Overexpression of IbpB enhances production of soluble active Streptomyces olivaceovirdis XynB in Escherichia coli.
The small heat shock protein IbpB of Escherichia coli can accelerate protein disaggregation from inclusion body by Hsp100-Hsp70 re-activation system in vitro. It was therefore hypothesized that overexpression of IbpB might be able to promote protein disaggregation from inclusion body, by which more soluble recombinant proteins would be obtained. The overexpression of IbpB actually enhanced production of more active soluble XynB of Streptomyces olivaceovirdis in E. coli BL21(DE3). Surprisingly, the disaggregation of XynB from inclusion body was not accelerated. It seemed that the overexpressed IbpB protected improperly or partially folded XynB from aggregation and mediated the subsequent refolding. These results show potential of improving production of active heterologous proteins in E. coli.
Su
Xiaoyun
X
Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Zhang
Shan
S
Wang
Li
L
Dong
Zhiyang
Z
D043364:Endo-1,4-beta Xylanases / Q000096:biosynthesis* / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000096:biosynthesis* / Q000235:genetics; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000235:genetics; D002479:Inclusion Bodies / Q000201:enzymology*; D012995:Solubility; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D001617:beta-Glucosidase / Q000096:biosynthesis* / Q000235:genetics
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; C097579:IbpB protein, E coli; D001617:beta-Glucosidase; D043364:Endo-1,4-beta Xylanases; C090001:XynB xylanase