Over-expression and characterization of the recombinant small heat shock protein from Pyrococcus furiosus.
The gene encoding a small heat shock protein (sHSP) from Pyrococcus furiosus was redesigned and chemically synthesized by using bacteria-preferred codons. The gene product was over-expressed in Escherichia coli BL21(DE)(3) and purified to homogeneity. In the presence of this protein, the activities of Taq DNA polymerase, DNA restriction endonuclease HindIII and lysozyme were protected at elevated temperature, and also, thermal aggregation of lysozyme was prevented by this purified recombinant sHSP.
Chen
Huayou
H
Shanghai Institutes for Biological Sciences, Chinese Academy of Science, Shanghai, China.
Chu
Zhongmei
Z
Zhang
Yi
Y
Yang
Shengli
S
D004789:Enzyme Activation; D004795:Enzyme Stability; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D050888:Heat-Shock Proteins, Small / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D020027:Pyrococcus furiosus / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D015854:Up-Regulation / Q000235:genetics
D050888:Heat-Shock Proteins, Small; D011994:Recombinant Proteins