considered as a multifunctional module in protein technology.
This work was supported by the Deutsche Forschungsgemeinschaft (DFG) as part of the Sonderforschungsbereich SFB 610. We thank Gary Sawers for critically reading the manuscript.
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©2013 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: Protein states with cell biological and medicinal relevance
- HIGHLIGHT: PROTEIN STATES WITH CELL BIOLOGICAL AND MEDICAL RELEVANCE
- Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors
- Progress in demystification of adhesion G protein-coupled receptors
- The unresolved puzzle why alanine extensions cause disease
- Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
- Structure and allosteric regulation of eukaryotic 6-phosphofructokinases
- Polyionic and cysteine-containing fusion peptides as versatile protein tags
- p0071/PKP4, a multifunctional protein coordinating cell adhesion with cytoskeletal organization
- Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin
- Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why
- Oxidative in vitro folding of a cysteine deficient variant of the G protein-coupled neuropeptide Y receptor type 2 improves stability at high concentration
- Identification of prolyl oligopeptidase as a cyclosporine-sensitive protease by screening of mouse liver extracts
- In vitro maturation of Drosophila melanogaster Spätzle protein with refolded Easter reveals a novel cleavage site within the prodomain
- Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains
- High level expression of the Drosophila Toll receptor ectodomain and crystallization of its complex with the morphogen Spätzle
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: Protein states with cell biological and medicinal relevance
- HIGHLIGHT: PROTEIN STATES WITH CELL BIOLOGICAL AND MEDICAL RELEVANCE
- Towards improved receptor targeting: anterograde transport, internalization and postendocytic trafficking of neuropeptide Y receptors
- Progress in demystification of adhesion G protein-coupled receptors
- The unresolved puzzle why alanine extensions cause disease
- Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD
- Structure and allosteric regulation of eukaryotic 6-phosphofructokinases
- Polyionic and cysteine-containing fusion peptides as versatile protein tags
- p0071/PKP4, a multifunctional protein coordinating cell adhesion with cytoskeletal organization
- Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin
- Methylation of the nuclear poly(A)-binding protein by type I protein arginine methyltransferases – how and why
- Oxidative in vitro folding of a cysteine deficient variant of the G protein-coupled neuropeptide Y receptor type 2 improves stability at high concentration
- Identification of prolyl oligopeptidase as a cyclosporine-sensitive protease by screening of mouse liver extracts
- In vitro maturation of Drosophila melanogaster Spätzle protein with refolded Easter reveals a novel cleavage site within the prodomain
- Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains
- High level expression of the Drosophila Toll receptor ectodomain and crystallization of its complex with the morphogen Spätzle