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An Intrinsically Disordered Peptide Tag that Confers an Unusual Solubility to Aggregation-Prone Proteins

Byung Hoon Jo

2022Applied and Environmental Microbiology33 citationsDOIOpen Access PDF

Abstract

Production of recombinant proteins in Escherichia coli still suffers from the insolubility problem. Conventional solubility enhancers with large sizes, represented by maltose-binding protein (MBP), have remained the first-choice tags; however, the success of the soluble expression of tagged proteins is largely unpredictable. In addition, the large tags can negatively affect the function of target proteins. In this work, the NEXT tag, an intrinsically disordered peptide, was introduced as a small but powerful alternative to MBP. The NEXT tag could significantly improve both the expression level and the solubility of target proteins, including a thermostable carbonic anhydrase and a polyethylene terephthalate (PET)-degrading enzyme that are remarkable enzymes for environmental bioremediation.

Topics & Concepts

Maltose-binding proteinEscherichia coliSolubilityRecombinant DNAPeptideBiochemistryEscherichia coli ProteinsChemistryEnhancerMaltoseBiologyBiophysicsGene expressionGeneFusion proteinEnzymeOrganic chemistryProtein purification and stabilityMonoclonal and Polyclonal Antibodies ResearchViral Infectious Diseases and Gene Expression in Insects