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.
Original language | English |
---|---|
Pages (from-to) | 1044-1048 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 586 |
Issue number | 7 |
DOIs | |
Publication status | Published - 2012 Apr 5 |
Keywords
- BL21(DE3)
- Chaperone-like protein
- Heat shock
- YrhB
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology