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YrhB is a highly stable small protein with unique chaperone‐like activity in Escherichia coli BL21(DE3)
Author(s) -
Ahn Keum-Young,
Park Jin-Seung,
Han Kyung-Yeon,
Song Jong-Am,
Lee Jeewon
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.02.051
Subject(s) - escherichia coli , chaperone (clinical) , heat shock protein , heterologous , biochemistry , protein aggregation , chemistry , inclusion bodies , hsp70 , fusion protein , recombinant dna , biology , medicine , pathology , gene
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.