YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3)

Keum Young Ahn, Jin Seung Park, Kyung Yeon Han, Jong Am Song, Jeewon Lee

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish
Pages (from-to)1044-1048
Number of pages5
JournalFEBS Letters
Volume586
Issue number7
DOIs
Publication statusPublished - 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

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