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 journalArticlepeer-review

2 Citations (Scopus)


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
Issue number7
Publication statusPublished - 2012 Apr 5

Bibliographical note

Funding Information:
This study was supported by the National Research Laboratory Project (grant no. 2011-0020464 , the main project that supported this work), the Microbial Genomics and Applications Center at KRIBB (grant no. 2011-K000406 ), the Public Welfare & Safety research program (grant no. 2011-0021116 ), and the Basic Science Research Program (ERC program, grant no. 2011-0000874 ) of the National Research Foundation of Korea (NRF) grant funded by the Korea government. This work was also supported by Korea University and National Research Foundation of Korea (NRF) (grant no. 2011-0027538 ).


  • 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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