Induced fit of passenger proteins fused to Archaea maltose binding proteins

Biochemical and Biophysical Research Communications
He HuangArio de Marco

Abstract

Maltose binding proteins (MBPs) are used as carriers for improving the solubility of passenger proteins. Our results indicate that the higher solubility of the fusions correlates with their elevated heat stability. Fusions of the otherwise thermo-sensitive GFP with MBPs from Archaea, but not GST-GFP and Escherichia coli MBP-GFP, maintained their fluorescence and structure after 10min incubation at 100 degrees C and could be purified by heating the bacteria lysate, with yields even higher than those obtained using metal affinity chromatography. Furthermore, only correctly folded proteins could stand the heating treatment and, therefore, the heat-purification method can be used as a quality control step to select homogeneous monodispersed material whereas soluble aggregates are removed by precipitation.

References

Aug 19, 1999·Protein Science : a Publication of the Protein Society·R B Kapust, D S Waugh
Dec 24, 2003·Proceedings of the National Academy of Sciences of the United States of America·Manuela López de la Paz, Luis Serrano
Jan 9, 2004·Journal of Biotechnology·Ario de MarcoArie Geerlof
Aug 10, 2004·Nature Biotechnology·Laurent JespersGreg Winter
Dec 21, 2004·Journal of Biotechnology·Hans Peter Sørensen, Kim Kusk Mortensen
Mar 24, 2005·Journal of Molecular Biology·Mar CarrióSalvador Ventura
Jun 1, 2005·Trends in Biotechnology·David S Waugh
Sep 20, 2005·Protein Expression and Purification·Sreedevi Nallamsetty, David S Waugh

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Citations

Aug 22, 2007·Reproduction : the Official Journal of the Society for the Study of Fertility·Jirí KalinaPavel Trefil
Jan 20, 2017·Protein Engineering, Design & Selection : PEDS·Vandan ShahJin Ryoun Kim
Sep 24, 2015·Chembiochem : a European Journal of Chemical Biology·Brennal PierreJin Ryoun Kim

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