PMID:22569261

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Citation

Ahn, KY, Park, JS, Han, KY, Song, JA and Lee, J (2012) YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3). FEBS Lett. 586:1044-8

Abstract

Escherichia coli YrhB (10.6 kDa) from strain BL21(DE3) that is commonly used for protein overexpression is a stable chaperone-like protein and indispensable for supporting the growth of BL21(DE3) at 48 °C but not defined as conventional heat shock protein (HSP). YrhB effectively prevented heat-induced aggregation of ribonucleotide synthetase (PurK). Without ATP, YrhB alone promoted in vitro refolding of uridine phosphorylase (UDP) and protected thermal denaturation of the refolded UDP. As a cis-acting fusion partner, YrhB also significantly reduced inclusion body formation of nine aggregation-prone heterologous proteins in BL21(DE3). Unlike conventional small HSPs, YrhB remained monomer under heat shock condition.

Links

PubMed Online version:10.1016/j.febslet.2012.02.051

Keywords

Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carboxy-Lyases/chemistry; Carboxy-Lyases/metabolism; DNA-Directed RNA Polymerases/genetics; DNA-Directed RNA Polymerases/metabolism; Enzyme Stability; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Enzymologic; Heat-Shock Response; Hot Temperature; Inclusion Bodies; Kinetics; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Molecular Weight; Mutation; Promoter Regions, Genetic; Protein Denaturation; Protein Refolding; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Sigma Factor/genetics; Sigma Factor/metabolism; Uridine Phosphorylase/chemistry; Uridine Phosphorylase/metabolism

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