---
pmid: '22569261'
title: YrhB is a highly stable small protein with unique chaperone-like activity in
  Escherichia coli BL21(DE3).
authors:
- Ahn KY
- Park JS
- Han KY
- Song JA
- Lee J
journal: FEBS Lett
year: '2012'
full_text_available: false
doi: 10.1016/j.febslet.2012.02.051
---

# YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3).
**Authors:** Ahn KY, Park JS, Han KY, Song JA, Lee J
**Journal:** FEBS Lett (2012)
**DOI:** [10.1016/j.febslet.2012.02.051](https://doi.org/10.1016/j.febslet.2012.02.051)

## Abstract

1. FEBS Lett. 2012 Apr 5;586(7):1044-8. doi: 10.1016/j.febslet.2012.02.051. Epub 
2012 Mar 8.

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

Ahn KY(1), Park JS, Han KY, Song JA, Lee J.

Author information:
(1)Department of Chemical and Biological Engineering, Korea University, 
Anam-Dong 5-1, Sungbuk-Gu, Seoul 136-713, Republic of Korea.

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.

Copyright © 2012 Federation of European Biochemical Societies. Published by 
Elsevier B.V. All rights reserved.

DOI: 10.1016/j.febslet.2012.02.051
PMID: 22569261 [Indexed for MEDLINE]