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

Authors
Ahn, Keum-YoungPark, Jin-SeungHan, Kyung-YeonSong, Jong-AmLee, Jeewon
Issue Date
5-4월-2012
Publisher
WILEY
Keywords
YrhB; BL21(DE3); Chaperone-like protein; Heat shock
Citation
FEBS LETTERS, v.586, no.7, pp.1044 - 1048
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
586
Number
7
Start Page
1044
End Page
1048
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/108738
DOI
10.1016/j.febslet.2012.02.051
ISSN
0014-5793
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 degrees 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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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