Investigating the function of GroES with hard-to-fold proteins in vivo
2019
Hild Walett, Oliver | Berlin, Emmanuel | Larsson, Johan | Arvidsson, Sofie | Fors, Filip | Gavelius, Marianne | Genander, Filip | Granqvist, Johanna | Lifwergren, Philip | Sandéhn, Alexandra | Viksten, Martin | Wenhov, Irma
The use of molecular chaperones can increase the yield of correctly folded proteins. This is especially needed in the expression of proteins non-native to the host organism. This study set out to investigate the function of the chaperone GroES; a component in the GroE-system. The function of this chaperone has only been studied alone in vitro. Here we lay ground to further studies on GroES and its ability to act alone in vivo. GroES was expressed from a plasmid and characterized through its potential to increase the amount of correctly folded proteins. Characterization was mainly done by fluorescence spectroscopy with hard-to-fold proteins linked to fluorescent probes. Results show a very clear increase in fluorescence for most of the substrate proteins tested, indicating that GroES has a significant role in the GroE-system and perhaps outside of it.
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Эту запись предоставил Linköping University